2018 年 27 巻 2 号（通巻 83 号）

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第26回学術集会ベストイメージング賞・浜ホト賞受賞

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「BAC-GLT-1-G-CaMP7 #817系統 (G7NG817)遺伝子改変マウスによる経頭蓋マクロイメージング」

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ƺƹƻƬƿǂǉƬƯƬƿƬƻǍǃǆƵƥƦƶƯƵ Ğĩƥ ƧƿƵǄƿƶƯƵƨźj©cɕȨȹȌȝȠƥĥƔłɕȯɠȧɘɣȸɡȰƩƥƥ
Ù1ƥ  Ưƫưǩw ƥ Ɖ ưǩ|ìƥ ı ưƥƯ
ǲŀȎÛijelƥ ÷lŻùñlđǩư ÷lČĖƥ ĶďĥđlČĖȻɡȽɣƥE-mail: monai.hiromu@ocha.ac.jpĶȣÎǾȠŌġȉǼȇďĥĢĳƥ ƧɇɛɣɠɡƨȉŇěȏȝǶĊȞȡȇǯȠǴǩnȏȌȰɝȦĢĳȉPȐȡȠĶĢĳǴ
ǮȠǪȰɝȦĢĳȎĕȈǮȠȦȹɄɠȵȧɄȏĶ1ȈǩɇɛɣɠɡȉŇěȎȧɡȽɣɎȩɣȹȉǼȇ&ǯȇǲȟǩĶ1øbȎī țǩɇɛɣɠɡȓȎÉƚ ĨȋȊȵɔɣɄăȋ;ȣÅȂǼȇǯȠǪȖȂŬ}ǩȦȹɄɠȵȧɄǴǩòȌùĶȌǲǯȇǩȷɆɐȹFaȣŚĜǼȇǯȠ$œǴǯǶȆȚōȆǳȅȇǵȇǯȠǪƥƥ ȦȹɄɠȵȧɄȏǩɇɛɣɠɡȉÿȋȟß@ƌȣāùǼȋǯǪȁȎȂșǩÀȎƌÚù÷lăçmÝȈȏǩȁȎß@ǴōůǻȡȇǵȂFĴǴǮȠǪ¯ǩȦȹɄɠȵȧɄȏǩß@ȌǽȇĢĳ1 ƻǍưƪëȣeǵǶc@ǻȀȠǹȉǴ_NǻȡȇǯȠǪȦȹɄɠȵȧɄȎ ƻǍưƪ²ȏǩȦȻȿɞȳɝɡțɈɞȦɅɟɆɝɡȋȊȎďĥ!ƙñŞȌȝȅȇŗšǻȡǩƄµƆɢ~ĝXȌæȅȇďĥß@ȎŚĜȣňȋȅȇǯȠFĴǴǮȠǪƥƥ ǫȏǩùĶȌǲǯȇȦȹɄɠȵȧɄȎ ƻǍưƪ²ȣǩ~ĝXɢƄºƆȌæȅȇFŎAǾȠȂșȌǩĢĳ1 ƻǍưƪëȌĚǼȇņ+ȣāǾȠȽɡɊȯŞƥ ƧƿƬƻǍǃǆƵƨȣȰɞȽɖɡŽɄɜɡȹɔɣȽɣƯƥƧƿǂǉƬƯƨȎàȌāöǻȀȠǹȉȣŔȗ
ȂǪŔňƂŘȎĦÅǩƶƯƵ ĞĩȌǲǯȇ ƿƬƻǍǃǆƵ ȎǯāöȣȂǴǩȦȹɄɠȵȧɄȎȗȋȞǿŻȎĻhɇɛɣɠɡȌȚÿăȋāöǴŖșȞȡȂƥ ƧƺƹƻƬƿǂǉƬƯƬƿƬƻǍǃǆƵƥƦƶƯƵ Ğĩźj©cɕȨȹƫƥǇǀǁƽǄƥƺǕǙǇǑǜǙǞǛǏǑƥƻǑǘǝǑǛ
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³ȞǳȉȋȅȂƥ ƧĥƔłɕȯɠȧɘɣȸɡȰƨǪǫȏǹȎɕȨȹȣ ƿƵǄƿƶƯƵ ɕȨȹȉKǷȂǪƿƵǄƿƶƯƵ ɕȨȹȏǩƔłƞţǼȌĶȎß@ǴōǱȠǹȉǳȞǩĶÒĴɕɀɍɡȰȌ¹?ȈǮȠǪǱȐǩɋȲ¼¼ȌpǾȠɉɟɞąŞȎɇɛɣɠɡß@ȋȊƟµƆɢƟėƆ4ŒĴȈFŎAǾȠǹȉǴȈǵȠǪȖȂǩtȣȆȍȠ8êȌpǼȇȏǩȦȹɄɠȵȧɄüÀȎȜȅǶȟȉǼȂƍ{Ȍ³Ƞǯ ƻǍưƪ²ǴeĶąŞ-]ȈJºǼȇùǽȠǹȉǴ4ǳȅȂǪǹȎ¯ÝȣúǯȇǩǹȡȖȈ
ǫȏǩĥƔłćàƌÚ8êÝƥ ƧǝƼƻǈƨȌȝȅȇŗqǻȡȠȷɆɐȹFaȌȦȹɄɠȵȧɄȎ ƻǍưƪ²ǴžŌȋ;ȣÅȂǼȇǯȠǹȉȣ_NǼȇǵȂƥ ƧǃǙǘǍǕƥǑǝƥǍǖƭƫƥǄǍǝƭƥƻǙǗǗǞǘƭƥƵƸƯƯƯƮƮƥƧưƮƯƴƨƥƨǪƥƥ(A) ɕȨȹZmĶȌǲǷȠņ+ȎāöɊȽɣɡȎĉóƎ (zHȌ4ǷȠƎ) Ȏ­ƎYɪ ØŨúȎſù\ (C57BL/6)ɕȨȹĶǪɪ ŋǼȂ G7NG817 ɕȨȹĶǪeĶąŞȉâƛȎŻȌǯ GCaMP7 ȎāöǴȗȞȡȠǪǹȎǯāöȎȂșȌǩņ+cAȣƔłƞţǼȌçmǾȠǹȉǴȈǵȠǪ
(B-D) ĥƔłɕȯɠȧɘɣȸɡȰȌȝȠäǯƢżȎ G7NG817 ɕȨȹȌǲǷȠĹāăȋ Ca2+¢@ȎFŎAŎŏſ (B ȎƤǯUő1)ȌǲǷȠņ+ŪcAõ (ΔF/F)ȣ (C)ȌɐɠɀɄǼȂǪ¢@ȎOÞ«ȏǲȝȁ 0.5 ǳȞ 2
Hz ȈǮȟǩǹȡȏƢżȎǸȅÕƗȈçmǻȡȠuƌ`ƌ (LFP)ȎÞȌpǾȠȚȎȈǮȠǪý'ȏĒǮȂȟ 10 ÄEǼȂǪ(D)Ȉȏǩ(C)ȌǲǷȠíĭŻȣeǼȇŊčǼȂǪȑǼȈčǻȡȂµƆȌpǾȠý'ȣ (B)ȈŊčǼȂǪ
(E-G) G7NG81 ɕȨȹȎĥƔłȧɘɣȸɡȰȌȝȠeĶąŞȬɞȷȨɗ@ȎÒĴɕɀɍɡȰ(E) ƢżȣǳǷȂóȈǩ5 ĒƆȌ 50 VǿȆɋȲ 1 ¼ 1 ¼ȣ8êǼȂǪȁȎȉǵȎɉɟɞſ (zý'ȎƣľÆ1)Ȍ
ǲǷȠȬɞȷȨɗĚȎņ+ŪȎcAõȣǩĀȬɜɣŊčǼžȍȇŊčǼȂ (fý')ǪǹȡȏǩHYȌčǾ°ĊȎɉɟɞąŞȎɋȲ-ɉɟɞſȎpȉĺǼȇǯȠǪȹȱɣɞɉɣȏzý'Ǵ 1mmǩfý'Ǵ 250 ɕȧȯɠɘɣɄɞ (µmǩ1µm ȏ 1000 4Ȏ 1mm)Ǫ
(F) ĆǴŏșȇǯȠóȈǩ10 ɖɝĒȎ LED Ɏɜɀȷɛ8êȣzĆȌǱȂǪȁȎȉǵȎŎŏąŞȎȬɞȷȨɗ
ĚȎņ+ŪȎcAõȣĀȬɜɣȈŊčǼȂǪĚȏǩ1 Ēȉǯǰƍ{ȌċǯȚȎȈǮȅȂǪ(G) ƢżȣǳǷȂóȈȎɂɣɞɍɡȿ8êȌpǾȠĚǪÖȏǩĥƔłȧɘɣȸɡȰȌȝȠĦÅǪB ȎŎŏ8êȉØŨǼȇĠ 10 #Ĕņ+ŪȎcAõǴeǵǶǩµƆȚ 20 ĒƆĔĪǶǩȜȅǶȟǼȂȚȎȈǮȅȂǪÖȏǩŏſ (ÖzĘȎƤľÆ1)ȎŻȌǲǯȇǩ +jƖƃȣúǯȂŕǼǯŐoȎĦÅ (ȂȃǼǩÖȉȏÿȋ
Ƞ")ǪÖȉJÏȎµƆĥŶȣȂȊȠĂǶ³ȠǯĢĳȏǩɬȦȹɄɠȵȧɄɭȈǮȅȂǪŎſȎeǵǻȏūǴ
400µm ĔǪ― 11 ―

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27― 13 ―‫ ➨ ڦ‬27 ᅇ᪥ᮏࣂ࢖࢜࢖࣓࣮ࢪࣥࢢᏛ఍Ꮫ⾡㞟఍‫ڦ‬୺ദ㸸᪥ᮏࣂ࢖࢜࢖࣓࣮ࢪࣥࢢᏛ఍
ඹദ㸸ᅜ❧◊✲㛤Ⓨἲே⏘ᴗᢏ⾡⥲ྜ◊✲ᡤඹദ㸸⛉Ꮫ◊✲㈝⿵ຓ㔠 ᪂Ꮫ⾡㡿ᇦ◊✲ࠕ⣽⬊ᶵ⬟ࢆྖࡿ࢜ࣝ࢞ࢿ࣭ࣛࢰ࣮ࣥࡢゎㄞࠖ఍ᮇ㸸ᖹᡂ 26 ᖺ 9 ᭶ 2 ᪥㸦᪥㸧㹼 9 ᭶ 4 ᪥㸦ⅆ㸧   ◆බ㛤ㅮᗙ㸸9 ᭶ 2 ᪥㸦᪥㸧12:00 㹼 18:30㸦ཷ௜ 11:30~㸧
◆Ꮫ⾡ㅮ₇఍㸸9 ᭶ 3 ᪥㸦᭶㸧8:50㸦ཷ௜ 8:00~㸧㹼 9 ᭶ 4 ᪥㸦ⅆ㸧18:20
఍ሙ㸸⏘ᴗᢏ⾡⥲ྜ◊✲ᡤࡘࡃࡤࢭࣥࢱ࣮ ඹ⏝ㅮᇽ㸦Ⲉᇛ┴ࡘࡃࡤᕷᮾ 1-1-1㸧
  㸦https://www.aist.go.jp/aist_j/guidemap/tsukuba/center/tsukuba_map_c.html ࢆཧ↷㸧኱఍㛗㸸ຍ⸨ ⸅㸦⏘ᴗᢏ⾡⥲ྜ◊✲ᡤ ࣂ࢖࣓࢜ࢹ࢕࢝ࣝ◊✲㒊㛛ࠊ        ᪂Ꮫ⾡㡿ᇦ◊✲ࠕ⣽⬊ᶵ⬟ࢆྖࡿ࢜ࣝ࢞ࢿ࣭ࣛࢰ࣮ࣥࡢゎㄞࠖィ⏬⌜ဨ㸧Ꮫ⾡㞟఍࣮࣒࣮࣍࣌ࢪ㸸http://j-bioimaging.org/bioimaging2018/
ཧຍ㈝㸸බ㛤ㅮᗙ㸦↓ᩱ㸧Ꮫ⾡㞟఍୍⯡㸦఍ဨ࣭༠㈶Ꮫ఍ဨ㸸6,000 ෇ࠊ㠀఍ဨ㸸8,000 ෇㸧኱Ꮫ㝔⏕㸦఍ဨ㸸2,000 ෇ࠊ㠀఍ဨ㸸3,000 ෇㸧Ꮫ㒊Ꮫ⏕ ↓ᩱ㸦Ⓨ⾲ࡍࡿሙྜࡣ኱Ꮫ㝔⏕࡟‽ࡎࡿ㸧༠㈶Ꮫ఍㸦஬༑㡢㡰㸧ᛂ⏝≀⌮Ꮫ఍ྍど໬᝟ሗᏛ఍

᪥ᮏ໬Ꮫ఍᪥ᮏ㢧ᚤ㙾Ꮫ఍

໬ᏛᕤᏛ఍᪥ᮏ☢Ẽඹ㬆་Ꮫ఍᪥ᮏ⣽⬊⏕≀Ꮫ఍᪥ᮏ⏕⌮Ꮫ఍

᪥ᮏ⚄⤒໬Ꮫ఍
᪥ᮏ⤌⧊⣽⬊໬Ꮫ఍᪥ᮏ⏕≀≀⌮Ꮫ఍᪥ᮏ㎰ⱁ໬Ꮫ఍

᪥ᮏ≀⌮Ꮫ఍
᪥ᮏศᯒ໬Ꮫ఍

᪥ᮏศගᏛ఍
᪥ᮏච␿Ꮫ఍

᪥ᮏศᏊ⏕≀Ꮫ఍᪥ᮏ⸆Ꮫ఍᪥ᮏ⸆⌮Ꮫ఍

᪥ᮏ⺮ⓑ㉁⛉Ꮫ఍᪥ᮏศᏊ࢖࣓࣮ࢪࣥࢢᏛ఍

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ќ 27 ǎ̵̊¾Ïß¨Ü◆̵̊¾Ïß¨ÜȚĕȚԄ‫׊‬ĕ։Ǌȑƾĕ



Țĕ

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P37. In Vivo Temperature Imaging for Deeper Abdominal Region of Mice Using 
Ratiometric Over-1000 nm Near-Infrared Fluorescent Rare-Earth-Doped NaYF4
Nanothermometer 
HShota Sekiyama1, Masakazu Umezawa1,2 , Shuhei Kuraoka1, Takuji Ube1, Masao 
Kamimura1,2, and Kohei Soga1,2
   1
Department of Materials Science and Technology, Faculty of Industrial Science and Technology, Tokyo University of Science; 2 Imaging Frontier Center, RIST, Tokyo 
University of Science
P39. FE-SEM Ɲ{ EDS uҳвʳţwţ͂     HΊ̵̮ 1E̸‫ ̑׿‬11ƊͻхȚˀԄǽȚǽȚּ ŋхȚгѓх― 33 ―

P41. ՙԡŅ‫ץ‬ʍְЀRjǀö‫ק‬ǽӀЗϾ̘wÚÌ±ÜͦւǹƅwԟȭrͱҸԡ̑Hɣ֣ƺɗ 1EΟɣ̐à 1EЁët 1EŻӸӶ 1
   1Ͽ͢ˀԄҌƬгѓʹ¾ÏµØгѓֲ֙
P43. Ì©Ӏ©Ö©ѽҷwοɬÏß¨Ü Hɇ֙ɶǤ 1E̔‫ ׷׈‬1EΑՃԎú 1EȸɅׁǿ 1EӓΥ‫׷‬ʓ 1
    1̿ăǽȚǽȚּӷȚѲгѓх
P45. ψβë FM-AFM ЀRj̬ͱÞϾĞţȖ̺́Ԉ‫ה‬wΊƺͦւÏß¨Ü HɣЁӘͮ 1E̲ƎԎ̗ 2Eȸ̓ǚ 2EɅЁǅ̀ 2EЁëЫϾ 3E‫؀‬ϕӞ 1
    1Ͽ͢ˀԄҌƬгѓʹĺɯɒȚгѓֲ֙E2 ă֚ǽȚɒȚгѓхE3 ǥϸɒ͢ǽ ȚɒȚ֙
P47. ‫͒׵‬џÍ¶£Ü·×ͦւwœϢϟ‫ץ‬ʍְԡ͂rџӪҔuʀ‫ט‬ H͸ЁѸɣ 1EвɅ‫ג‬ӭ 2EŻӸӶ 2E͸˸ʐ 1

 
  

1

ѡΟǽȚĞұѲE2 Ͽ͢ˀԄҌƬгѓʹ¾ÏµØгѓֲ֙
P49. ʳֱŗ֬ÖÏ×Ëµ‫מ‬Ǣw±Üw̼ƅ¯Ü¿ՕÃ§ÜwͱҸԡ͂ HЁët 1,2EӸþԎѳ 3Eɣ֣ƺɘ 1EвɏӔͮ 4EɇɎșΙ 3E
ŻӸӶ 11
ϿҌг¾ÏµØE2 ѡΟǽּϾƹϽǯE3 ƆǽּEʢǨхȚE4Ҟ‫ױ‬ЦїĺɯхȚǽ  

11:35P11:40 ‫ؗ‬ĔʭÞщƀ‫ؘ‬
11:40P13:00
MĒ͢ƬƮ«Í¸ß؄ÖÜ±ÕÜɼɴ؅NԬՁȑƾĕ
13:00P13:05 ‫ؗ‬Ĕʭ‫ؘ‬
13:05P13:35
MЧɊũƺƐǵչʡԽώNɭֱ֧̲ؕƺЄ؄ɝăǽȚ؅ŻӸӶơϿ͢ˀԄҌƬгѓʹ؅ЧɊũƺƐǵrџơҔţȖͱͦвξĮà̍яЁǽȚϼɒȚԄּ
13:35P13:40 ‫ؗ‬Ĕʭ‫ؘ‬― 34 ―

ǩʹؕëĕՁȤǩʹؕȸĕՁȤ
13:40ࠥ15:15
࠙ࢩ࣏ࣥࢪ࣒࢘ 1-bࠚ ࠕศᏊࢆࡳࡿ 2㸦㟁Ꮚ㢧ᚤ㙾㸧ࠖᗙ㛗㸸ᑠ᳚ಇᙪ㸦⏘ᴗᢏ⾡⥲ྜ◊✲ᡤ㸧ᐑᕝᣅஓ㸦ᮾி኱Ꮫ㸧S1b-1. ୕ḟඖග㟁Ꮚ┦㛵㢧ᚤ㙾ἲ(3D-CLEM)࡛ぢࡿ࣑ࢺࢥࣥࢻࣜ࢔ࢲ࢖ࢼ࣑ࢡࢫ
ኴ⏣ၨ௓ 1, 2
1ஂ␃⡿኱Ꮫ་Ꮫ㒊ඛ➃࢖࣓࣮ࢪࣥࢢ◊✲ࢭࣥࢱ࣮ࠊ2 ஂ␃⡿኱Ꮫ་Ꮫ㒊ゎ๗Ꮫㅮᗙ
S1b-2.

Structural changes in actin filaments induced by repetitive interaction withmyosin II have an important role to inhibit cofilin binding and severing toactin filaments, as demonstrated by high speed AFM
ien uanano i e cience nstitute- ano, ana awa ni ersit ,S1b-3. ㉮ᰝ㟁Ꮚㄏ㟁⋡㢧ᚤ㙾࡟ࡼࡿỈ⁐ᾮ୰ࡢ⏕≀ヨᩱࡢ㧗ศゎ⬟ほᐹࠐᑠ᳚ಇᙪ 1ࠊᒸ⏣▱Ꮚ 1
1 ⏘ᴗᢏ⾡⥲ྜ◊✲ᡤࣂ࢖࣓࢜ࢹ࢕࢝ࣝ◊✲㒊㛛
S1b-4. ᭱ඛ➃㟁㢧࢖࣓࣮ࢪࣥࢢἲ
ᒾᓮ᠇἞኱㜰኱Ꮫ⺮ⓑ㉁◊✲ᡤ
15:15ࠥ16:25
࣏࠙ࢫࢱ࣮ウㄽ㸯 ࣏ࢫࢱ࣮ወᩘ␒ྕࠚ
16:25ࠥ18:05
࠙ࢩ࣏ࣥࢪ࣒࢘ 2ࠚࠕࣉ࣮ࣟࣈ࡜ಶయࡢ࢖࣓࣮ࢪࣥࢢࠖ
ᗙ㛗㸸᭮ᡃබᖹ㸦ᮾி⌮⛉኱Ꮫ㸧ᵽཱྀࡺࡾᏊ㸦ி㒔኱Ꮫ
S2-1. ࣐ࣝࢳࣔࢲࣝከගᏊ㢧ᚤ㙾ࡢࣂ࢖࢜࢖࣓࣮ࢪࣥࢢ࡬ࡢᛂ⏝ሬ㇂╬⏕៞ᛂ኱Ꮫ་Ꮫ㒊S2-2. 㔞Ꮚࢼࣀᮦᩱ࡟ࡼࡿ iPS ⣽⬊࢖࣓࣮ࢪࣥࢢ࡜෌⏕་⒪࡬ࡢ㈉⊩‫‮‬ᕝ༤ྡྂᒇ኱Ꮫ኱Ꮫ㝔ᕤᏛ◊✲⛉S2-3. ᳜≀࢖࣓࣮ࢪࣥࢢ࡟࠾ࡅࡿ㉸⪏ගᛶ㏆㉥እ⺯ගⰍ⣲ࡢ฼⏝ࠐబ⸨Ⰻ຾ 1ࠊከ႐ṇὈ 1
1 ྡྂᒇ኱Ꮫࢺࣛࣥࢫࣇ࢛࣮࣐ࢸ࢕ࣈ⏕࿨ศᏊ◊✲ᡤ― 35 ―

S2-4. Bioluminescent technology for visualization of biological functions
Takeharu Nagai
The Institute of Scientific and Industrial Research, Osaka university.
18:05P18:20 ‫ؗ‬щƀ‫ؘ‬
18:20P20:00
MʰԞĕNǩʹؕÃÂ¹²؄‫ש‬ǧ؅

9 ̫ 4 ̊؄Ϝ؅
8:50P11:05
M§ÜË¨Î 3NIѽҷԘEπJɭֱؕǿЁǆέ؄̿ăկɒǽȚ؅ɇ֙ɶǤ؄̿ăǽȚ؅
S3-1. ՙԡŅŋȚ‫ץ‬ʍְuҗ҉ϰ±ÜwÏß¨ÜHЁët 1.2EŻӸӶ 11Ͽ͢ˀԄҌƬгѓʹ¾ÏµØгѓֲ֙E2 ѡΟǽȚǽȚּϾƹϽǯхȚгѓх
S3-2. ‫׷‬ցՙԡŅ©Â¹Ü µ©œϢϟ‫ץ‬ʍְwִЗ
H̜ӻñ 1E̿ˌƽ 11ͭΗ‫͏ͱ׎‬ɴĕн ÖÃ¼Çß§ÕÜù̵֙͢ ¾­×Óß§ÕÜ«Ü¯ßS3-3. ѽҷŖοɬwÏß¨Ü ԟȭr˱ġuοɬϾϮȚ
Hɇ֙ɶǤ 1EӓΥ‫׷‬ʓ 11̿ăǽȚǽȚּӷȚѲгѓх
S3-4. Ø»ÖwɼʨūʋΞ iCOM wִЗHȥ̵ɋƧ 1EɊ֣Ć 11ѡΟǽȚ ƈȚƈЕѲ ŖţΝČԾÞѱȽАŖх
S3-5. Split-GFP ЀRjØ»Ö£Ü¯¶¥¶wƦԚƅrԡ͂Ё̻ɯɅɼǽȚϼȚ֙ϼȚх
S3-6. ѽҷ͐ÞÚÌ±ÜƀʨwϾѽҷÏß¨Ü̲̻ȟ̿ăɒ͢ǽȚхȚˀԄŷʳгѓּѽҷūʋɒȚгѓ«Ü¯ß
11:05P11:10 ‫ؗ‬Ĕʭ‫ؘ‬― 36 ―

11:10P12:30
MË©¯ß¥Ì×ßԽώ‫؍‬NɭֱؕͰ̵‫װ‬ĭȖ؄Ɗӭɒ͢ǽȚ؅̶Υƺɥ؄̿ăϼхǽȚ؅
P2. ϮϼƅȚrԤѥхȚu×©Ђ̾b ØÜwїĞͦւԡ͂
 

P4.

H̻̀ҟׁ 1, þãɧǽ 1, Ǳ֣ıԵ 1, ðĭҝ‫װ‬Ȗ 1, Ţ̻ӟӤȖ 1, ɚɇׁɥ 1,̵͜ɯɦ 1, ЁČň 2, вͰĺà 3, ǽ֣ȺĆ 3, ȸɊͷͮ 11̿ӷǽ¥Ͼƹ, 3 ӷ, 2 ̑̔ǽ¥ϼɒйʚ¸¼ÅÚßÄuØ§ÎʔѢǟ fMRI
HɇЁ̟ 1EBenjamin B. Bartelle2ENan Li2EVincent Breton-Provencher3,4E
Jiyoung J. Lee2EElisenda Rodriguez2EJames Melican2EMriganka Sur3,4E
Alan Jasanoff 2,3,5
1
Ͽ͢ˀԄҌƬгѓʹĺɯɒȚгѓֲ֙E2MIT ϾϮɒȚхE3MIT ӀԲахȚ

P6.

хE4MIT ÂÛßȚҡԦʯгѓʹE5MIT ƘȖŹɒȚхШӨЂ̾ β ØÜ 3 ֤ĞwїĞͦւԡ͂

P8.

HǜЁǉĄ, ë̻Кӗ, Ȱ̹̓ϼ؈Δ͹, ̻̀ҟׁ, ȸɊͷͮ̿ӷǽ¥Ͼƹ
ƏàÍ¶£Ü·×Ïß¨Ü u×©´ͦւȝȢƅͱͦwгѓ

HѫЁШЂ 1E͌ЁՌɶ 1Eǽϕ̯֗ 2EǿЁǆέ 11̿կɒǽÞּɒÞϾƹɒE2 ֚ĺɯֱȲƈЕ«Ü¯ßгÞϾĞԹѧͱҸ
P10. Intracellular Ca2+ dynamics in guinea pig-pulmonary vein cardiomyocytes
HYusuke Tanaka, Tamano Ohmori, Shogo Hamaguchi, Iyuki Namekata, Hikaru
TanakaDepartment of Pharmacology, Toho University Faculty of Pharmaceutical Sciences
P12. Green-Red ӽŋ¯Ü¿ՕЀRjúŋȖ FRET Ïß¨Ü ̽Đw̪֑ƅH̷ϕŇʎ 1,2EћŖŒɣ 1,3EЁë‫ ט‬1E‫ל‬ЁĄ 2,3Eë̻ɉƧ 1,31̿ăϼхǽÞϾƹгE2 ̿ăϼхǽÞϼɒÞϮϼE3 ̿ăϼхǽÞIFCE
P14. ¬¹¤¡ÐµØrbj͞Ϯwֱ՝‫¸ §׌‬ØĖ֍wÏß¨Ü ԡ͂HͰ̵гʓ 1EօӸǽժ 2ÉͰ͸ 2Eχΐ̡ 2 EֱՃɏȣƻ 2E̶Υƺɥ 1,21̿ăϼхǽȚÏß¨Ü ÃÚÜ´«Ü¯ßE2 ̿ăϼхǽȚϼɒȚ֙ʔЀϾϮхȚхP16. ȸҷĞщԃʚCEPIAЀRjӊӋβѽҷ͏INS-1wȸҷĞCa2+wƦԚƅؕ‫׷‬ҹҰ֟ϽǯWȸҷĞ-ѽҷՕֵwCa2+ƀʨuæTʀ‫ט‬ɏðĭʦҝ 1EЁëŋ 2EHЁëТȖ 11ǽȏȊȖǽÞ‫ש‬ϮE2 ֖̿ǽÞӷ― 37 ―

P18. W©ÃÚ·ԡ͂wjִЗwÏß¨Ü

«ØÂ²ßrɼʨʢǨԡ͂wHŻӸ Ȭą 1EμЁ Шҁ 1E̊ä֙ γȖ 2EԀΐ ʪ 1Èþ ԎƧ 2E͋ΖШϔ 3E֥͜ ˹ɥ 4E̷ά ʩΙ 4EŻӸ јƪ 11ƯǽּÞŷӷхȚ, 2 ѡΟǽÞƈ, 3ESCO, 4 ϿҌгÞŷӷǤР
P20. »ӯ¯Èß¶ɄwÅÚ ÖÎѽҷͽ‫؞‬ӗѬʳϧuU\Χʚ֟Ѻю(ROS)Ͼʳ‫؞‬ß¶Ã¨ßwƀʨԡ͂rhwʁŶH̶Υƺɥ 1,2EϕЁ‫ׇ‬ɣ 1EтΌđƴ 1EӗįҖ 2,3Eȸ֣ҩú֘ 4E
ȸɏƺŞ 1EՐɁуׁ 1,5,6EǗɆѰà 6E֣G̻Քà 4E̾‫ל‬șŋ 2,71̿ăϼхǽȚϼɒȚ֙ʔЀϾϮхȚхE2 ̿ăϼхǽȚÏß¨Ü ÃÚÜ´«Ü¯ßE3 ̄ϑǽȚӎϣхȚѲ؄կ؅E4 Ǖї֔ĖȚгѓʹȣ‫׳‬ǖ
ǩE5 կгͱͦ‫؞‬ϾϮͱҸũЀֲ֙E6 ʦȕǽȚկȚ֙E7 ŒїԺԧ̿ăϼхǽȚɒȚ֙
P22. ŗ‫כ‬ťǹЊĞwѿƬfu Rab11 «Ü¥ßw°¸Í²ÙÜ¨wˎǽǓH̀þШņEϤþҢE֥ŋ؄ӸЁ؅̑‫ח‬Eë̻ɉƧ̿ăϼхǽȚϾƹƈхȚгѓʹ
P24. ֤Ȗ·²¶uȞŐս̑ƅѿҙŖщ͞ɦѽҷÏß¨ÜHΊəИʓͮ 1Eςɏ Ɛ Eȸ֣ɊǽĈ EΦɌʟȀ EãЁΡɗ E‫ױ‬ǩǋĮ
1ƯƥɁǽȚǽȚּɒȚгѓхϾƹţȖɒȚȴ˶E2 ̿ăǽȚǽȚּƈȚѲгѓхͱҸϾϮȚȴ˶
P26. ͞ϮwЗϾ‫؞‬ɼʨɼʳuU\Χʚ֟Ѻю(ROS)wʁŶ-¬¹¤¡w ROS Ͼʳ֞ѺͲ˩ǹЊĞwɼʨɼʳЊɠwÏß¨Ü ԡ͂HӫƘ‫ ͮ׈‬1EͰ̵гʓ 2Eȥ̵ǽթ 1E‫׸‬ɏ̟ɶ 1EΪþƌô 3EȸֶΡñ 2,3E
̶Υƺɥ 1,21̿ăϼхǽȚϼɒȚ֙ʔЀϾϮхȚхE2 ̿ăϼхǽȚÏß¨Ü ÃÚÜ´«Ü¯ß
P28. X Ҏ 1 ţȖչ՞Ξu TRPV1 ±Ñ»Øw 3 ͳŇ։ƀHӸ̻љȖ 1Eâȼƺɶ 1Eıˑ̐ɶ 2EֶƤƐƧ 3EâȼȠČ 1EðĭΡ 1E
   ĝG̲Ԏͳ 1, 2, 3
     1ϿҌгÞ̿ǽŊњÈÖÜ·ԤπˀԄ OILE2 ̿ăǽȚǽȚּ̄‫מ‬Ǣŷʳх   ȚгѓхE2 ‫׷‬ժɬŋхȚгѓ«Ü¯ß SPring-8
P30. pH ʧƣʚӽŋÅÚßÄuе‫׵‬ѽҷÅÚ¶ÜËÜÅƀʨw in vivo ԟȭ   HӳɊ҉̀ 1)Eǽ͜‫׈‬ǿ 1)E ӧǛƺô 1,2)
     1)ǽַǽȚǽȚּɒȚгѓхE2) ǽַǽȚōЎȚÃÚÜ´гѓ«Ü¯ß

― 38 ―

P32. ͧGtÌßßЀRj͞ϮѽҷŖw±ÜÃÖÏÜ¶wÖÄÏß   ¨Ü   HՌɎѷð 1EֱɌ̙ 2EŋЁɂׁ 1EãЁǿ֘ 3
     1Ͽ͢ˀԄҌƬгѓʹϾϮÅÚ«©гѓֲ֙E2 Ͽ͢ˀԄҌƬгѓʹ¾Ï   µØгѓֲ֙E3 ̍яЁǽȚŊօϼɒȚ֙
P34. Toward Automated Identification and Analysis of Cell Differentiation Stages
using Bright Field Microscope Image by Artificial Intelligence
Archana Bajpai1, HToutai Mitsuyama1    1
National Institute of Advanced Industrial Science and Technology (AIST)
P36. Ǽϟ՗͍ǟ 2 ŋȖ‫ץ‬ʍְu 4 ֢ͪԿϾѽҷw 3 ͳŇҀ̘ԟȭ   H֮ЁʜƧ 1,2Eǽƞɯɣ 1,2E̻Ёׁ 3,4EֱՃ֙ŋΡ 3,4E̵͑аɗ 1,2
     1Ɔί֌ǽȚÞǽȚּʢǨхȚгѓхE2 Ɔί֌ǽȚÞ‫׎‬ȖхȚгѓʹE     3ǤкϾϮȚгѓʹÞϾϮօƅгѓֲ֙E4 ҌƬгѓǽȚּǽȚÞϾƹхȚг    ѓх
P38. ÌÚ¾ÄØrՙ‫ח‬ΟЀRjӀͪЛӷϮµ×¾×ßuֶdǤкЛ͟ԥ   Hȸįǽͮ 1E֧̲ Ą 1EӫƘӖҝȖ 1EJohan Unga1EȠŅϼѷ 1E
   Ɋ ʕŋ 1EʀɅΕҙ 1EìɅà‫ ׈‬1     1ɝăǽȚ ӷȚ֙
P40. Ùß¦ßԴ՘Ԉ‫ה‬ǹě‫ץ‬ʍְЀRj͞ϮѽҷԈɄwѯɺʚϯʚwԡ͂:   Χʚ֟ѺюĈbj͞ϮѽҷwŊњʳֱrѽҷǲwŹȚЛϯʚwūʋͱͦ   H͜ġĬѳ 1EǽՊĆз 2EͰ̵гʓ 3E̶Υƺɥ 3,4EЂþȟΙ 1,2
     1̿ăϼхǽȚ гѓˠօͱͦ ҌƬгѓּ ß¯ßÃÚÜ´¥Ü   ©&´¼Ú¨ßгѓ«Ü¯ßE2 ̿ăϼхǽȚ ϼȚ֙ќà֙ ƅȚхE     3̿ăϼхǽȚ гѓˠօͱͦ ҌƬгѓּ Ïß¨Ü ÃÚÜ´«Ü¯   ßE4 ̿ăϼхǽȚ ϼɒȚ֙ ʔЀϾϮхȚх
P42. ÌÚÃß¨ѽҷwÃ¤¥¶ß§©uU\ LPS w¨Ó¾Ü¶ġЀHǽƞ ˌô 1 ؈Ͱ̵ ‫װ‬ĭȖ 1,2
     1Ɗӭɒ͢ǽȚɒȚгѓхϾƹϽǯхȚȴ˶؈2 Ɗӭɒ͢ǽȚŊօɒȚ֙Ͼƹ   хȚх؈
P44. OTN յՖǻӽŋÏß¨Ü §©´ÎЀRjҳ΍˜ΜwÖÄÏß¨Ü   H͕ϕ‫׉‬ƺ 1,2EƭЁө 1Eã̻ШϾ 1,2ĘʴŒɣ 1,2
     1̿ăϼхǽȚǤкɒȚ̺֙́ɒȚхE2 ̿ăϼхǽȚҌƬгѓּ IFC
P46. ѿҙս̑ƅˀԄuНӇŖ֙ͦւw 3D Ïß¨Ü rͦւԡ͂   Hԕϕʓï 1E̿ÝɌĺ 1Eвξϓ՟ 1ÈϦрȖ 1
     1͏ɴĕнÃÜ¡ØҌƬгѓʹ― 39 ―

P48. ƏàŋȖqţŋƦҸtՙĖȷեщњ«Ü¥؄TES؅wÏß¨Ü   HíҠàͮḘ֙‫֡װ‬EтЁǽΙ   Ͽ͢ˀԄҌƬгѓʹϮϼԤπͪυгѓֲ֙
P50. ѽҷŖȾʹqwÌ »§ÎÜw FRET Ïß¨Ü    B̄ӸՄ 1EɅë‫ ؂‬1E֧̲șΙ 2EǦЁҨƪ 1Eɇέǿ֘ 11ʬǽϼɒϾƹʢǨE2 ʬǽϼɒʔƅʔЀ

12:30P13:10
MҌĕN
13:10P13:15 ‫ؗ‬ĔʭÞщƀ‫ؘ‬
13:15P14:15
MùƁȾîŁÖÜ±ÕÜ«Í¸ßNǩʹؕëĕՁȤɭֱؕĝG̲љ؄Ͽ͢ˀԄҌƬгѓʹ؅ë̻ɉƧ؄̿ăϼхǽȚ؅
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Development of chemistry-based state-of-the-art imaging and perturbation technologiesBΟ֎Εϖ 1,2,3
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BYasuteru Urano1,2,3

1

Graduate School of Pharmaceutical Sciences and 2 Medicine, The University of Tokyo, 3CREST AMEDӪŉÎÞ§ÛʸΒxEϮXpRѫҥŽϠĜœuU\ƧмϮĜʍѐEÖ×®Í

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Umezawa K, et al., Nat. Chem. 2017)F`uƪƔϬuǠoXEŻՄϢʡVwЇӪŉċǷwѾƶնкўȦuŨʄd^rqEactivatable ǛϮϠЇŉÄÙÞÃÝŉǬʠÄÙÞÃƢԇŉŻՄÞ§¶ƂƨϠtsw˼jtԌγÝ˥ŽʸӱwŴӽu ʬŷbpXj(Takakura H, et al., J. Am. Chem. Soc.
2015; Ichikawa Y, et al., Angew. Chem. Int. Ed. 2014; Umeda N, et al., ACS Chem. Biol. 2014)F̫ԪρqxEƂȕЋtЇʜ‫כ‬ġd^rqԠϮd̠˼‫ͦנ‬ҦÎÞ§ÛÝ˥ŽÄÙÞÃ
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Med. 2009; Urano Y, et al., Sci. Transl. Med. 2011; Asanuma D, et al., Nat. Commun. 2015; Ueo H, et al.,Sci. Rep. 2015; Shinden Y, et al., Sci. Rep. 2016)F̫ÄÙÞ°xEƌùȓw½ËÞÞƢԇƂuǠoZԗ˻ÄÙÞÃw֟Їk\qtZEыҔwˉn˶Њм‫ב‬wӪŉÄÙÞÃVʬÕÃÕÖÞ˼‫פ‬Һɡ͕Ĝ}rռϰbpÕÃÎÞ§ÛӰS^rqE˼jt½ËÞÞwЇԅƢҦrd wqQ(Onoyama H, et al., Sci. Rep. 2016)E`uƪß½ËÞÞΚϰbjԗ˻r΍ЅwßĜƂ ȞϪd wqQ(Chiba M, et al., Angew. Chem. Int. Ed. 2017)F̫ԪρqxE^wWԗ˻r΍Ѕu֡d̠˼wʬ̻

― 45 ―

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Functional analysis and exploration of proteins based on imaging
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BRyo Iizuka1

1

Graduate School of Pharmaceutical Sciences, The University of TokyoρҔx^qEX Ѽѯ̔͛խԎ̸Β[1, 9, 11, 16], EX Ѽȳԍ˳ôΒ[2, 6, 17]E͆ШͽŐ‫צ‬Β[10]Eָȑ‫׏‬ʆ֛Β[5–7, 12, 17, 18, 21]EӪŉ‫׏‬ʆ֛Β[3–5, 8, 13–15, 19–23]tswÎÞ§ÛʳΒ‫כ‬ġbE®Û¾Ձ
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1 ŠȑӪŉÎÞ§ÛWƢҦrtF^ŦϰbEǹҲӕw¦ÐÇÙ¸Û GroEL wͦҦЋtƜʍê֠ĜwВ˗ԌȨuʬŷbj[20]F^wЇԅWȂͦrtEϮƂȕÝѫҥϮϠȕw˲д̝uԓՓ`s̢ƫt GroEL wƜʍÏ´×wԅВbWբSutmjFϭǫêw 99%ċâwʆϮϠxEϪǕwʸӱqxǟ‫ח‬WǍַtʆϮϠ‫ַ׬‬ǟ‫ח‬ʓʆϮϠ‫׭‬r`pRFַǟ‫ח‬ʓʆϮϠWϯϮd։ѨxE˼jt։ѨԽηrbpֽəuǹXtƢҦʓжp
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¦Û×ª×ƌęqʆϮϠwŎ¡»ÍǬɚӰSFʃj¡»ÍʛǤŦϰbE͟Ћ։ѨտĔȑƞʃdF^w˽ΒwȞՌuE΢;êw̩ǟ‫½ח‬³Öϲ̴˼Ԇ β-×¢¦¯Þ«տĔȑǸ˶ƪȝd^ruʬŷbj[24]F[1] J. Mol. Biol. 335, 1265–1278 (2004) [2] J. Biol. Chem. 279, 18834–18839 (2004) [3] J. Biol. Chem. 279, 31788–31795(2004) [4] FEBS Lett. 579, 3718–3724 (2005) [5] J. Biol. Chem. 280, 32586–32593 (2005) [6] J. Biol. Chem. 280, 40375–
40383 (2005) [7] Extremophiles 11, 225–235 (2007) [8] J. Lumin. 127, 192–197 (2007) [9] Proteins 70, 1167–1174 (2008) [10]Proteins 70, 1257–1263 (2008) [11] J. Mol. Biol. 376, 1130–1141 (2008) [12] Proteins 71, 771–782 (2008) [13] Nucleic Acids
Res. 36, e70 (2008) [14] J. Biol. Chem. 283, 23765–23773 (2008) [15] J. Biol. Chem. 283, 23931–23939 (2008) [16] J. Mol.
Biol. 383, 465–474 (2008) [17] J. Biol. Chem. 283, 34773–34784 (2008) [18] Proteins 74, 6–17 (2009) [19] Biochem. J. 427,
247–254 (2010) [20] J. Biol. Chem. 285, 23159–23164 (2010) [21] PLoS ONE 6, e22253 (2011) [22] Proc. Natl. Acad. Sci. U.
S. A. 109, 4881–4885 (2012) [23] J. Biol. Chem. 287, 41118–41125 (2012) [24] Sci. Rep. 6, 22259 (2016)― 46 ―

ЗɅŦƶƍǱդʚԪρ
Ĥ¼£¬%ĴŅ±ôñDr. Toshikazu Majima and the Molecular Mechanism of Muscle ContractionBСαĬß 11̄нϱǹȕÝϬɌȕӱ֧BShin’ichi Ishiwata1

1

Waseda University, Faculty of Science and Engineering ЗɅŦƶƍǱxE֢ǹÝǠЩɌÝϮϠɌȕд̎ĊwƌѫҥϮϠwӰŽuȋEϮĜҶѮpEȦЙǛՏ X Ѽ‫׏‬ʆ֛ΚϰbjϮĜ͛խErZuѫҥ͛խwТсrRSˋʮЋtТс`j^rqПpRdFhwɻWERy̠ʀwćørbpEэƝ҂Šȑͦ͛u֡dϣһwԣŏӵ`j^rEhuʊӯΔWj^rxEQПpRtRkSrʑRdFЗɅƍǱW^wԨ˸ğʬuŶΔWj^runRpxEhwŮuгwТс×ÞÄWЇӵbjԨ˸‫׬‬Ref. 1, 2‫׭‬W± wßnutmpUEhwԨ˸șʬ`fâqEBIOPHYSICS ԞwѽִȌƺ֜bpRjг ԭԨdͦēWQmj^rVEЗɅ`w̠ʀwUćø‫׬‬Ref. 3‫׭‬իbpEЗɅ`wТсҔrbpw҃͘wßш_ѬĆbjRrʑRd ЗɅ`xϮϠɌȕдw‫̧״‬ϮqdWEǹȕ֧qȠ̫Ț`Eě΍ИϬ`rƪ̧ōȕqdF
hwׄгxEƫǹÝϬÝϠϬȕдwƍǱԥкuRbjWE^wŅͽwӁRµÖw^rxȓcâ]pRbjFȴGТс³ÞËWϺt^rVEhwʀТсâwĀΛxQtVmjwq
dWEЗɅ`WэƝ҂Šȑͦ͛u֡bpɲRҾƳjj^rVEʑR

tRТсĀΛWqXjwqbjF Õ¨Ǡ̷âuƮЙbjÌ¦ÛŠȑwâß̫w°ÛÂÕÎÛµWμմŽd In
vitro μմŽѠrRSȞ‫ל‬ѠWȲō`j^rqEгjlxVvpVͽutmpRjEμմŽuĕmp°ÛÂÕÎÛµxhw֜ՑwƲǊՐbtRVEԐR˽ǵTyEÌ¦ÛŠȑÏÞ®ÞWЇϮdμŶxE°ÛÂÕÎÛµw֜ՑuΎSμմŽŶuŸTpE
ÂÕÎÛµǊՐ`fStµ×ʬŠƭtRVErRSǀRuѐTȞ‫ל‬ѠɌǼbbjFhwѯ̻Ehwµ×wȓǕumpE°ÛÂÕÎÛµWˑEՅfɵʬdrRSʑRW\tRЇԅd^rWqXbj‫׬‬Ref. 1‫׭‬FЗɅ`x^wԨ˸uɲRҾƳˉjEÌ¦ÛŠȑÏÞ®ÞwЇϮŶuƭµ×ʬŠwʞƳΨZғȨbEŎZ
˼bRƝ҂ŠȑÏ´×͛ʜ`^rutbj‫׬‬Ref. 3‫׭‬Fɴ́x^wԨ˸êʊuЗɅ`w҃͘_ѬĆbE2 ɝŮuþZtjЗɅ`Ĺ{jRrʑRdF[Ɨғ˸ϥ]
1) Nishizaka, T., Yagi, T., Tanaka, Y. and Ishiwata, S. "Right-handed rotation of an actin filament in an invitro motile system." Nature, 361, 269-271. (1993). 2) Tanaka, Y., Ishijima, A. and Ishiwata, S. "Super helix
formation of actin filaments in an in vitro motile system." Biochim. Biophys. Acta, 1159, 94-98. (1992). 3)
Majima, T. “Load-dependent sliding direction change of a myosin head on an actin molecule and its energetic
aspects: Energy borrowing model of a cross-bridge cycle.” BIOPHYSICS, 5, 11-24. (2009).

― 47 ―

S1a-1
 rԑѓдȕwѳƨuџ֚wͨŅ͛խ¯·Ì¨wԎ̸Conformational analysis of oligosaccharides using NMR−validated MD simulationО̨Țƶ 1Ę֒ոƹ 1,2Eԯêřȑ 1,2EɀƠ˄Ȟ 1,3EŸӥ̏ß 1,21ƫơȼɔхǹȕǹȕ֧ӤȕТсдE2 һϕдȕТсͦ͛ϮƵŴʬ˖сªÛ®ÞE3 ƃ֩ňшǹË
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Hirokazu Yagi1, Tatsuya Suzuki1,2, Saeko Yanaka1,2, Takumi Yamaguchi1,3, Koichi Kato1,2

1

Graduateed School of Pharmaceutical Sciences, Nagoya City University, 2Explatory Research Center

on Life and Living Systems, National Institutes of Natural Sciences, 3School of Materials
Science, Japan Advanced Institute of Science and Technology.
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Vud^rWʋԃqQF^SbjϢΏw

rEʭGxəШʓż̻ŦϰbjNMRŠŉΒrԑѓдȕѭƨfjџ֚wŽЋ͛խԎ̸ʳΒw֟ЇuŶΔRqXjFəШʓNMRΒx0P4ÉÏÑÈ´Vxs<

S§.²¥§¯±@6)¨Ryt]§ * NMRÆÑ»¨+½ÇÂ&´ghd}¦¾Ê»ÂÍ¨W´® °¥:§Vx#´ºÄÑ²qi~5$´Z§|²¥¤
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S1a-2ńŁãñſŢé'©"ñſĕĎ²(ł¡8`orQ

Integrative approach for structural biology based on X-ray crystallographyBȠɊ˄ó 1Eϱðįń 11̵āǹȕǹȕ֧՚ȕϮƵдȕТсд

BTakuya Miyakawa1, Masaru Tanokura1
1

Graduate School of Agricultural and Life Sciences, The University of TokyoϮƵϪԱ͛їdƂȕƜʍrŠȑ֠ГúğϰƔȑØÆ×qϬԎdI͛խϮϠȕJuUR
pEX Ѽѯ̔͛խԎ̸xϮƵϪԱ˂S®Û¾Ձ͆֊EhuѯƨbpͦҦdǸ͜tϮĜŠȑӤűwğϰ͛խԎ̸djw̠

̢żtʳΒwßnqQFSPring-8  Photon

Factory tswǹǛ˯Ȱŉ˾ԕwÀÞÍÕÛw֟ЇWհEX Ѽѯ̔͛խԎ̸WռϰƢҦtȬԱxҶ®Û¾ՁxcrbpЎGˆǹbpRFX Ѽѯ̔͛խԎ̸qxEԎ̸ȬԱrdŠȑwѯ̔ʋԃrdWEϪǕqx˶ÌÙÛwʆѯ̔Vq

X ѼǊʽŃƝִbpԎ̸qX

sÀÞÍÕÛr´Þ®ƝִwʸӱWЇոbpRFX Ѽѯ̔͛խԎ̸umpԇԉƂ`jϮĜŠȑw 3 ͨŅ͛խxEǸZwǥƨuƂȕƜʍrŠȑ֠Гúğϰԣ̈djwíԃt͛խǠАЪƽbpZFbVbtWEŠȑwѭƨfumpxEʆѯ̔dʃtR^
rWQE֦jŠȑϢʡw¨·±Ä¦Ô±µk\qxϬԎWǍַtğŽͦ͛u֡dʛǤӼșdjuxEĈwʳΒrѭƨfjѳƨЋtÄÙÞ°uԎ̸W֍ԃrtF
̠ՠEʭGxEX Ѽѯ̔͛խԎ̸uʃj͛խʛǤuȬbpEX Ѽȳԍ˳ô‫׬‬SAXS‫׭‬EŠȑŽŶȕ‫׬‬MD‫¦׭‬ÌÒØÞ¦ÔÛE`uÌ×½Ù§ÞwʳΒѭƨf^ru

EϺt®Äwѫҥœ®Û¾ՁwğŽͦ͛wԎ̸ԚjF̫ԪρqxċãuЪdStʭGwТсѯ̻unRpѬĆbjRF
Ca2+ĤȓЋt͛խսиw SAXS Ԏ̸‫׽‬Õ¦Ûxўȑw‫׀‬ͺuȓǕd Ca2+ѯƨ®Û¾Ձ
qQEўȑWƑuƬVmpճՃdjw‫׀‬ͺմŽ Ca2+ĤȓЋuŨʄdFX Ѽѯ̔͛խԎ̸uʃj Ca2+ѯƨǛÝֽѯƨǛwѯ̔͛խqxERe

2 м‫ב‬w͛խ‫͛֟׬‬խƙ{֞͛խ‫׭‬Wƪ̎uԌγ`jF^͛խwϬԨ˳ơ̂Ѽr SAXS ´Þ®rw͹ՒԎ̸uECa2+ѯƨx֟͛խV֞͛խ}rÕ¦Ûw͛խսиԡȲd^rWЪƽ`jF
ՐŗǋȑwǩǠֆŢԟԬͦ͛w MD Ԏ̸‫͔׽‬ϠwÃÕ¦»¨³Ù¶‫׬‬BR‫׭‬ʛǤĔոwË¨®
ÞՐŗǋȑqQ BIL1/BZR1 x bHLH ՐŗǋȑrƪcÌ»֊ʹǠϰRp G-box ֆŢ‫׬‬CACGTG‫׭‬ԟԬdß˽ECA ֆŢuȬdԟԬWѾR^rq BR ϡϺЋtՐŗŨʄƢҦubpRFѯ̔͛խϰRj MD Ԏ̸wѯ̻ECA ֆŢrhԟԬdÌ»֊ʹǠwԋƶʓĚã`f BIL1/BZR1 ϣһwГúğϰº±µÚÞwɵʬWЪƽ`jF£¸¨µƂƨϠwŦϰu͔ϠÈ×ÏÛƟȣĜwğŽͦ͛wԎ̸‫͔׽‬Ϡw¨µÖ£ÕµÛ‫׬‬SL‫׭‬ƟȣĜ D14 x SL ĤȓЋu͟ЋwՐŗŨʄǋȑ D53 ƙ{ SLR1 rГúğϰd^rqE
SL ʛǤĔոΚʓƂdFD14 uğϰd£¸¨µƂƨϠŦϰbjԎ̸umpED14 W SL
Ÿ;ŠԎd^rqϮcjƜʍϯϠW D14 r D53 ƙ{ SLR1 rwГúğϰԡȲdğŽͦ͛
WЪƽ`jF― 49 ―

S1a-3
Bk:?ř

ƙÈƌ$±5ş3%Observation of individual molecules with cryogenic fluorescence microscopeӥӅ ̵̖āɌ͘ǹȕ Ϭȕ֧ ϠϬȕѠ
Satoru Fujiyoshi
Department of Physics, Tokyo Institute of Technology
jmjßnwϮƵϪԱЇϪ`fjuEѫҥêqxϓ˶wŠȑWłRpRFbV E^wŠȑxƌϣqxtZEº±µÚÞğͦҦbpRF^wStӿֵѠwȞĜПuxEhwϪǥͬЧuϵŃƂd^rWҜԃqQF^wStБ͟uȬbpEϮĜԚ˹w
jwָȑ‫׏‬ʆ֛xEБԉbZЇȽbpRFĢTyEѫҥǷqQyEѯ̔ƂfeuϮĜŠȑӿƨĜwƔȑÏ´×WʳuōSutmpRFß˽EŠԎҦuɰϑWQmjŉȕ‫׏‬ʆ֛ŠԎҦw˭ǂWԅE^qԅTtVmjʆѫtѫҥœ͛խWԌγ`pXpRFbV
bEslw˽Βq EѫҥœքŠȑØÆ×qÎÞ§Ûd^rxqXtRFh^qʭGxEŜѯǐȝbjԚ˹VwӪŉԌȨdjwƜȰǛ‫׏‬ʆ֛‫׬‬ÕƜȰǛӪŉ‫׏‬ʆ֛‫׭‬ϣһ֟Їd^rqEӪŉ‫׏‬ʆ֛wԎŃɥŠȑØÆ×uɮXâ]^ruʬŷbj[1-3]FԪρqxE̵ɌǹЙďċ̴ƞѭqXjÕƜȰǛӪŉ‫׏‬ʆ֛w֟ЇunRpգ~jʀE̠˼wȞ‫ל‬ѯ̻unRpѬĆdF[1] S. Fujiyoshi et al.; Phys. Rev. Lett. 100, 168101 (2008).
[2] S. Fujiyoshi et al.; Phys. Rev. Lett. 106, 078101 (2011).
[3] T. Furubayashi et al.; J. Am. Chem. Soc. 139, 8990 (2017).

― 50 ―

S1b-1töƓ±ģƐƙÈƌýơ

Ƣ$ş3fUEpVl8P:WfBK

Visualization of mitochondrial dynamics using 3D-correlative observation between lightmicroscopic live imaging and FIB-SEM tomography method.
BǻϱǁĆ 1, 2
1ïϷљǹȕƅȕքňшÎÞ§ÛТсªÛ®ÞE2 ïϷљǹȕƅȕքԎůȕԪɦ
BKeisuke Ohta1,2

1Advanced Imaging Res. Center, Kurume Univ. Sch. Med., 2 Dept. Anat, Kurume Univ. Sch. Med.

Ìµ¢Û¶ÖxϣһwտĔȑrƨʬѠˉlEѫҥœq̎GŬGrhwȍǵƂbtWѫҥœwº×ÞģѲEҧՁ×¦ÍwĊԫӰmpRFÌµ¢Û¶ÖwɵʡxEѫҥмѫҥwϢʡuǹXZϺtjEhwɵʡrͦҦw֡ĨʓxơZV͕Ԓ`pXjWEϪǕ̈ЧtѯԨxşpRtRFÌµ¢Û¶ÖwɵʡǵƂq̠Тс`pRwWŠӸÝӫƨwնкqQEŠӸÝӫƨ‫׊‬ɥwǵƂWÌµ¢Û¶Öw֜`ԆȝdrғTpRFßҿuͦҦǾmjÌµ¢Û¶Öx˻ϜƂbEhwßքWËµÂ§ÞumpŠԎ`
^rqEѫҥŎĜrbpwͦҦѷˉÝƸՁєϬuȥåbpRrғTpRF^wնкwǸZxϮƂȕЋU{ŉȕ‫׏‬ʆ֛ϰRjѮ̎ЋԎ̸uհEjϡȝwͶ֭unR
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bVbϮƵϪԱŉȕ‫׏‬ʆ֛rָȑ‫׏‬ʆ֛è˽qˏTSrbjǥƨEèҔwŠԎҦWǹXZչS^rEָȑ‫׏‬ʆ֛qxßծwնкw¨·±Ä¦Ô±µbVԌȨqXtR^rtsVE̫ɴuƪcϪԱˏTpRwVsSVEϡu‫׊‬ɥwĚRϪԱԌȨd֯uxhwԎ֋һĜWǍַutǥƨWǸVmjF^wǀ‫׍‬ԎΆdjEŉȕ‫׏‬ʆ֛qԌȨbjwrƪcԚ˹Eƪcǥʱָȑ‫׏‬ʆ֛qԌȨdŉ-ָȑГ֡‫׏‬ʆ֛Β‫׬‬correlative light electron microscopy; CLEM Β‫׭‬W
ϰRpXjF^w CLEM Βqʃ´Þ®x lèҔwÐ±Äǜ

wqQ

WEԚ˹Ԧ˷ʼƔʓwīˉtsEȞϪduxʸӱЋuǍַqQ^rWǸRʳʸqQmjF
ąǊʭGxEјħqEænʛǤ֏wǸR 3D-CLEM Β֟ЇbEÌµ¢Û¶Öw¯·Ì¨unRpԎ̸bjFĢTyҭŐɺűuҶָęǾmjÌµ¢Û¶Öxʒψu˻ϜƂbÖÛϢ͛խ}ǵƂd^rWПpRFȞ֯ŉȕ‫׏‬ʆ֛ãu CCCP ʻådrÌµ¢Û¶Öx˶ŠœuÖÛϢrtmjFąǊ^wնкEŉȕ‫׏‬ʆ֛ØÆ×w Live-imaging uŽЋuԌȨbEhwÌµ¢Û¶ÖһՎ FIB-SEM tomography uָ‫׏‬ØÆ×wáͨŅ͛խrbpГ֡ЋuԎ̸bjFhwѯ̻Eʂ̴wԅԎrxϺtEͦҦäŎÌµ¢Û¶ÖxȞՁЋu˻ϜƂd^rtZŉȕ‫׏‬ʆ֛ãuÖÛϢut^rEbVbָȑ‫׏‬ʆ֛ãuxȞ֯uрxȓǕfeEhwǸZWZˉmjǴϢw͛խƞ^rẄVrtmjF^wնкxE‫נ‬R͹ӵ‫־‬пˉnȳҥWӵ‫־‬ɱŶwuʂmpɵʡǵƂd֯uԅϠϬЋҶŽʡϪԱr͙p‫ב‬ĘbpUEÌµ¢Û¶ÖwͦҦäŎrɵʡǵƂnt[˼bRÎ¸©ÍwȓǕЪƽd

wqQmj 1F̫ʳΒux FIB-SEM ӹ҉WʋԃqxQWEʳ‫ׅ‬һĜxјħqQFh^qʭGwȞĢѬĆbnnhwʳʸunRpԎԣbEhw̢żʓrԥ‫׍‬unRpԭԨԚF
1. Miyazono Y, Sci Rep. 2018;8(1):350.

― 51 ―

S1b-2
Structural changes in actin filaments induced by repetitive interaction with myosin II
have an important role to inhibit cofilin binding and severing to actin filaments, as
demonstrated by high speed AFM
Kien Xuan NGO
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan
Email: ngoxuankien@staff.kanazawa-u.ac.jp / Tel: 076-234-4571
Abstract
Actin filaments are helical polymers with intrinsically changeable structures (polymorphism). Their changeable
structures are affected by bound nucleotides (i.e. ATP, ADP) and specific actin binding proteins (ABPs). Indeed,
actin filaments interact with over a hundred different ABPs in cells to perform various functions, and the interactionof actin filaments with different ABPs should affect the atomic structure of actin protomers in filaments differently.
Thus, polymorphic structures of actin filaments may play a crucial role to regulate the binding, localization andfunctions of different ABPs in cells. For instances, cofilin is an actin regulatory protein that binds and severs actin
filaments locating in the front of motile cells while myosin II is enriched at the rear and utilizes actin filaments
and ATP for contraction. Our recent results support that these two major ABPs utilize very different actin structures
to bind, localize and function. Indeed, most of the motile cells utilize “actin polymerization” and “actomyosin
contraction” as the basic cell’s engines to migrate. In these two migration modes, actin filaments play distinct roles,“expansion” and “contraction”, respectively. Understanding the molecular mechanism of how polymorphic
structures of actin filaments are regulated and how they utilize their polymorphic structures to control the binding
and functions of different ABPs will provide critical information for understanding how, for example, amoeboid
cells can switch between two modes of migration, “polymerization-driven mode” and “bleb-driven mode”.
Previously, we demonstrated that supertwisted helical pitches of actin filaments induced by cofilin are unidirectionally propagated to neighboring actin protomers in the same filament (cooperativity) and cofilinpreferentially binds to supertwisted actin [1, 2]. Contrarily, myosin II (S1 motor) repetitively binds to actin
filaments during many ATP hydrolysis cycles. These repetitive bindings untwist helical pitches of actin filaments.
We now understand that the mutually exclusive binding of cofilin and myosin II to actin filaments [3] is aconsequence of different cooperative conformational changes in actin induced by these ABPs.
References[1] Kien Xuan Ngo, Noriyuki Kodera, et al., Cofilin-Induced Unidirectional Cooperative Conformational Changes of Actin
Filaments Revealed by High-Speed AFM. eLife, 4, e04806 (2015).
[2] Taro QP Uyeda, Kien Xuan Ngo, et al., “Uni-directional Propagation of Structural Changes in Actin Filaments.” The Roleof Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer, Singapore, Page 157-177, Print ISBN: 978981-10-8459-1 (2018).
[3] Kien Xuan Ngo, et al., Allosteric Regulation by Cooperative Conformational Changes of Actin Filaments Drives Mutually
Exclusive Binding with Cofilin and Myosin. Scientific Reports, 6(35449), 1-11 (2016).

― 52 ―

S1b-3
ůìƓ±ũƓĒƙÈƌ'03úąāw(ĕĎŨÝ(ƞŢōš·

Nanoscale imaging of biological specimens in water usinga scanning-electron assisted dielectric microscopyBȳ͓Īɶ 1EɂϱПȑ 11ϯ͘ʸӱѺƨТсʱ½Î´×Тсք֝
BToshihiko Ogura1, Tomoko Okada1

1

National Institute of Advanced Industrial Science and Technology (AIST)ϮϠuU\ϮƵϪԱԎ̈dâqEϮϠԚ˹;λΥêwhwwϢʡq‫נ‬ŠԎҦԌȨd^rx͙p֍ԃqQFbVbEʂ̴wŉȕ‫׏‬ʆ֛qxEŉwǊʽ֦϶wj 200 nm wŠԎҦuŨ֦`E·»ØÆ×qwԌȨxַbRFß˽EßҿЋtָȑ‫׏‬ʆ֛qxE‫׏‬ʆ֛œք
ИтudʋԃWQEλΥêw¤ÛÄ×hwԌȨd^rxǍַqQFhwjE1970ɝĊVλΥêw¤ÛÄ×ָȑ‫׏‬ʆ֛qԌȨdjwǹͽǔÈ×¯Þw֟ЇWհp̴
jF^Sbj˽ΒwǸZxEҕǔʓw‫נ‬R֊Ƃ¦Ö¢ÛфƂ¦Ö¢ÛӢҶϰRpλΥêw¤ÛÄ×ȮōÝȦȮbEָȑѼВ˗ϖȰd^rqE¤ÛÄ×VwƜȰָȑընָȑuԌȨӰSFhwjEָȑѼu¤ÛÄ×}w¯ÎÞ§WǹXZE¢ÛµÕ¨µW͙pĚRǀ‫׍‬WQmjF
ʭGx^qEָȑѼß̂֐ȾӢҶuƮƝ`fEh^VϮc 2 ͨЋtϠϬѼԚ˹}֠˗ЋuϖȰd^rqEϮϠԚ˹}wָȑѼ¯ÎÞ§ǹɚuĚΰ`fE‫נ‬¢ÛµÕ¨µqwԌȨƢҦud˽Β֟Їbp̴jF̠ՠ˼ju֟ЇbjՃָ̓ȑԡָϨ‫׏‬ʆ֛(SE-ADM)qxEλΥêwϮϠԚ˹ҕǔʓw‫נ‬R 50 nm ƓwфƂ¦Ö¢ÛӢҶ 2 ̺uȦȮdF^wӢҶâքuxE10 nm Ɠw®Û¨³Ûw֐ȾȿɵʬbE^^uĚŸլwִ̲bjָȑѼϖȰd^rqEָȑѼ֐Ⱦȿu˳ôÝƮƝ`fF^uָȑѼwϖȰքęuȹʱЋtָęǵƂWϮcE^wָęǵƂ;λΥêwϮϠԚ˹ըն`fpã‫־‬w֐Ⱦшȑu͕şdFָęǵƂwընʓxEϠՁwԡָϨÛÁÞ¯Û¨uԆȝ`E;x͹ԡָϨW 80 r‫נ‬RjָęǵƂZընdFß˽EϮϠԚ˹͛ʬd®Û¾Ձx͹ԡָϨW 2؅3 кɥrĚRj
ընW֤ȡ`F^uEָȑѼВ˗ϮϠԚ˹uϖȰd^rtZE‫נ‬¢ÛµÕ¨µqwԌȨWqX‫׬‬Ǐ‫׭״‬F̫
ТсqxE^w˼ԆԡָϨ‫׏‬ʆ֛ϰRpE;λΥêwhw
wϢʡw½³Öǟ‫ח‬ѫҥEϞõьwԌȨӰmjFhw
ѯ̻Eֽ̿ӂÝֽǐȝϢʡuUR
p‫נ‬R¢ÛµÕ¨µq‫נ‬ŠԎҦԌȨWƢҦqQmjF― 53 ―

― 54 ―

S2-1
emQiPm¯±ƙÈƌ([:?:hrJpC+(ÊĖApplication of multimodal multiphoton microscopy for bioimaging
BǦԯКϮ 1,2,3
1ʥʪҍǪǹȕƅȕքӤϬȕ˲ȟE2 ͢ΞǑхǹȕϭǫʛǤȕ֧E3 JST `XW\
BMutsuo Nuriya1,2,3
1

Department of Pharmacology, Keio University School of Medicine, 2 Graduate School ofEnvironment and Information Sciences, Yokohama National University, 3 JST PRESTO ӿֵuѱƨmjϮƵдȕϪԱE̴̫wѫҥÝѭ҇͛խѷˉbjwԚ˹uURpԎ̸d^rxϮƵдȕТсuURpֽəu֍ԃqQFbVbEӿֵt͛խˉnѫҥWȦuԛEĦԁЋt˩ğuȬbpҨɰtѫҥѭ҇uURp^xǍַtԥ‫׍‬qQEϡuҮѭ҇qxhW‫׏‬ӛqQF^^qEѭ҇ընʓW‫נ‬RՠՂǷŉϰREֽѼɵż̻u 3 ͨŅЋu‫נ‬Rт֠ŠԎҦȞϪdǸŉȑ‫׏‬ʆ֛xE^wStѭ҇œqwϮƵϪԱwƢԇƂԎ̸uֽəu̢ϰqQ^rẄVrtmjFêq

ӪŉŠȑw 2 ŉȑŻՄŦϰbjǸŉȑŻՄ‫׏‬ʆ֛ʸӱxϮƵдȕТсEϡuҮдȕТс}wʍϰWўŶЋuԚEǸZwÃØÞ¨×Þjbp̴jFbVbEӂѨ®Û¾ՁwӪŉԌγuURpxE¨Çµ×w֍ӿtsVƪ̎uƢԇƂqXϪԱu֦WQEǸ‫־‬ЋtԎ̸u ֦϶WQF^wStŨѢxEӪŉċǷwŉȕϪԱŦϰd^ruòՆTƢҦʓWQFȞ֯EǸŉȑ‫׏‬ʆ֛uURpϰ
RՅР¾×¨ØÞ¥ÞwϖȰuӪŉċǷuӿ˶wֽѼɵŉȕϪԱՄ^bEhwƪ̎ԌȨuË×°Ï¯×Ǹŉȑ‫׏‬ʆ֛ԌγWƢҦrtFbVbE^wStӪŉŠȑwŻՄċǷwϪԱwϮƵдȕТс}wʍϰxkֽəu֦pRF^wϪϢʴ֟bֽѼɵŉȕ‫׏‬ʆ֛wϮƵдȕТс}w̜tʍϰƢҦʓš˄ZjEʭGx^q 2 ŉȑӪŉŻՄċǷwֽѼɵŉȕϪԱwϮƵдȕEϡuҮдȕТс}wʍϰƢҦʓ͠ѩbpXjF2 ŉȑӪŉŻՄuŸTE Þ§¶ƂƨϠwÛ Þ§ÛEӪŉԀӂǊʅEhbp
ŉъù‫נ‬ԦΓЇϮ‫׬‬Second Harmonic Generation, SHG‫׭‬tsѺƨЋuŦϰbEѫҥœǷuU\ŠȑwŽʡѫҥwϮϬȕЋʍѐtswԑγԚpXjFjՠɝEֽѼɵÕËÛ‫׏‬ʆ֛qQ
 CARS‫׬‬Coherent Anti-Stokes Raman Scattering‫׭‬ϰRj;ŠȑwֽÕÆ×ƢԇƂԚEիə
wŠ˳ǟ‫ח‬bjÙÞÛѫҥuȋE3 ͨŅǟ‫ח‬bjѫҥִǌuURp;wընƢԇƂd^ruʬŷbpXjFϪǕE^̜uЇȽ`fEѫҥEhbpѫҥǷт֠w͛խѷˉbj
Үѭ҇uURp;ŠȑwŽXˏT^rԚpRF̫ԪρqxE^wՠɝwԚ

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fE½ÎÞ§ÛТс}wË×°Ï¯×Ǹŉȑ‫׏‬ʆ֛wʍϰwԚunRp_ѬĆdF― 55 ―

S2-2
Ɖ±WZæÝ'03

ľŌ:hrJpC%ĕğ+(ŬđImaging of iPS cells using quantum-nano materials for regenerative medicine
BεɊ ƍ 1,21ƫơȼǹȕ ǹȕ֧ɌȕТсд ϮƵŠȑɌȕȯˮE

2ƫơȼǹȕ ňш·»½´½¨ТсªÛ®Þ
BHiroshi Yukawa 1,2

1

Department of Biomolecular Engineering, Graduate School of Engineering, Nagoya University
2

Research Center for Advanced Nanobiodevices, Nagoya UniversityŕϮƅЅwȘŎʓ˂ībE΍Ѕż̻̠ǹ֦uɮXşdjuxEи͔ʀwɟѫҥŕϮѫҥwϮĜœŽʡͬЧuʹ˝Ýԗ˻dʋԃWQFbVbE^quҺɡʍϰ`pRϵŃԗ˻ʸӱxѭ҇ÝҹǈȬԱrbj

wWrsqQEѫҥȬԱrbjÎÞ§Ûԗ˻ʸӱwЧхWʒžwԥ‫׍‬rtmpRF
ʭGxE֏ȑ¤©ż̻uǠoZֽəuńjŉȕϡʓ‫׬‬Յ‫נ‬ўѫEՅ‫נ‬ʠɥEՅ֜ȭƵEЕºEĚ¢¨µ‫׭‬VիĬÝ̋Ń‫׬‬4KÝ8K ´¨ÄØ‫׭‬Š֎uURp̀uȞϰƂ`pR֏ȑ¶±µ‫׬‬Quantum Dots: QDs‫̀׭‬uҜҹw MRI խɹűrbpҺɡʍϰ`pRńjШͽϡʓ̢dШʓ·»ћȑ‫׬‬Magnetic Nanoparticles‫׭‬ьw֏ȑ·»̰˹uΔБbEŕϮƅЅuU\и͔ɟѫҥ in vivo ÎÞ§ÛuƞѭqXj 1‫ױ‬4‫׭‬F̫ʳΒxEɟѫҥŕϮѫҥи͔dŕϮƅЅw˶Ǹw‫׈‬ǞuʍϰȽ֟WƢҦqQE^qä̈qQmjи͔ʀwɟѫҥÝŕϮѫҥwϮĜœŽʡ̈VubnnQ 5‫ױ‬7‫׭‬F̫¦ÛÊ§ÍqxE^qЧхbpXj֏ȑ·»̰˹u iPS ѫҥÎÞ§ÛʸӱuŸTE̠˼wʬ̻rbpEAMED Vwˬ˟uŕϮƅЅȞϪ˅ϑº±µÚÞÄÙÕÍʸӱ֟Їİťԥ‫׍‬uURpƞѭqXjEŕϮƅЅwҺɡТсհňϮ˽rwŐƪТсʬ̻
unRp ѬĆdʊѓqQFMƗғ˸ϥN
1)

Yukawa H. et al., Adv. Drug Deliv. Rev., 2015; 95: 2-14.

2)

Yukawa H. et al., Anal. Chem., 2017; 89: 2671-2681.

3)

Yukawa H. et al., Anal. Sci., 2018; 34(5): 525-532

4)

Yukawa H. et al., Nanoscale. 2016; 8(10): 5435-5440.

5)

Yukawa H. et al., Sci. Rep., 2017; 7: 40047.

6)

Yukawa H. et al., Sci. Rep., 2017; 7(1): 8447

7)

Yukawa H. et al., J. Surg. Res., 2018; 227: 17-27.

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S2-3
ïĎ:hrJpC'3űŉ

ËŹŮ®ř

őļ(Ė

Application of super-photostable near Infrared dye for plant imaging
BěӥӁſ 1EǸǄͬΕ 11ƫơȼǹȕµÕÛ¨ÂÞË³ÃϮƵŠȑТсʱ
BYoshikatsu Sato1, Masayasu Taki1

1

Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University͔ϠǗâքwǸZwѫҥxEѻӂ͔Ϡϡ̢w×ºÕqQӚѻĜƭF͔Ϡѫҥ̰˹rbjӪŉÎÞ§ÛqxEӚѻĜœwŉƨʬӂѨ‫׬‬ÙÙÂ×‫׭‬xbybyƒĆtȓǕut
FÙÙÂ×xƢԇŉ‫׈‬Ǟd~pwΓ֜qŻՄ`E670-680 nm ĉՠÁÞuɲRӪŉ˯nVqQFÙÙÂ×r͟ЋӪŉŠȑrwŠֶunRpxEռštӪŉÂ×®ÞuѪǷѼVѻӂŉqŻՄ`ӪŉӂѨu֡bpxE͟ЋӪŉŠȑww͕şW͚vƢҦqQ
FbVbEŽϠѫҥwӪŉÎÞ§Ûq΃ϰ`ՂӂŉqŻՄ`ӂѨxEƌѤu½ÖÂ×®Þk\q͟ЋŠȑwwӪŉƞʃd^rxǍַqQEÙÙÂ×ӪŉrwŠ
ֶux¨Çµ×ÎÞ§ÛͦҦ̢d‫נ‬ĥt‫׏‬ʆ֛¦¨³ÍWʋԃqQmjFՠɝqxEϮѫҥœqwÙÙÂ×wӪŉȭƵwР`ŦϰbpE¾×¨ŻՄʀußȝwղɫ̎֠ԕ\pVӪŉ¦·×ƞʃd®Í¡ÞµÎÞ§ÛΒϰRp͟ЋŠȑwӪŉżϨӁZ
ˁşd^rƢҦutmjWE^w˽Β_Zßքw‫׏‬ʆ֛¦¨³ÍqbVոʬqXtRFß˽ʭGxEТсҔWĚ¢¨µqōʳƢҦqQEӪŉÎÞ§ÛuͦҦʓrˆɱʓjdӪŉŠȑw֟ЇuƞѭqRF^quՅԎŃÎÞ§Ûuʋ‫׆‬tɲRŻՄŉuҕTՅҕŉʓӪŉӂѨ‫׬‬PB430‫׭‬ts֟ЇbE_Z̠ՠEΨքÎÞ§ÛƢҦudՅҕŉʓՠՂǷӪŉӂѨ‫׬‬PREX 710‫׭‬w֟Їu ʬŷbǤƱbj 1, 2)F^wТсնкqʭGxEPREX 710
W͔ϠӪŉÎÞ§Ûu ֽəu̢żqQ^ruͽoRjFPREX 710 wƮƝÁÞΓ֜xÙÙÂ×uƮƝWrstRՠՂǷ‫׈‬ǞuQjEռštӪŉÂ×®Þª±µ‫״‬nqÙÙÂ×ӪŉrwŠֶȞϪqXwqQFjEPREX 710 x͔ϠÎÞ§ÛuU\
Ë×°ÕÞÎÞ§Ûwɚˆɱ`fk\qtZEϮĜընʓw‫נ‬RΓ֜wŻՄŉϰRjŉ͸ʓwǀ‫̫׍‬ՁЋuǊրqXF`uEPREX 710 wǔĲЋtҕŉʓxEʬ֜լɥ
WղRTu֜̎֠ԌȨW΂͔ϠwӪŉÕÃÎÞ§ÛƢҦudŗɾ`F
̫ԪρqxEíuՅҕŉʓՠՂǷӪŉӂѨ‫׬‬PREX 710‫׭‬w͔ϠÎÞ§Û}w̢żʓunRp͔ϠѫҥǮ̿ӂĢuѬĆdF1) Chenguang Wang, Masayasu Taki*, Yoshikatsu Sato*, Aiko Fukazawa*, Tetsuya Higashiyama,
Shigehiro Yamaguchi* (2017) A Super-Photostable Phosphole-Based Dye for Multiple-Acquisition
STED Imaging J. Am. Chem. Soc., 139, 10374-10381.
2) Marek Grzybowski, Masayasu Taki*, Kieko Senda, Yoshikatsu Sato, Tetsuro Ariyoshi, Yasushi Okada,
Ryosuke Kawakami, Takeshi Imamura, and Shigehiro Yamaguchi* (2018) A Highly Photostable Nearinfrared Labeling Agent Based on a Phospha-rhodamine Enables Long-term and Deep Imaging. Angew.
Chem. Int. Ed. in press.

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S2-4
Bioluminescent technology for visualization of biological functions
BTakeharu Nagai
1

1

The Institute of Scientific and Industrial Research, Osaka university.

Fluorescent proteins are an indispensable tool for live imaging of cells and cell structures. But the requirement
for external illumination definitely precludes its universal application because it can induce problems
including photobleaching, photodamage and the unintended activation of other light-responsive proteins.
Bioluminescence caused by chemical reaction by luciferase is an alternative to fluorescence because it does
not require an excitation light. One big problem in the application of luciferase to bioimaging was dimbrightness and lack of color variation. To overcome this drawback, my laboratory developed brightbioluminescent proteins (Nano-lantern series) by hybrid of a luciferase with various color variant offluorescent proteins with very efficient BRET (bioluminescence resonance energy transfer), enabling six
colors bioluminescence imaging of subcellular structures as well as single biomolecular complex such as
clathrin coated pit in living cells. In addition, we developed Ca2+, cAMP, ATP and membrane voltage
indicators, thereby we could perform imaging not only long-term and fast Ca2+ dynamics in cardiomyocyte
without any physiological perturbations but also ATP production and consumption in chloroplast of plant(Arabidopsis thaliana) leaf where conducting fluorescence imaging is difficult because of photosensitivity.
One notable application of this imaging modality is simultaneous use with multi-color optogenetics to control
protein and cellular functions with light, which is now essential technique for biology. Furthermore, we
recently succeeded to develop a bimodal bioluminescent indicator which is useful for spatiotemporallyscalable imaging. The bioluminescent probes will revolutionize conventional bioimaging by allowing
visualization of biological phenomena not seen before at the single-cell, organ, and whole-body level.
References
1. Inagaki S et al. In vivo brain activity imaging of interactively locomoting mice. bioRxiv.
doi: https://doi.org/10.1101/203422
2. Suzuki K and Nagai T. Recent progress in expanding the chemiluminescent toolbox for bioimaging. Curr.
Opin. Biotechnol., 48, 135-141, 2017.
3. Inagaki S, et al. Genetically encoded bioluminescent voltage indicator for multi-purpose use in wide range of
bioimaging. Sci. Rep., 7, 42398, 2017.
4. Suzuki K. et al. Five colour variants of bright luminescent protein for real-time multicolour bioimaging. Nat.
Commun., 7, 13718, 2016.
5. Takai A. et al. Expanded palette of Nano-lantern for real-time multi-color luminescence imaging. Proc. Natl.
Acad. Sci. USA, 112, 4352-4356, 2015
6. Saito K. et al.. Luminescent protein for high-speed single-cell and whole-body imaging. Nat. Commun., 3,1262, 2012

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S3-1
超解像光学顕微鏡による繊維状アクチンのイメージング

Filamentous actin observed with superresolution microscopy.
○田中みなみ 1.2、加藤薫 1
1

産業技術総合研究所バイオメディカル研究部門、2 筑波大学大学院生命環境科学研究科○Minami Tanaka,1,2 Kaoru Katoh1
1

Bio Med. Res. Inst., AIST, 2Grad. Sch. Life & Env. Sci., Univ. Tsukuba

光学顕微鏡の分解能は 200nm 程度であり、光とレンズだけでは、この壁を越えることは理論的に不可能である。ところが、光とレンズに、さらに別の要素（「光の照明パターン」「画像処理」、「蛍光色素の性質」「特殊な光学系」等）を加えると分解能の限界を超えることができる（超解像）。
現在では、光の波長以下の数十 nm の構造が観察可能になり、バイオメディカル分野への広がりが期待されている。
繊維状アクチンは非常に細かな線維である。数本の束でも、光学顕微鏡での観察は難しく、電子顕微鏡観察が必須とされてきた。特に、ラメリポーディア領域のアクチンの網目は、電子顕微鏡でなければ見えないとされてきた。ところが、超解像顕微鏡が実用化された結果、これまでよりも容易に、生きたままで、アクチン線維が観察できる様になった。この講演では、神経成長円錐等を例に、従来の顕微鏡と超解像でのアクチンの観察について述べる。SIM では分解能は120-130nm 程度だが、動態観察が可能であり、STED では固定試料になるが、50nm 以下の分解能での観察ができた。そこで、2 カメラタイプの SIM を使用して、アクチンとアクチン関連タンパク質（ファシン）の動的な共局在の変化を、10nm 以下の精度で完全に同時刻に記録し、動画で検討した。その結果、外液への薬物投与により、ファシンがリン酸化されると、アクチンから解離し、それに伴ってアクチン線維の方向が変わることを見いだした。2 カメラ SIM の分解能の限界のために、ファシンの解離後のアクチン繊維の方向を正確に見積もることが難しかった。そこで、ファシン解離後に固定し、STED で繊維の方向を観察し、確かにファシンの解離により、繊維の方向が変わることを確認した。このように、薬物投与により、ファシンを解離させ、アクチン束を選択的に壊すことができる様になった。
次に、アクチン束が、細胞の弾性に関係すると考え、ファシ
ンを解離させアクチン束の消失させる前後で、AFM によるヤング率の計測を行った。その結果、ファシンにより作られるアクチン束は、細胞のヤング率に３０％程度寄与していることが分かった。
図

STED 観察した神経成長円錐のアクチンの網目

― 60 ―

S3-3
ľŌĄÁ(:hrJpCš·%Û~'03ĄÁĕĎ²

Imaging and manipulation of temperature in single living cells for thermal biology
BɂքɯǠ 1EӀΘ‫נ‬ʌ 11̵āǹȕǹȕ֧ӤȕѠТсд

BKohki Okabe1 and Takashi Funatsu1
1

Graduate School of Pharmaceutical Sciences, The University of TokyoβɥxEĊԫÖ©ÍrRmjϮϬͦҦu֍ǹtɹׂåTpRFѫҥØÆ×qβɥr֡ծdϪԱrbpxEŀȡʓ‫נ‬βuȬd¿Þµ¦Ô±ʍѐѫҥǷքwβɥǵƂѫҥœք}ʛǤĔոdβɥʠƟʓ°Ðº×‫׬‬TRP °Ðº×‫׭‬WПpRWE^qѫҥœքwβɥwǵŽhwʞҍunRpx̩ПqQmjF^quʭGxϮѫҥœuռʍƢҦtӪŉʓÊÖËÞβɥªÛ¤Þ‫׬‬Fluorescent polymeric thermometer, FPT‫֟׭‬ЇbE^wʍѐȝ֏ЋӪŉÎÞ§ÛΒu͕şd^rqϮѫҥœwβɥγȝϮѫҥwβɥÎÞ§ÛոʬbjF
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ҦqQF̫ΒϰRj͕ԒuEūψuʍѐbjѫҥœβɥwâ̆EȝəϢʡuU\ѫҥœβɥwäǙßtŠɕЇԅbjFѫҥœβɥǵƂWѫҥȳǈȜwͦҦѫҥÆÛµrΨZ֡ծd^rVEβɥWѫҥwͦҦΚʓuΨZ֡ådǋȑrbpΔБִpRß˽qE
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̫ΒϰRpѫҥœȹʱuU\ЇϚwϮϬͦҦԎ̈djEѫҥW¨µØ¨Ɵ\j֯u
RNA W¨µØ¨‫׌‬ћɵʬdϪԱuʍϰbjF^w͕ԒqxEIR ØÞ¥ÞϰRjѫҥœȹʱwŸϚuEœǕʓ RNA WլVu‫׌‬ћɵʬd^rЇԅbjFjE¨µØ¨‫׌‬ћɵʬ̎wβɥÎÞ§Ûьwѯ̻rƨfrEѫҥœȹʱwЇϚW mRNA wßնЋŝִԡՄbpRøЇԅbjF^w¨µØ¨‫׌‬ћɵʬxϡȝw mRNA wß̎ЋґԖԦѕ˂mpUEѫҥw¨µØ¨ʍѐͦ͛uְֽȡʓβɥǵƂuʛǤĔոIβɥ¦·ÖÛJWȓǕdøWЪƽ`jFβɥxмGwϮĜ‫נ‬ŠȑuյZɹׂåT^rVEβɥ¦·ÖÛxѫҥͦҦЇϪuɠіuԴϥd˼Ԇ͚ʏqQV

btRFąʀEѫҥœβɥWѫҥwϢʡͦҦƜ̋d¾ÕÎÞ®rbpЇȽd^rW̧ɾ`F― 61 ―

S3-4?mAYk(ÄÎÇý(ƎĠDesigning Organelle Morphology at willBȠ̫Ɇƣ 1EɅ֎Ą 11яΓǹȕ ƅȕƅЅѠ œŠΑĊԫÝџȸЀœдBTakafumi Miyamoto1, Hitoshi Shimano 1

1

Department of Internal Medicine (Endocrinology and Metabolism), University of Tsukuba

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Ǌx iCOM wϪϢrąʀwȽ֟unRp_ѬĆ`fpRjkXjRrғTpRF― 62 ―

S3-5
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BYasushi Tamura
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― 63 ―

S3-6
ľŌíqBoeQpÎ(ĕľŌ:hrJpC

Imaging nuclear and chromatin dynamics in living cells
Ḇ̨ Ț 11̵āɌ͘ǹȕдȕʸӱŴʬТс֧ѫҥŨʄɌȕТсªÛ®Þ
BHiroshi Kimura1

1

Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology¡»ÍâwտĔʛǤWEswSuѷˉEӿӽEЇϪdwVErRSǀ‫׍‬Ԏ̈d^rxE
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― 64 ―

S4-1
ğ'3^>UXBK(ƀøÑŚÜ×IKSg+(ÊĖ

Recent advances in photonics for image-guided surgery
B‫̶נ‬ƻփāօɤхƅдǹȕƅȕÂµ¸¨ԪɦTetsuro Takamatsu
Department of Medical Photonics, Kyoto Prefectural University of Medicine
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― 65 ―

S4-2
ôōËWZĸ±5Ė6Ó}ŗ(ŗ:hrJpC

Imaging of efficacy of antibody drug for cancer treatment using functional nanoparticles
B͡ϱɞЭ 1Eʇ΀ͬð 1EơχВȑ 2Eê֎ȩ 21̵ƃǹȕǹȕ֧ƅȕѠТсдE2 ¢¸Ì»×®(ͅ)֟Їѳˇ̫ք½ԃѨʸӱ֟Їȟ
BKohsuke Gonda1, Masayuki Tokunaga1,2, Naoko Furusawa,2, Yasushi Nakano,21
2Graduate School of Medicine, Tohoku University,

Bio Advanced Technology Division, Corporate R&D Headquarters, KONICAMINOLTA. INC.

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˶x 730 м‫ב‬ċâuwFmpʼĜƅӤuȬbEIӤżÎ¸©ÍwƢԇƂJIӤżwʗҔȿťwƢԇƂJӰSÎÞ§ÛxEŴӤўȦƅЅ}wʍϰʸӱrbp̧ɾ`pUE¸Þ©W͙p‫נ‬RF̫ԪρqxEdquҺɡʍϰ`pRWʼĜƅӤrbpE (1) ӯєœЍǬ͵ǋȑ (VEGF) wʼĜƅӤ Bevacizumab r(2) ¿µâЍʓǬ͵ǋȑƟȣĜ®Ä 2 (HER2) w
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Bevacizumab wteE˼jtʼӯє˼ϮӤű֟Їw˘հW̧ɾqXFʭGxEϣһw֐·»ћȑ[1]խɹűuϰRj‫נ‬ŠԎҦ X Ѽ CT ÎÞ§ÛumpEֽĦԁVn 3 ͨŅЋuBevacizumab ʻåbj˂WË¨wұЄӯє͛խwǵƂԝѫuԦ~jFhwѯ̻Eʼ VEGF
ӤuȬdҕʓͦ͛wßш̈Vud^ruʬŷbjFՠɝ‫װ‬õWqxEӱŮuϮ͕qWѭ҇wßք˕ƞbEhwѭ҇wԗ˻´Þ®ruӱŮuӤϠЅΒӰREWȳ`ZbpVʳӱӰmjEWuȬdʼWűwż̻ЧVtW΍ЅӰS˽ΒW˾Ӱ`pRFTrastuzumab xEϮ͕wѯ̻ HER2 ֫ʓqQmjʗҔuȬb‫װ‬ӱŮӤϠЅΒwӤrbpġϰ`pRF^w΍ЅΒqxETrastuzumab ռʍȬԱrt
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hwѯ̻E̫˽Βx̀ȓw˽Βqx÷γWǍַqQmjʗҔw Trastuzumab ȁżʓ‫נ‬Чɥqȿťd^ruʬŷbj [2-4]F[1] Nakagawa, T., Gonda, K., et al. Sci. Technol. Adv. Mater. 17, 387-397 (2016)[2] Gonda, K., et al. Sci. Rep. 5, 14322 (2015).
[3[ Miyashita, M., Gonda, K., et al. Cancer Med. 5, 2813-2824 (2016).
[4] Gonda, K., et al. Sci. Rep. 7, 7509 (2017).

― 66 ―

S4-3'03ĕ}:hrJpC

Functional imaging using PETBɂΊвɶбüǹȕ‫נ‬º×ÞƅȕТсªÛ®Þ ϮĜͦҦԎ̸ȕք֝
BHidehiko Okazawa
University of Fukui, Biomedical Imaging Research Center (BIRC), Medical Imaging DivisionÊ§µÙÛ CT‫׬‬PET‫׭‬x 1970 ɝĊêׄu֟Ї`EĈwϵŃ͕̓r͹~pȝ֏ʓuńjϮĜͦҦϵŃʃ^rWƢҦt²Þ×rbpEíuҮʊҹwТсuϰRpXjFbVbE
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ʁGȗƙbxcjF1990 ɝĊʀƈu FDG-PET wī֪ԗЅWԟrEPET Ȳōd˾ԕx‫ג‬ՍЋuǬTEϪǕǑœuQѢ 400 w PET ˾ԕqx FDG-PET/CT êʊuEíuWԗЅwjw͕̓rbpŦϰ`pRF^w͜tѮѿVEßҿЋux PET ͕̓rRSr FDGPET/CT ͕̓w^rˊdrRmjԟԬWQWEՠɝŠȑÎÞ§ÛwЇȽuEĈu ԗ˻uɺхn͜GtƂƨϠW֟Ї`EҺɡʍϰƢҦqQ^r ʁGuϬԎ`SutmjFWԗЅuŦϰqX PET ӤűrbpxE®Û¾ƨʬҦƜ̋dr`[11C]methionine E͆֊Ċԫ°Ì§Û·Þ«‫׬‬TK1‫׭‬ΚʓƜ̋bEǬ͵wˊ͟utr`[18F]fluorothymidine‫׬‬FLT‫׭‬tsEұЄǬ͵ҦƜ̋dµØÞ¤ÞWßҿЋqQWEhwĈu E΍ЅʿʼʓĚ֊
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PET qx¨µÙ¡ÛƟȣĜÎÞ§ÛűrbpϰR[18F] fluoroestradiol‫׬‬FES‫׭‬ŮхҴϡϺЋ®Û¾ՁʼƔwÎÞ§ÛűqQ[68Ga]͟Ԭ prostate specific membrane antigen‫׬‬PMSA‫׭‬tsWΔБ`pRFß˽EPET ֟ЇɴţVíԃt®Þ¡±µr`pXjҮÎÞ§ÛqxEǑœq̠ţuī֪ռʍrtmj 15O ͟Ԭw;ù֊ƂϐѨE֊ѨьuҮӯΛÝ֊ѨĊԫ PET wVEՠɝxÌÙ¶ÎÞ§Û®ÎÞ§ÛrRmjEԟПЁwЀϬŃƜ̋dŠȑÎÞ§ÛẀußҿƂbnnQF̫ԪρqxEhSbj PET ŠȑÎÞ§Û͚ԣdrrɡТсunRpuEҺɡȲōʀ֠ tR̠˼Ǜ PET/MRI ßĜǛӹ҉rhϰRjҺԏ÷ȝqQF― 67 ―

S4-4
5Ėôō:hrJpC(U]RBKTopics of Functional Imaging using MRIBƔϱֳƣ 11ʇɅǹȕƅͯӤȕТсք˯ȰѼƅȕŠ֎
BMasafumi Harada1

1

Department of Radiology, Graduate School of Biomedical Sciences, Tokushima University

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BKazuo Kurokawa, Daisuke Miyashiro, Akihiko Nakano
RIKEN Center for Advanced Photonics

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BYusuke Kato1, Fuyu Ito2, Kazuhiro Takahashi3, Ryuichi Sugamata2, Sumire Kurosawa1, Kazuko Yorita1,
Syoichi Suzuki2, Tomoko Yamamoto2, Shoji Kawachi2, Masakazu Mimaki3, Kazuo Suzuki2, Kiyoshi
Fukui1
1

The Institute for Enzyme Research, Tokushima University, 2 Asia International Institute of Infectious
Disease Control, Teikyo Univ, 3Department of Pediatricts, Teikyo University School of Medicine ԑѓдȕu։Ѩ֡ծТсwƞѭrbpED-Ì»֊֊Ƃ։Ѩ (DAO) wΚʓŨʄǋȑ
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In vivo Observation of Dynamics of Osteoclast Proton Pump Using pH-activatable
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1)

Graduate School of Engineering, 2) Immunology Frontier Research Center, Osaka University‫מ‬ѭ҇qxФ‫מ‬ѫҥu‫מ‬ƮƝr‫מ‬Ӈѫҥu‫מ‬ɵʬW҈ա`Eŕ͛ї`^rq
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pH ϭǫwǵƂ֜̎֠ujդՊd^rqEФ‫מ‬ѫҥÄÙµÛÊÛÄwŽXuĕmj֊ʓ‫׈‬ǞwɵʬÖ×®ÍqˏT^ruʬŷbjF1) T. Kowada, J. Kikuta, A. Kubo, M. Ishii, H. Maeda, S. Mizukami, K. Kikuchi, J. Am. Chem. Soc. 2011,
133, 17772.
2) H. Maeda, T. Kowada, J. Kikuta, M. Furuya, M. Shirazaki, S. Mizukami, M. Ishii, K. Kikuchi, Nat. Chem.
Biol. 2016, 12, 579.
3) J. Kikuta, Y. Wada, T. Kowada, Z. Wang, G. H. Sun-Wada, I. Nishiyama, S. Mizukami, N. Maiya, H.
Yasuda, A. Kumanogoh, K. Kikuchi, R. N. Germain, M. Ishii, J. Clin. Invest. 2013, 123, 866.

― 71 ―

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Fluorescence imaging of intracellular Magnesium ion concentration changesB˼ӥ԰ 1Eɀê‫ ת‬1Ę֒Ȕ΍ 2EǢϱҖƦ 1EɂΠǻփ 11ʥǹϬɌϮƵʛǤE2 ʥǹϬɌʍƂ

BYutaka Shindo1, Ryu Yamanaka1, Koji Suzuki2, Kohji Hotta1, Kotaro Oka1
1

Department of Bioscience and Informatics, Keio University
2

Department of Applied Chemistry, Keio UniversityËº¦ÍÛ‫׬‬Mg2+‫׭‬x×¦ÍÛ‫׬‬Ca2+‫׭‬ré{EϮĜœuȓǕdíԃt 2 ĥ֫ÛqQFCa2+xѫҥœ¦·×rbphwωɥǵƂW֍ԃtʞƳˉmpR^rWɠ
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Three-dimensional structure analysis of b-glucans from Agaricus brasiliensis
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BYoshitaka Matsumura1, Kodai Inoue1, Makoto Suminokura1, Mikako Kubo1, Mariko Demura1, Takayuki
Ichioka1, Yasumasa Morimoto1,Mitsuru Tashiro2, Ken-ichi Ishibashi3, Naohito Ohno3 and Masaki Kojima1
1Sch. of Life Sci. and 3Sch. of Pharm., Tokyo Univ. of Pharm. and Life Sci.
2

Dept. of Chem., Coll. of Sci. and Tech., Meisei Univ.

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ʶmpRXjRF― 76 ―wхĜ͛խԎ

― 77 ―

P-4ĪËWZ`or_'03@mI;gÊĵ¦Calcium-dependent fMRI using a magnetic nanoprobe
1

Bɂϱ̕ EBenjamin B. Bartelle2ENan Li2EVincent Breton-Provencher3,4EJiyoung J. Lee2E
Elisenda Rodriguez2EJames Melican2EMriganka Sur3,4EAlan Jasanoff 2,3,51ϯ͘ʸӱѺƨТсʱĸɨɌȕТсք֝E2MIT ϮϠɌȕдE3MIT ҮԟПдȕдE
4

MIT ÁÚÞȕҏԓʨТсʱE5MIT ƔȑŶɌȕд

BSatoshi Okada1, Benjamin B. Bartelle2, Nan Li2, Vincent Breton-Provencher3,4, Jiyoung J. Lee2,
Elisenda Rodriguez2, James Melican2, Mriganka Sur3,4, Alan Jasanoff 2,3,5
1
2

Health Research Institute, National Institute of Advanced Industrial Science and Technology,

Department of Biological Engineering, 3Brain & Cognitive Sciences, 4Picower Institute for Learning& Memory, 5Nuclear Science & Engineering, Massachusetts Institute of Technology ×¦ÍÛ‫׬‬Ca2+‫׭‬xEѫҥœǷuURp͜GtʛǤĔոu֡ådªÛ¶Î±ªÛ§ÐÞqQFЮѮĔոϠՁw˯ş̎uxEָęĤȓʓ×¦Í°Ðº×ĆbpѫҥǷVœ
mpE
ѫҥǷ Ca2+ŽʡxEӯΥŽʡǠudʂ̴w functional MRI‫׬‬fMRI‫׭‬}r Ca2+WΛōdF
uĊЮѮΚŽÎÞ§ÛwВ˗Ћtˊ͟rtʃFbVbEŉȕЋʸӱuԌȨʳΒWЧх`pRѫҥœ Ca2+rxϺtEѫҥǷ Ca2+wԌȨʳΒx֦pRF
 h^qѫҥǷ Ca2+ÄÙÞÃrbpEÖÛҧՁqӵ‫־‬Į‫ז‬bjՅəШʓ֊Ƃ֓·»ћȑ‫׬‬SPIO‫׭‬r×¦Íѯƨ®Û¾ՁqQ¦·Äµ®ÌÛΪƨbjEmagnetic calcium-responsive
nanoparticle‫׬‬MaCaReNa‫֟׭‬ЇbjF̫ÄÙÞÃxEѫҥǷ Ca2+wωɥǵŽіǎqE¦·Äµ®
ÌÛWÖÛҧՁĆbp SPIO Õ¨®ÞƂdSuԕԑ`pRFSPIO xŝִdrEՠĽuȓǕd;Šȑw 1H-NMR ͢ѾƶĩհdjEMaCaReNa ÄÙÞÃumpѫҥǷ
Ca2+ Žʡ T2 ɲԦ MRI qµÕ±ÛƢҦrtFăɌҮҫ‫ן‬ΥêqwͦҦԙĥwѯ̻E
MaCaReNa ÄÙÞÃxEѫҥǷ Ca2+w͕şuռbjԋƶʓ̢bpR^rWVmjF
 ͨuEÄÙÞÃϮXjÕ±µҮѼ̳ĜuʻåbjʀEƪքęǩƂÖÍqҭŠ͙ūψbCa2+ʍѐǛ fMRI ԚjFūψ֟ȋʀEūψքęƲ՛wĬƥɲɥxѢ 20%â̆bEūψķͫV
Ѣ 5 ŠqÆÞ¨ÕÛ}rʰmjFūψӿ˶Ǌ҈աbp ƪ͜wǵƂWԅj^rVEÄÙÞÃWҮœqƢէЋuͦҦd^rWVmjFß˽qEº³Ã¢ÛµÙÞ×ÄÙÞ

ÃrļūψqxĬƥǵƂxԌȨ`tVmjFjEҾȅʓЮѮĔոϠՁqQ×®ÌÛ֊wʻåuURpEǩƂÖÍūψrƪ͜wĬƥǵƂWԌȨ`jF`uEǤֈѠǊՋqQœĺŮҮ̲ָ͙ūψbj֯wѼ̳ĜwЮѮЇώEеØÆ×qԑγd^r ƢҦqQmjF
 ċâEMaCaReNa ÄÙÞÃϰRpEÏ´×ŽϠwҮœq Ca2+ʍѐǛ fMRI uţpʬŷbjF̫ÄÙÞÃϰRjҮͦҦÎÞ§ÛuEąʀwЮѮдȕТсWǹRuհȽdøW̧ɾ`Fj̫ÄÙÞÃxEϮXjҮœqͦҦdţpw SPIO ÄÙÞÃqQEąʀwÎÞ§Û̰˹wԕԑ֟ЇuURp֍ԃtշ͟rtʃF― 78 ―

P-5
ƞž AFM '03 2 !(Ě&3ŵĭÿËVh:p5å3ĺŵĭƅļ(ġñſŢé

Dynamical structural analysis for glycosyltransferase with two active sites using
high-speed AFMBƩϱ̄ɖ 1EО̨Țƶ 1Eα՛ǹՕ EȳԳлО EȗɅ ĸ 3Ḙɀͬ̈ 3EœͥԸð 2,4EŸӥ̏ß 1,41ƫơȼɔхǹȕӤȕքE2 ƫơȼǹȕǹȕ֧ϬȕТсдE3 āօǹȕӿƨƔȑŶдȕТсʱE4 һϕдȕТсͦ͛ϮƵŴʬ˖сªÛ®Þ
1

BSaki Yoshida , Hirokazu Yagi1, Hiroki Watanabe2, Toshiya Kozai2, Ken Morishima3, Masaaki
Sugiyama3, Takayuki Uchihashi2, and Koichi Kato1,4
1

Faculty of Pharmaceutical Sciences, Nagoya City University, 2Faculty of Science, Nagoya University,
3

Institute for Integrated Radiation and Nuclear Science, Kyoto University, 4 Explatory

Research Center on Life and Living Systems, National Institutes of Natural Sciencesџ֚x®Û¾ՁҧՁĮ‫ז‬bE͜GtϮƵͦҦŨʄbpRFџ֚x¡»ÍuВ˗Ũʄ`pUeEhwϮƨʬ˂mpRwWџՐи։ѨqQFĢTyE¿µqx 200 м‫ב‬ՠZwџՐи։ѨWƪȝ`pRWEhwǸZWƌßwԏȏ¶ÎÛ̢d 2 ǛҶ®Û¾Ձq
QF^w։ѨWƨʬdџ֚wм‫ב‬uʍcpϡϺt։ѨӿƨĜɵʬbEżϨwӁRџ֚ƨʬ˂mpR^rWғTpRFß˽qE2 џw҈աb͛խƨʬdџՐи։Ѩwêuxƌßм‫ב‬w։Ѩq 2 nwџՐиΚʓքę̢d8½ÂÛ¦Ô·×9t։ѨWйqx
QWȓǕbpRWE^SbjÓ¸Þt։Ѩuџ֚Ė֜wԝѫtÎ¸©ÍẍVu`pRtRFǹҲӕwӒҶw͛ʬʬŠqQ¢Û¶Ù°Ûx×ÙÛ֊‫׬‬GlcA‫׭‬r Nª°×Õµ¤ÌÛ‫׬‬GlaNAc‫׭‬w 2 џ҈աb͛խ̢bpUE2 nwՐиΚʓ̢d¢Û¶Ù°Ûƨʬ։ѨumpϮƨʬW˂pRFh^q̫ТсqxǹҲӕw K4 ӕмϲ̴w¢Û¶Ù°Ûƨʬ։ѨqQ K4CP uЙБbE̫։Ѩuџ֚wĖ֜Î¸©ÍԎ̈djE‫נ‬լƔȑ֠Ŷ‫׏‬ʆ֛AFMϰRjŽЋ͛խԎ̸ӰmjFՅպʊŠ̸uλΥêw K4CP x 0.2 mg/mL ċâqx 2 ֏Ĝɵʬd

wwEAFM wγȝωɥqQ 0.05 mg/mL qxƌ֏Ĝɵʬd^rẄVrtmjFK4CP w‫נ‬լ AFM uγȝqxEƧ¶ÎÛuȬʍbpRrғTՕϑ 2 nWՠ˗bpRŃWԌγ`E^
wՕϑWˠŽbpR͜ȑԌȨd^ruʬŷbjF^Sbj 2 ՕϑWˠŽbpR¯ÛÆ
×Ǜw K4CP ŠȑҌuŸTpEhɚWϤZŽXWͲstR͖ŔǛwŠȑҌԌȨ`jF`uEџģåĜr¢Û¶Ù°Û 6 џǠՁrbpŸT^rqEĖ֜bjџ֚rғT¿ÏϢw͛խĜЧԟd^rWqXjFjEǠՁwΫŸu¯ÛÆ×ǛwŠȑwųƨWǬ
Ÿbj^rVǠՁrwѯƨW K4CP w¢ÛÂÎÞ¦ÔÛuɹׂƙd^rẄVutm
jF
ċâE;λΥêw K4CP x 2 nw¶ÎÛW˗ՠrԎֶ҈աd^rqE2 nwΚʓքęWт֠Ћu˗ՠbEџ֚wÖÁÞµ͛խwĖ֜WżϨЋuӰpRƢҦʓWғTF― 79 ―

P-6ĥŔėèbCm@p

Ɖ}(Ĳ}ñſŢé

Conformational analyses of trimer form of b-glucans from fungusBǘϱǅĂ, ê̱Њӄ, ȫ̹̯Ϭ‫װ‬Έͮ, ̶̱ҍ֬, ȳɅ̵ͬͣӤǹ:ϮƵ
BKyosuke Sakata, Momoka Nakamura, Anri Terabayashi, Ayumu Oki, Yoshitaka Matsumura and Masaki
KojimaSch. of Life Sci., Tokyo Univ. of Pharm. and Life Sci.
 b×Ûx×¢Þ¨W2Ö¢¦¶ѯƨqntWmjǸџqQ‫»װ‬¢tsИӕ‫ב‬wѫҥǮ͛ʬbpRFhwŋϾğϰĆbpEʼұЄż̻tswϮϬΚʓЪbEĸɨǬհwSTq̢ϰtϠՁqQFĢTyE¨¿Ù®

ϲ̴wb×ÛqQ¦­ÂÕÛxʼWű¬¸ÂÕÛrbpԟƢ`pRF Иӕump2×Ûwßͨ͛խx͜GqQE¦­ÂÕÛx2-1,3 ѯƨwí֚u×¢Þ¨ƌџW2-1,6 ѯƨq̼ŠVbpUE¼Õ® ȾwßмqQÖ¨‫׬‬Agaricus‫׭‬ϲ̴w2×Ûx2-1,6 ѯƨwí֚u2-1,3 ѯƨwŠ̼̢dFj¦­ÂÕÛx;λʓq 3֏Ĝɵʬbpf͛խr^rW X Ѽѯ̔Ԏ̸uԎ̈`pR[‫]״‬WEĈwИӕw
2×ÛxßҿuַλʓqхĜ͛խʓ̢drRSǤƱ

ä̈tϑWǸRF`u¦­ÂÕÛxƌ֏ĜqϮϬΚ

QEĈwИӕ2×Û‫׬‬ØÛ°·ÛEÞ¶ÕÛ‫׭‬ƌ֏Ĝqf͛խɵʬd^rWǐĜ NMR uЪƽ`pRF ʭGx^quÖ¨b×ÛuȬbpEX ѼλΥ˳ô‫׬‬SAXS‫׭‬ENMREŠȑŽŶȕ¦ÌÒØÞ¦ÔÛuEhwßͨ͛խWb-1,6 ѯƨwí֚rb-1,3 ѯƨwŠ̼VʬE;λΥêq 3 ֏Ĝjxƌ֏ĜrbpȓǕd^r̈Vubj[2]FjÖ¨b×ÛÛ§¯×ÛxEɜӳϢʡuURpƌ֏Ĝqf͛խɵʬd^r

Ъ`jF̫Тсqx

ѯ̔͛խ[3]ǠuEмGwb×Û 3 ֏ĜqŠȑŽŶȕ¦ÌÒØÞ¦ÔÛӰREhwхĜ͛խԩϠʓ÷γbpEƌ֏Ĝrw͹ՒԎ̸ӰmjF[1] Kony et al., Biophys. J. 93, 442 (2007)[2] ̶̱EȳɅI2×ÛwǠЩТсrʍϰÝŦϰwŽƬ ъ 5 чJ‫¦׬‬ÞÍ¦Þşϝ‫׭‬2018[3] Deslandes et al., Macromolecules 13, 1466 (1980)― 80 ―

― 81 ―

― 82 ―

P-9
ƥƉ±VRU5ĖĭïÀľŌqěľŌƏ interaction ř:hrJpCƦ

‫׿‬Fluorescence imaging of transplanted stem cells to immune cells

interaction using quantum dots‫؀‬Hƃ̱̏ǹ ,εɊƍ ,ěӥ ƶв ,̢̫ Пȑ ,ȳ֎Ʌ ǹĆ ,⁴,СɊ ƻó ,‫ך‬ǥ ǇĬ , ,⁴,⁵
ƫơȼǹȕǹȕ֧ ɌȕТсд, ňш؎؏ؐؒ؈؉‫ؒؐؒ؍‬؈؊Тс؋ؑ،؇, ƅȕѠТсд,⁴̴̩ЬēŴխͦ͛,⁵ϯ͘ʸӱѺƨТсʱ ĸɨɌȕТсք֝
HKoudai Kitamura , Hiroshi Yukawa , Kazuhide Sato , Tomoko Arimoto , Daisuke Onoshima ⁴,
Tetsuya Ishikawa , Yoshinobu Baba ⁴⁵
Graduate School of Engineering, Nagoya University, Advanced Nanobiodevice Research Center , Graduate School of Medicine , ⁴Future Society
Creation Organization , ⁵National Institute of Advanced Industrial Science and Technology, Health Engineering Research Division̫˸MБЋNŕϮƅЅxϏЁϢʡwʗҔȬԱuȞ˾`^rWǸZEŕϮƅЅwȘŎʓ΍Ѕż̻ƬâuƬ\pEϏЁu֡ådWѫҥŋϾѫҥWи͔ɟѫҥuƙdѫҥ֠ ineraction ϬԎd^rW͙p֍ԃqQFʭGxE^qu̠ňшӪŉ·»̰˹w֏ȑ¶±µ(QDs)ϰ
RpҧҞϲ̴ɟѫҥ mASCs wÕÆ×ƂʳΒƙ{ и͔ʀw in vivo ÎÞ§Ûʸӱ֟Їbp
XjF̫ТсqxE˼ju QDs uWѫҥrŋϾѫҥwÕÆÖÛʳΒEƙ{ in vivo ӪŉÎÞ§Ûʸӱ͛їbEѫҥ֠ interaction wԎ̈uƞѭkF
M˽ΒN¿µҠҥǠɣâЍҴІѫҥ A549 ѫҥr BALB/c Ë¨˕ִbjËÙÂÞ§
QDs ÕÆÖÛbEŐϔϑ‫׏‬ʆ֛uԌȨrÕÆÖÛżϨwԙĥӰmjFjEQDs ÕÆ×Ƃ A549 ѫҥ BALB/c-nu ¹Þ¶Ë¨ 6 կ‫ש‬uЍã˗мbp˂ІË¨ğӽbjFhw
ʀEQDs ÕÆ×ƂËÙÂÞ§˗мbEin vivo ӪŉÎÞ§Ûӹ҉(IVIS Lumina K)qԌȨd^rqEA549 ѫҥrËÙÂÞ§֠wГúğϰԙĥbjF`u A549 ѫҥrËÙÂÞ§wŐǟ‫ח‬EC57BL/6J Ë¨V˕ƞbj mASCs rËÙÂÞ§wŐǟ‫ח‬Õ¨ÉµÍâqӰREӪŉÎÞ§Ûuѫҥ֠ interaction wԙĥӰmjF
Mѯ̻NQDs  R8 r̠ռ͹qΪƨd^rqEA549 ѫҥEËÙÂÞ§u‫נ‬żϨuȲō`^rŐϔϑ‫׏‬ʆ֛qԌȨbE‫נ‬żϨÕÆÖÛWƢҦqQ^rЧԟbjFjEQDs ÕÆ×Ƃ A549 ѫҥEËÙÂÞ§wË¨ϮĜuU\ in vivo ӪŉÎÞ§ÛuʬŷbjF`uEWѫҥÝŋϾѫҥ֠rɟѫҥÝŋϾѫҥ֠wѫҥ֠ interaction  in vitro qӪŉÎÞ§Ûd^ruʬŷbjF^u֏ȑ¶±µÎÞ§ÛʸӱϰRp 1 ѫҥØÆ×winteraction ӪŉÎÞ§ÛʳΒ͛їbjF̫ТсǠuEin vivo uU\ѫҥ֠ interaction w
ԙĥհF― 83 ―

P-10
Intracellular Ca2+ dynamics in guinea pig-pulmonary vein cardiomyocytes
BYusuke Tanaka, Tamano Ohmori, Shogo Hamaguchi, Iyuki Namekata, Hikaru Tanaka
Department of Pharmacology, Toho University Faculty of Pharmaceutical Sciences
The pulmonary vein contains a myocardial layer which has automaticity, the ability to generatespontaneous action potentials. The action potential originating in the pulmonary vein, when propagated tothe adjacent atrial myocardium, can be the trigger for atrial fibrillation. Thus, the pulmonary vein
myocardium is receiving attention as a therapeutic target for atrial fibrillation. Electrophysiological andpharmacological studies in our laboratory have shown that the reduced repolarizing membrane currents of
pulmonary vein cardiomyocytes play a permissive role in the generation of action potentials (Tsuneoka et al.,2017). Further, inhibition of spontaneous activity by ryanodine and SEA0400, agents which inhibit Ca2+
release from the sarcoplasmic reticulum and transsarcolemmal Ca2+ extrusion by the Na+-Ca2+ exchanger,
respectively, suggested the intracellular Ca2+-dependence of the automaticity. We also found thatneurohumoral influence such as noradrenaline and angiotensin II enhances automaticity (Irie et al., 2017)
In the present study, the intracellular Ca2+ dynamics of guinea pig pulmonary vein cardiomyocytes werevisualized with confocal microscopy. Isolated pulmonary vein cardiomyocytes were loaded with the Ca2+
sensitive fluoprobes fluo-4 and imaged at millisecond intervals with Nikon A1R. The pulmonary vein
cardiomyocytes were about 100µm in length and 15µm in width. Most of the cardiomyocyes lacked a Ttubular system. About one third of the cells showed spontaneous Ca2+ transients, a uniform elevation of Ca2+
throughout the cytoplasm triggered by action potentials. The elevation of Ca2+ began at the subsarcolemmal
region and propagated transversely toward the cell center. Ca2+ in the cell nucleus followed the changes in
the cytoplasm. Most of the cardiomyocytes showed spontaneous Ca2+ sparks, a non-propagating local rise inCa2+ concentration which lasted for about 40msec. Application of angiotensin II markedly increased thenumber and amplitude of Ca2+ sparks; in some cases, Ca2+ waves, a propagating local increase in Ca2+
concentration, were induced. Induction of Ca2+ waves and Ca2+ sparks by angiotensin II was followed bygeneration of Ca2+ transients. Ryanodine inhibited all three Ca2+ types of Ca2+ movements: Ca2+ sparks, Ca2+
waves and Ca2+ transients. In contrast, SEA0400 inhibited Ca2+ transients but affected neither Ca2+ sparks
nor Ca2+ waves. These results indicate that angiotensin II enhances the automaticity of pulmonary vein
cardiomyoytes through intracellular Ca2+-dependent mechanisms. Further understanding of such mechanisms
may lead to a therapeutic means for atrial fibrillation.

― 84 ―

P-11ƣ±ŰƙÈƌ5Ė:p^m=pH;:mKÍëe;K'3
Ŋ(ĕ}:hrJpC

In vivo imaging of the pathophysiological changes and dynamics of immune cells in influenza
virus-infected mouse lungH̨͔Ѧƣ 1, I-Hsuan Wang1, бɀҘ 1, ͉ɪĂ 1, Lopes TJS1, 2,
Gabriele Neumann2, ΋ɂҍӻ 1, 2
12

̵ǹƅдТÝ×¨ʠ̿Š֎Department of Pathobiological Sciences, University of Wisconsin-Madison

HHiroshi Ueki1, I-Hsuan Wang1, Satoshi Fukuyama1, Hiroaki Katsura1, Lopes TJS1, 2,
Gabriele Neumann2, Yoshihiro Kawaoka1, 2
1

Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science,
University of Tokyo
2

Department of Pathobiological Sciences, University of Wisconsin-MadisonÛÂ×Û¥xE̎rbpҽͱʓwҠѭְ҇ȡɮXՄ^dEƅȕÝϦƅȕâwȬёWʋ‫׆‬tăϦŐիʠ̿ЁqQFÛÂ×Û¥×¨wЀƔʓuxEȤíʍѐumpʝՄ`jҠwϏЁW֡ådrғTpRWEhwԝѫunRpẍVqtRFÛÂ×Û¥×¨uʠ̿bjҠwϮϬЋtϭǫqwԌγxEȤíʍѐÎ¸©ÍԎ̸djwǠ̫rtʛǤrtF̫ТсqxEϮĜÎÞ§ÛΒϰRp×¨uʠ̿bjҠƢԇƂd^rqEÛÂ×Û¥×¨uȬdȤíʍѐunRp˼jtПԅʃF
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Kenji Hashimoto1, Hiroki Shindo2, Takeru Itabashi2, Hikaru Mizoe2, Misaki Hasegawa2,
Kazuyuki Kuchitsu1,2

1Imaging Frontier Center and 2Department of Applied Biological Science, Tokyo University of Science͔ϠxƧѫҥwһɿЋtʍѐʓuǠoZŠ˳ǛwʛǤŞϬuİĜŎĜѳʄd¦¨³ÍհƂ`fp̴jF͔ϠxЮѮѠˉjtRWEϭǫ¨µØ¨tsu``rEhwūψВ˗Ɵ\jքęuU\ȹʱЋʍѐrruE֜Չֶujѫҥ֠¦·×wĔոĆbpŎՎЋtʍѐԡȲdF^w֜Չֶ¦·×ĔոuxEָͽЋ¦·×EΚʓ֊Ѩм(ROS)ECa2+tsW֡åd^rWПpRWEhwŠȑͦ͛x̩Ԏ̈wϑWǸRF֩â͔ϠwǠքuę҉
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BAi Goto1, Kohei Otomo1,2, Tomomi Nemoto1,2

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Department of Applied Biological Science, Tokyo University of Science, 2 Imaging Frontier Center,
Tokyo University of Science, 3 Graduate School of Science and Technology, Niigata University,

4

Experimental Farm, National Institute of Genetics, 5 Institute of Agrobiological Sciences, National

Agriculture and Food Research Organization, 6 Graduate School of Agriculture, Ehime University,
7

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BJohtaro Yamamoto1

1

National Institute of Advanced Industrial Science and Technology (AIST)Mԃ̃N λΥѫҥœuU\Šȑwˆ˳ԑγƢҦtӪŉГ֡ŠŉΒ‫׬‬Fluorescence Correlation
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ɲ`EU{Ǹ֏ĜƂwԎ̸ьϮѫҥêq`TƢҦudFFCS wֹԃxɝG‫נ‬mpRWEßҿЋtɔԵ FCS ԑγӹ҉xŐϔϑӪŉ‫׏‬ʆ֛wÄ¦ÔÛrbpģѲ`EɏǹVn‫׎נ‬ut
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P-23
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'03ĩƝƟƚ;oE(ñſŢéStructural analyses of goldfish and medaka scales by vibrational spectroscopyBȀӁֳðEëɀֲĆẸքΩɶ̵āƅдͯдǹȕ˲‫ח‬քBMasayuki Nara, Yusuke Maruyama, Atsuhiko Hattori
College of Liberal Arts and Sciences, Tokyo Medical and Dental University (TMDU)
MxcuNХ‫בףמ‬wÙ¢xҶʓ‫מ‬uĘjХѭ҇qQE¢ÕÞ¡ÛWíʬŠqQ҅ѷȿrE¢ÕÞ¡Ûu¼¶Ù¦¾®µ‫׬‬HAP‫׭‬W·Йbj‫מ‬ՁȿrVqXpRFՠɝE
Х‫בףמ‬wÙ¢x¿µw‫מ‬rƪ͜uEФ‫מ‬ѫҥr‫מ‬Ӈѫҥump‫¦×׬מ‬Í‫׭‬ĊԫWԦ
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Mѯ̻rғȨNŎƜȰƮƝ‫׬‬ATR‫׭‬ՂǷŠŉϰRpÛÔwÙ¢wÊ±µĺγȝbj

EӺ‫־‬x¢ÕÞ¡Ûur^Eӵ‫־‬x HAP u½Û¶W 1013 cm-1 uԌγ`‫׬‬Ǐ 1a‫׭‬Ì¶‫(؂‬؅1631 cm-1)‫װ‬Ì¶=(؅1550 cm-1)EÌ¶>(؅1240 cm-1)½Û¶WԌγ`j‫׬‬Ǐ 1b‫׭‬F
jE‫׏‬ʆÕËÛŠŉΒϰRpÙ¢Ԧ~rEHAP w PO43-ȬзĖ҂ˍŽuϲ̴d 960
cm-1 w½Û¶xE֬ՄѼâqɲZtE֬ՄѼ֠qxɰZt^rWVmjFÙ¢ӵ‫־‬uxE
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1550
1453
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rsˈmpRrғTϓӂ‫׬‬Љӂ‫׭‬qQ^rVEӂѨҥϲ̴wӪŉ

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2000

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1600
1400
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                      Ǐ‫ ״‬ÛÔwÙ¢wՂǷ¨Çµ×1) Azuma K. et al., Biochem. Biophys. Res. Commun., 362, 594-600 (2007).
2) Yano S. et al., Zool. Sci., 30, 217-223 (2013).

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P-24
Ɖ±VRU'03´ŽáĿŇĭïÀľŌ:hrJpC
Single cell imaging of transplanted stem cells
in the whole transparent tissue by quantum dots
B;ɓЈʌͣ 1EεɊ ƍ/Eȳ֎ɅǹĆ/EΙɇʘǼ.EâϱΕɑ.E‫ך‬ǥǇĬ/1ƫơȼǹȕǹȕ֧ɌȕТсдϮƵŠȑɌȕȯˮE2 ̵āǹȕǹȕ֧ƅȕѠТсдͦҦϮϠȕȯˮ

BToshiki Mizumaki1, Hiroshi Yukawa/,Daisuke Onoshima/,Etsuo Susaki.,Hiroki Ueda.,Yoshinobu Baba/
1

Graduate school of engineering, Nagoya university, 2 Graduate school of medicine, Tokyo universityŕϮƅЅwȘŎʓƙ{΍Ѕż̻̠ǹ֦uɮXşdjuxEи͔ɟѫҥWҹǈ:ѭ҇œwswքęuִпbEϮЙbpͦҦЇ˞bpRVßѫҥØÆ×qԎ̈dʋԃWQFbVbE^qϮĜœwd~pwи͔ɟѫҥѸҊЋuÎÞ§Ûԗ˻qXʸӱxЧх`p
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֦jԇ֎qwԌȨuϷmpR

wWϪϢqQF̫ТсqxE֏ȑ¶±µ (QDs) ӪŉÎÞ§Ûʸӱrѭ҇ը̈Ƃʸӱ
(CUBIC) ӫƨd^rqEʒʓҜäŎÏ´×Ë¨uU\и͔ɟѫҥwѸҊЋÎÞ§ÛƢҦudֿ˼Ћԗ˻ʸӱwЧхuƞѭkF
 QDs655 ϰRpÕÆ×ƂbjɟѫҥʼŝǐӤqQÅ¾ÖÛrŐuEʒʓҜäŎÏ´×Ë¨wȷּҪи͔bjr^Ein vivo ӪŉÎÞ§Ûӹ҉uи͔ɟѫҥWíuË¨w
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ċâE֏ȑ¶±µӪŉÎÞ§Ûʸӱrѭ҇ը̈Ƃʸӱӫƨd^rqEи͔ɟѫҥwѭ҇ÝҹǈœѸҊЋÎÞ§Ûԗ˻WƢҦqQ^rWЪƽ`jF

― 98 ―

P-25=BNNrge:Bo(`o^7:lpC'©"ĜĝťÞIKSg(ƎĠDevelopment of a diagnostic system based on exosomal microRNA profilingB‫ה‬ǧ ʐ 1,2EǓȼ чß 2EŦɂ ˸ҋ 2EӀΘ ‫נ‬ʌ 1Eß̨ ֬і 2,31̵āǹȕ ǹȕ֧ӤȕѠТсдE2 ·»ƅЅ»ÆÞ¦ÔÛªÛ®ÞE3̵āǹȕ ǹȕ֧ɌȕТсд

1,2

BRyo Iizuka , Shoichi Tsuchiya2, Fumi Toshioka2, Takashi Funatsu1 and Takanori Ichiki2,4
1
2Graduate School of Pharmaceutical Sciences, The University of Tokyo,

Innovation Center of NanoMedicine, 3Graduate School of Engineering, The University of TokyoӯΥƿΥEȸtswĜΥêuȓǕdËÙ RNA‫׬‬miRNA‫׭‬Er\¬¬ÞÍuœƁ`j miRNA xEWxcrd͜GtϿʗwԗ˻uŦϰqX½ËÞÞrbp̢̦ԇ`pRF^wjE՞լVnјħu miRNA wÄÙÂÖÛȞϪd¦¨³ÍW
̦pRFʭGxEĜΥʻōdr¬¬ÞÍËÙ RNA wÄÙÂÖÛѯ̻WşŶ`ϿЀԗ˻¦¨³Íw֟ЇӰmpRF ̫¦¨³ÍxEӹ҉̫ĜEŨʄϰ¾¬¢ÛEÞµÖ±§Ǜ´½¨u͛ʬ`FԚ˹ÝԚӤΫŸbj´½¨ӹ҉uª±µdrEIĜΥêw¬¬ÞÍwƌֶJE
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miRNA wÄÙÂÖÛѯ̻WşŶ`F ̀ȓwËÙØΒxEmiRNA wӪŉ͟Ԭtsϗֵt˩ğE¼ÃÖ¯«Þ¦ÔÛuǸǹt̎֠ԃd^rWǀ‫׍‬rtmpRFh^qE^wǀ‫׍‬ԎΆdËÙØΒ‫׬‬Ligase-Assisted Sandwich Hybridization‫׬‬LASH‫׭‬Β‫֟׭‬ЇbjFLASH ΒqxEǠ̷âuǐȝbj C-probe U{Ӫŉ͟Ԭbj D-probe ϰRp͟Ћ miRNA ːˏbET4 DNA ligase ϰRp
3 Ҕծѯ`fF^uEmiRNA В˗Ӫŉ͟Ԭd^rtZE՞լt miRNA w͕şWƢҦrtFLASH Βâԓw¦¨³ÍâqȞՌbEhsa-miR-143-3p ωɥĤȓЋu͕şqX^rЧԟbjFj 30 fmol hsa-miR-143-3p ȓǕãuURpEλΥwʻōV 10 Šq miRNA ȝ֏Ћu͕şd^ruʬŷbjFϪǕEӯςўӽbj¬¬ÞÍuœƁ` miRNA w͕şԚpRF
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― 99 ―

P-26
ïĎ(ĠĕƧÄÎÄÏ'3ÿËƆļĮ(ROS)(Æ-MXFD( ROS ĕÏƅļõÙ­Ě}(ÄÎÄÏĚ¾(:hrJpCŢéPhysiological function of reactive oxygen species (ROS) in plant development andmorphogenesis: Imaging analysis of abnormal development in a knockout mutant
defective in ROS-producing NADPH oxidase in Marchantia polymorphaӘƔֲͣ 1E̫ͥТʌ 2EȠ̫ǹՔ 1E‫ס‬Ɋ̕ɯ 1EΝüƉó 3Eȳ֡Εð 2,3E̬Θƶɞ 1,21̵āϬдǹȕϬɌȕքʍϰϮϠдȕдE2 ̵āϬдǹȕÎÞ§ÛÂÙÛ³ªÛ®ÞYuki Hagiwara1, Kenji Hashimoto2, Daisuke Miyamoto1, Tomohiro Takagawa1, Takuya Asai3,
Yasuyuki Ozeki2,3, Kazuyuki Kuchitsu1,2
1Department of Applied Biological Science and 2Imaging Frontier Center, Tokyo University of Science,3

Department of Electrical Engineering and Information Systems, University of Tokyo֊ѨƴƮŉƨʬwնкqäƢրЋuϮʬ`Κʓ֊Ѩм(ROS)w͸ʓWɠZПpR
WEѫҥҶuȓǕd ROS Ϯʬ։Ѩ NADPH oxidase (Nox)/Respiratory burst oxidase homolog (Rboh)uѫҥǮт֠uп͙ЋuϮʬ` ROS r Ca2+rWE͔ϠŋϾEϭǫ¨µØ¨ʍѐEňшʬ֜؆ЇϮEÄÙÕÍѫҥͱts͔Ϡw‫ͦͨנ‬ҦwǠАrtѫҥӵȿuU\ʛǤѳʄѠw͇ɟ
q֍ԃtɺų̻jd^rẄVutnnQFROS wп͙ЋϮʬxEѫҥǮwɲɥԦѕE
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3D MOTION OF TRPV1 CATION CHANNEL DEPICTED BY DIFFRACTED X-RAY
TRACKING METHOD
Bӥ̱чȑ 1Eáȷƶɯ 1Eįˉ̇ɯ 2E֡Ơƍƣ 3EáȷțĊ 1EïīΕ 1EěG̨ӻͨ 1, 2, 3
1ϯѺТÝ̵ǹňшÇÕÛ¶ԑγʸӱ OILE2 ̵āǹȕǹȕ֧˼‫׈‬ǞŴʬдȕТсдE2 ‫נ‬ՕɥŉдȕТсªÛ®Þ SPring-8

BShoko Fujimura1, Kazuhiro Mio1, Masahiro Kuramochi2, Hiroshi Sekiguchi3, Muneyo Mio1, Tai Kubo1,
Yuji C. Sasaki1, 2, 3
1

AIST, 2 Graduate School of Frontier Sciences, The Univ of Tokyo, 3 Japan Synchrotron Radiation
Research InstituteTransient receptor potential (TRP) °Ðº×xѫҥҶuȓǕbœǋʓϠՁEƂȕϠՁEϠϬūψtsumpΚʓƂ`ªÛ¤ÞqQFTRP °Ðº×wǸZxՎĜwRjr^uȓǕb
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ąǊ TRPV1 wğŽͦ͛Ԏ̈djuESpring-8 upЉӂ X ѼϰRj X Ѽ‫״‬ŠȑդՊΒ‫׬‬DXT: Diffracted X-ray Tracking‫׭‬Ԛj‫׬‬ãǏƗϖ‫׭‬FDXT qx®Û¾Ձ֐·»ѯ̔q͟
ԬbEǊʽ¨Ê±µwǊՐմŽŁ˺ԍ4EǊՐԍ7rbpÖ×®ÍuԑγbŠ̸ӰmjF̎֠ŠԎҦx 100 5m/frameEԍɥўɥxhi04 = 0.18 mradE07=0.74 mrad qQF
hwѯ̻E7Ց˽ƬwǊՐմŽxEÄ¤¦Ûϰ֏ĤȓЋuǬɲ`jFjETRPV1 wÛ®£¸¨µōjǥƨw7Ց˽ƬwǊՐմŽxEÄ¤¦Ûōjǥƨr͹~p̢ʞuʺTpRjFjE^wմŽx֐·»ѯ̔q͟Ԭdę҉uϺt^rWЧԟqX
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TRPV1 ȣúǯȂ X ĭɨ4jŭŤÝȎÍYƥ« 10 nm ĔȎƁɆɈĦ¶ȣ TRPV1 ȽɡɊȯŞȌÐśǼǩȽɡɊȯŞ4jȎ1Żŵ@Ȍų@ǼȂɆɈĦ¶Ȏ@ǵȣŭŤǾ
ȠǪ ƥ― 102 ―

P-29
űŢ:hrJpC'02á1%&ß&ëő}ñſ

Super-resolution microscopy revealed a novel chromosome structureB‫נ‬ϱӊ̍ 1ERawin Poonperm2EŸӥӣ 1E̶ϱƓʌ 3EɜɂΕ 4Eбüɖß 21ϯ͘ʸӱѺƨТсʱ½Î´×Тсք֝E2 ǹ֢ǹȕǹȕ֧ɌȕТсдE3 ʛǤիĬТс̴̩ͦ͛ ICT ТсʱE4 ǹ֢ǹȕǹȕ֧ϮƵͦҦТсд
BHideaki Takata1, Rawin Poonperm2, Kaoru Kato1, Atsushi Matsuda3, Yasushi Hiraoka4, Kiichi Fukui1
1

National Institute of Advanced Industrial Science and Technology (AIST), 2 Osaka Univ. Grad. Sch.
Eng., 3NICT, 4Osaka Univ. Grad. Sch. Biosci.

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µuʽϻ^rqȘŎVnǙьtտĔʛǤwŠֆոʬbpRF

bE̿ӂĜ͛խWͬb

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ՁW‫נ‬ȦɥqִƨbjŽЋ͛խĜqQjEϪǕw‫׏‬ʆ֛ʸӱ

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Ehw͛խwŎԲԎ̈duxҼmpRtRF
̫ТсqxEŠӸ̧̿ӂĜ͛їdâq֍ԃtłXˉn8̿ӂĜ¨ÐÂÞ×¶͛խ9uϔϑɴpjF̿ӂĜ¨ÐÂÞ×¶xE̿ӂĜҰwêʊuՑϢuŠɕd®Û¾ՁVt͛խqEDNA ×ÞÄϢu̲vp˷Ţ`f^rq͏Ϣw̿ӂĜ͛їbpRrғT
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rbpxE¢Û´Û¦ÛӿƨĜETopoisomerase II1EKIF4A tsWПpRF̫ТсqxEՅԎŃɥ‫׏‬ʆ֛‫׬‬3D-SIM‫׭‬rָȑ‫׏‬ʆ֛‫׬‬FIB/SEM‫׭‬Ŧϰd^rqE̿ӂĜœqw^w
өЉՁwŠɕԝѫuԌȨbjFhwѯ̻EիəwӪŉ‫׏‬ʆ֛qxE¨ÐÂÞ×¶өЉՁw
Šɕx̿ӂĜҰwêʊu 1 ̫wՑϢwŠɕЪbjWE3D-SIM U{ FIB/SEM ϰRjԌȨuE1 ̫qxtZíu 2 ̫wՑϢwŠɕqQ^rẄVrtmj‫׬‬Ǐ‫׭‬FjE¨ÐÂÞ×¶өЉՁ»±¯Ûbjʀw͛խԌȨd^ruE^w 2 ̫֚Ϣw̿ӂĜ¨ÐÂÞ×¶͛խw͛їuxE¢Û´Û¦ÛӿƨĜr Topoisomerase II1wȥåWǹXR^r̈

VrtmjF`uE^wŠӸ̧ϡϺЋt¨ÐÂÞ×¶͛խwɵʬxEŠӸ̧·Þ«qQ CDK1 ĤȓЋt KIF4A
wÖÛ֊ƂumpքŠЋuŨʄ`pR^r

̈V

rtmjF
ċâwSuE̫Тсu̿ӂĜ¨ÐÂÞ×¶͛
խWíu 2 ̫wՑV͛ʬ`^rWŠVmpXjWE̿ӂĜxœքuӿ˶wՑ͛խˉn^rqEŠӸ̧uU\̿ӂĜ͛խwˠYŽXϮşbdZbpRr
ғTF― 103 ―

Yƭƥ ņ+ƖƃɤƾǃɥȉŢŒ'ƖƃɤƱƼƬǈǀǃɥȈŐoǼȂÇľȹȮɚɎȪɣɞɅÎŲǪƺǍǛƫƥưƳƮƥǘǗƭƥ

P-30
ÍËř

`or_'03ĨƝľŌ`oUpdp`Î(š·

In vivo Observation of Dynamics of Osteoclast Proton Pump Using pH-activatable
Fluorescent Probe
BӠɅѷ˸ 1)Eǹֲ͒ǻ 1)E ӔǗƶó 1,2)
1)ǹ֢ǹȕǹȕ֧ɌȕТсдE2) ǹ֢ǹȕŋϾȕÂÙÛ³ТсªÛ®ÞBMasafumi Minoshima 1), Yuta Omori 1), Kazuya Kikuchi 1,2)

1)

Graduate School of Engineering, 2) Immunology Frontier Research Center, Osaka University‫מ‬ѭ҇qxФ‫מ‬ѫҥu‫מ‬ƮƝr‫מ‬Ӈѫҥu‫מ‬ɵʬW҈ա`Eŕ͛ї`^rq
ʔəʓWѷˉ`pRFФ‫מ‬ѫҥΚʓwÿհx^w½ÕÛ¨ɈbE‫מ‬ќ‫ע‬ЁE֡ѕÖË°ьw‫מ‬ϿʗwЇЁuntW^rVEhwͦҦԎ̈d^rx֍ԃqQrғTFʭGw×ÞÄqxEФ‫מ‬ѫҥW‫מ‬λVdrXuɵʬdĚ pH ‫׈‬ǞuЙБbE‫מ‬ѭ҇âuU\Ě
pH ‫׈‬ǞƢԇƂqXӪŉÄÙÞÃw֟ЇuƞѭqXj[1,2]F^qu֟ЇbjÄÙÞÃË¨uʻåbEϮXjѫҥŽʡԌȨqXùŉȑŻՄ‫׏‬ʆ֛ϰRpÎÞ§ÛӰS^rqEФ‫מ‬ѫҥWΚʓƂd͜ȑԌȨd^ruʬŷbpRF`u‫מ‬ƮƝͦ͛wԝѫԦ~juEʭGxФ‫מ‬ѫҥuU\ ATP ‫כ‬ŽǛÄÙµÛÊÛÄwŽʡuЙБbjF‫מ‬ƮƝw֯u˯ş`֊xÄÙµÛÊÛÄumpӰpRrғT
pUE^qwФ‫מ‬ѫҥÄÙµÛÊÛÄwÎÞ§Ûѯ̻VxEѫҥ_ruhwȹǕWϺt͜ȑWԌȨ`pR [3]FbVbtWERnEs^q֊˯şbpRVwʛǤWͧȈbpUE֊ʓ‫׈‬Ǟɵʬrw֡ծʓWä̈qQmjFh^q̫ЇӵqxEpH ʠƟʓӪŉÄÙÞÃϰRpÄÙµÛÊÛÄŽʡrĚ pH ‫׈‬Ǟrw֡ĨÎÞ§Ûd^rrbjFċŮqu֟Їbj pH ʠƟʓӪŉÄÙÞÃqxÄÙµÛÊÛÄw͟ԬuϰRpRѻӂӪŉ®Û¾ՁrΓ֜W֍tmpRjjE˼juՂӂ‫׈‬ǞuӪŉ
Ъd pH ʠƟʓÄÙÞÃԕԑÝƨʬbEhwʓՁunRpԙĥbjFhwѯ̻Eռšt pH ‫׈‬ǞqʍѐWƢҦtՂӂӪŉÄÙÞÃ8Red-pHocas9֟ЇbjF^wÄÙÞÃux‫מ‬ѭ҇}ɲZѯƨdÀ¨È¨ÈºÞµǠWȲō`pRjEʻåʀx‫מ‬ѭ҇uϡϺЋuզոEνϷd
^rWqXFRed-pHocas Ф‫מ‬ѫҥÄÙµÛÊÛÄW͟Ԭ`jË¨Ï´×uʻåbEùŉ
ȑŻՄ‫׏‬ʆ֛ϰRp‫מ‬ѭ҇wÎÞ§ÛӰmjFÄÙµÛÊÛÄwȹǕr‫מ‬ѭ҇ӵ‫־‬qw
pH ϭǫwǵƂ֜̎֠ujդՊd^rqEФ‫מ‬ѫҥÄÙµÛÊÛÄwŽXuĕmj֊ʓ‫׈‬ǞwɵʬÖ×®ÍqˏT^ruʬŷbjF1) T. Kowada, J. Kikuta, A. Kubo, M. Ishii, H. Maeda, S. Mizukami, K. Kikuchi, J. Am. Chem. Soc. 2011,
133, 17772.
2) H. Maeda, T. Kowada, J. Kikuta, M. Furuya, M. Shirazaki, S. Mizukami, M. Ishii, K. Kikuchi, Nat. Chem.
Biol. 2016, 12, 579.
3) J. Kikuta, Y. Wada, T. Kowada, Z. Wang, G. H. Sun-Wada, I. Nishiyama, S. Mizukami, N. Maiya, H.
Yasuda, A. Kumanogoh, K. Kikuchi, R. N. Germain, M. Ishii, J. Clin. Invest. 2013, 123, 866.

― 104 ―

P-31ʊэ͌Ǩքę͟ЋrbjӤϠ´Ö½ÖÞÐÖw֟Ї

Development of drug delivery carrier for myocardial infarction̨֒ Ă 1EDasa Siva2Eëɀßֲ 1
Brent French2EKimberly Kelly2EAlexander Klibanov21ɗāǹȕӤȕքE2 University of Virginia, Cardiovascular Research Center

Ryo Suzuki1, Dasa Siva2, Kazuo Maruyama1, Brent French2, Kimberly Kelly2, Alexander Klibanov2
1

Teikyo Universitt, Pharma-Scinece, 2University of Virginia, Cardiovascular Research CenterMБЋNӦӯŕύΛʀwʊэ͌ǨքęuURpEʊэѫҥwīԮӤŕϮĩհdӤűw´Ö½ÖÞ
W֍ԃr`pRFbVbEʊэ͌ǨքęużϨZӤϠ´Ö½ÖÞqX˽ΒxЧх`
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Wʊэ͌Ǩքęwʊэѫҥ}wӤϠÐÖrbpŦϰƢҦut

wŗɾ`FąʀxE

ʊэѫҥīԮӤtsˣՓbjÖÊ¬ÞÍԦӽbEʊэ͌ǨuU\ʊэīԮğϰtsunRp͕ԒӰS÷ȝqQFMѯԨNÂÞ§´¨ÄØΒqԅşbjʊэѫҥuѯƨdÇÄ°¶ÖÊ¬ÞÍuĮ‫ז‬d^r
qE^wÖÊ¬ÞÍWʊэ͌ǨÏ´×Ë¨wЀǵքęuִпd^rẄVrtmjFąʀE
̫ÖÊ¬ÞÍwʊэ͌Ǩ΍Ѕ}wʍϰW̧ɾ`F

― 105 ―

― 106 ―P-33
Ŋ$(ĈĞũ¹'%/&

lp\ē(ĀĆòÂ(ŢéColor-coded cellular imaging of T lymphocyte accumulation in the lungB֜ԯɊ̈Ζ 1EӐ֎ӊՀ 1EêɀĪʧ 21ɀƠǹȕǹȕ֧ƅȕѠТсдE2 ƇӚǹȕǹȕ֧ƅȕТс֧
BAkihiro Hasegawa1, Hidetaka Ogino1, Toshinori Nakayama2

1

Yamaguchi University Graduate School of Medicine, 2 Graduate School of Medicine, Chiba
University ǃʖӄњЁxcrdØ×ÞʓϏЁϿʗxEʼƔʠğuʼƔϡϺЋͦҦǛÅ×¾ÞT(Th)ѫҥWԡȲ`Eŕ{ʼƔuֺ̙`^ruϏЁƜʍWԡȲ`FbVbtW T ѫҥx˶wâqxΣτѫҥw˶¾ÞªÛµкɥqQEȞ֯wҠwϏЁwǥqswStͦҦ̻jbpRwVEϡuΣτd®ÌÛΣτw͜ɭEΣτbj T ѫҥw¯·Ì±tѫҥŽʡẍVutmpRtVmjFh^qϏЁՄ^bjË¨wҠq T ѫҥwΣτȝ֏ЋuԎ̸djuϣһu֟ЇbjÖ×®ÍƢԇƂÏ¸®ÖÛѠU{Ë¨WϮXjϢʡwҠwœքÀ´˨ɹdÎÞ§Û¦¨³ÍϰRpѫҥˌŽwԎ̸ӰmpX
jFhwѯ̻EË¨ǃʖÏ´×qʼƔƮōʀuՄ^ʼƔϡϺЋ Th2 ѫҥwҠ}wִпxʼƔƮōʀ 6P20 ̎֠qEҠѭ҇œqѫҥwִǌ‫׬‬focus‫׭‬ɵʬbpEhwʀwȇ֊ϫΣτϏЁɋwɵʬŨʄbpR^rWVmjFͨuĈwͦҦЋ T ѫҥ¤Ãª±µunRpʼƔƮōʀwҠ}wΣτ͜ɭ͹Ւbjr^ETh1 ѫҥẍЛt focus ɵʬfeEhwм‫ב‬umpҠѭ҇œqwִп͜ɭWϺt^rẄVutmpXjFjťwҠϏÏ´×rbpŵЁǛʒʓҠϏÏ´×ϰRpŋϾѫҥwΣτ͜ɭԎ̸bjr^EִпbpXj T ѫҥȇêϫxҠѭ҇œuǙßuִпbpѫҥִǌɵʬfeEϏЁÏ´×uҠѭ҇œqwѫҥˌŽWϺt
^rWVmpXjF h^q̫ТсqxEѫҥwм‫ב‬ϏЁÏ´×wչRuѫҥΣτ͜ɭwչR̈Vud^rБЋrbpETh2 ѫҥwִпr focus ɵʬŨʄdǋȑwƪȝհjFhwѯ̻Eʼ
ICAM-1 ʼĜʼ TNF ʼĜtsʻåbpUZrǃʖÏ´×uU\ Th2 ѫҥwִпWʺŨ`ETh2 ѫҥִпu֡ådŠȑẄVrtmpXjFFocus ɵʬwǥΆ̠ţwXmV\
xҠѭ҇œuִпbpXjʼƔϡϺЋ Th2 ѫҥwYumpϮcȴ˶wѫҥwִʼƔ˛ЪѫҥrwşēRqQrғTʼƔƮōʀwͣϢѫҥwִп͜ɭ͕Ԓbjr^ETh2 ѫҥrƪcǥʱu focus ɵʬd^rẄVrtEfocus ɵʬuU\ɺųWЪƽ`jF
jʼƔϡϺЋ Th1 ѫҥr Th2 ѫҥ ƪc focus ‫׈‬Ǟuִпd^rWVmjF― 107 ―

Fig. 3. Accuracies of regression
tests for three features and their
combo.

― 108 ―

P-35
ƊWZĸ±5ĖsľŌ(ºÐġčý(ƎĠDevelopment of a method for local heating in a single cell using gold nanoparticles
B̫ǸȔ̈ 1EɂքɯǠ 1EӀΘ‫נ‬ʌ 11̵āǹȕǹȕ֧ӤȕѠТсд

BTakaaki Honda1, Khoki Okabe1, Takashi Funatsu1
1

Graduate School of Pharmaceutical Sciences, the University of Tokyo, JapanβɥxǠ̫ЋtϠϬ֏wßnqQEϮϠwΚŽuǹXZɹׂåTpRFjEβɥxѫҥœwQϮƂȕƜʍˬֆd^rVEѫҥœβɥxѫҥwϮϬͦҦuɹׂƙdr÷ʜ`FňӰТсuEūψumpѫҥœβɥWǵƂd^rѫҥœuxäǙßtβɥŠɕWȓǕbpR^rẄVutmpRFbVbEѫҥœβɥwԑγWўŶЋuТс`pRwrxȬϖЋuEѫҥœβɥwѫҥͦҦuU\ɺųunRpxä̈qQFѫҥœu
U\ȹʱЋtЇϚuѫҥwʍѐԌȨd^ruEѫҥœwϚϯϮäǙßtβɥŠɕwɺų̈VuqXrғTjFh^qEѫҥœβɥȹʱЋuŨʄd^rԚjF
̫ТсqxE֐·»ћȑ COS7 ѫҥœuȲōbpѫҥȹʱЋuŸϚbjF֐·»ћȑWŉƮƝbpϚuǵ˜dϡʓŦϰbpEØÞ¥ÞϖȰd^rq֐·»ћȑuŸϚӰ
mjFjE֐·»ћȑϰRjŸϚuѫҥœwβɥǵƂxӪŉʓÊÖËÞβɥªÛ¤ÞϰRpγȝbjF֐·»ћȑwŸϚuѫҥœβɥWâ̆d^rWЧԟqXEȝ֏ЋtŨʄӰS^r

qXjF`uE֐·»ћȑwŸϚ‫׈‬ǞwѫҥœuU\ȹʱʓunRpЧԟb

jF̫ʳΒuѫҥʍѐwԡȲrbp¨µØ¨‫׌‬ћwɵʬwԌȨӰmjF¨µØ¨‫׌‬ћrxѫҥՁœw mRNA Wŝִbpɵʬ`‫׌‬ћw^rqQEѫҥœβɥwâ̆uɵʬ`^rẄVutmpRF^w^rVѫҥœw·»¨Þ×qwβɥâ̆WѫҥʍѐuԴϥd^rЪfjFąʀxEϡȝwѫҥœŠȑ͟ЋrdtsEȹʱЋuѫҥœβɥŨʄbEѫҥœβɥwѫҥͦҦuU\ɺųϬԎd^rБˊdF― 109 ―

P-36
¯ĉůì¦ 2±ƙÈƌ'03 4 ƇóūĕľŌ( 3 öŀâš·

4-color, 3-dimentional time-lapse imaging of live cells by utilizing multi-point scanning
two-photon microscopy֙ϱʕƣ 1,2Eǹƚɨɜ 1,2E̱ϱ֬ 3,4E֜ԯքŉΕ 3,4E͇̫Пɑ 1,2
13ƃ΢շǹȕÝǹȕ֧ʛǤдȕТсдE2 ƃ΢շǹȕÝָȑдȕТсʱEǠЩϮϠȕТсʱÝϮϠհƂТсք֝E4 ѺƨТсǹȕ֧ǹȕÝϮƵдȕТсд

Takafumi Kamada1,2, Kohei Otomo1,2,Takashi Murata3,4 Hasebe Mitsuyasu3,4 Tmomi Nemoto1,2
1

Graduate School of Information Science and Technology, Hokkaido University,
2
3

Research Institute for Electronic Science, Hokkaido University,

Division of Evolutionary Biology, National Institute for Basic Biology,
4

Department of Basic Biology, School of Life Science, SOKENDAI¨Á¸Û´¨ϰRjŐϔϑՃ̓ӹ҉xEŻՄŉŠųbpԚ˹âǸϑՃ̓d^rq‫נ‬լuӪŉŃƞʃƢҦqQFʭGxEՠՂǷǞØÞ¥Þŉu‫נ‬RընϨ̢d¨Á¸Û´¨ϰRjǸϑՃ̓Ǜ 2 ŉȑŻՄӪŉ‫׏‬ʆ֛ (TPLSM-SD) ͛їbE‫נ‬ÁÞ¾ÚÞwØÞ¥ÞŉηȲōd^rqE‫נ‬R̎т֠ŠԎҦqwϮĜœքŉȕ˻ȿŃwƞʃƢҦrbj (Otomo, et al., Anal. Sci. 2015)FbVbEϪϢw TPLSM-SD wŻՄŉȕѠxEƌßØÞ¥Þŉηwŉ¾×¨т֠ōȰdć͜rtmpRjE2 ŉȑŻՄrRTs ƪ̎uŻՄƢҦtЇӂǌw˶uxŨ֦WQmjFß˽qEǸ֍͟Ԭ̫͟wԌȨuURpxƧӪŉЇӂǌwŻՄÝӪŉ¨Çµ×w֍tuϲ̴d°Ðº×֠wӪŉĬƥwπ՜WƔǋrtE͟ԬȬԱwŤťWǍַrtǥƨWQF
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jEƪ̎͟Ԭxր\wWßҿЋqQmjFʭGx‫؁؃‬ŉu 1 ŉȑŻՄwǸϑՃ̓ǛŐϔϑ‫׏‬ʆ֛uURpŻՄ¨ÇµÕÍwɐϺuЙБbjÛÌ¦ÛΒW̢żqQ^rЪbpXj‫׬‬đӥĈE2011 ɝÆ¨µÎÞ§ÛԿ̐‫ך‬Կ‫׭‬F̫ТсqxEѫҥœȳǈȜEϮĜŠȑwГúğϰEГȬֆ҉ьƪ̎uƢԇƂd^rБˊbEŻՄØÞ¥Þwƪ̎ġϰu‫נ‬լË×°ÕÞÎÞ§Û‫׏‬ʆ֛w֟ЇԚjFeE°®ÛÝ¤ÂÑØÞ¥Þŉ¾×¨(Spectra PhysicsEMai Tai eHP deepsee‫װ‬Γ֜ 910 nmE¾×¨ɚ 70 fs)r±³×ÀÍØÞ¥Þŉ¾×¨‫׬‬Spectra PhysicsEFemto TrainEΓ֜ 1042 nmE¾×¨ɚ 300 fs‫׭‬E¯Ù±ÌÕÞ‫׬‬THORABSEDMSP-1000L‫׭‬uƨΓbƪßŉՋq¨ÐÛ¸ÛÓ¸±µ‫͢׬‬΋ָͦECSU-X1‫}׭‬ȲōbjF
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½¢ BY-2 ǟ‫ח‬ѫҥuURpE¿¨µÛEʆȳєEªÛµÙÎEҧՁù֍ҶhiӪŉ®Û¾Ձ msGFPE
mCitrineEmCherry rӪŉӂѨ FM1-43 q͟ԬbE3 ͨŅ‫נ‬լÕÃÎÞ§ÛȞ˾bjF̜uEŻՄƙ{Ӫŉw¨Çµ×ϡʓwչRŦϰbÛÌ¦ÛӰS^rq‫ ^װ‬4 nwӪŉЇӂǌẅЧtŠֶuʬŷb
jFhwѯ̻EѫҥŠӸw֯wƧѫҥœȳǈȜwˌŽE3 ͨŅЋuƢԇƂb‫נװ‬լդՊd^ruţpʬŷb
j( z іǎ: 25 µmEֺŉ̎֠: 300 ms )FċâEʭGx‫נ‬R̎тŠԎҦq 4 ӂċâwӪŉЇӂǌWƪ̎ԌȨƢҦt 2 ŉȑŻՄӪŉ‫׏‬ʆ֛֟Їd^ruʬŷbjF― 110 ―

P-37
In Vivo Temperature Imaging for Deeper Abdominal Region of Mice
Using Ratiometric Over-1000 nm Near-Infrared Fluorescent
Rare-Earth-Doped NaYF4 Nanothermometer
BShota Sekiyama1, Masakazu Umezawa1,2, Shuhei Kuraoka1, Takuji Ube1,
Masao Kamimura1,2, and Kohei Soga1,2
1

Department of Materials Science and Technology, Faculty of Industrial Science and Technology,
Tokyo University of Science; 2 Imaging Frontier Center, RIST, Tokyo University of Science

Nanosized materials have become popular in the field of nanomedicine as they provide new perspectives
on imaging, diagnosis, and therapy. One of the applications of nanomaterials is luminescencenanothermometry, which has attracted much attention as a non-contact thermal sensing technique in thephysiological temperature range. However, it is not widely explored for in vivo applications owing to the lowtransparency of tissues for the light to be used.
Our group has developed and reported the synthesis of a β-NaYF4: Yb3+, Ho3+, Er3+ nanothermometer for
ratiometric LNTh in the OTN-NIR region (Kamimura M. et al. 2017). The sensing is attributed to the change
in the luminescence intensity ratio (LIR) of the Ho3+ emission (IHo) at 1150 nm to that of Er3+ emission (IEr)
at 1550 nm as a function of temperature under 980-nm laser excitation. This ratiometric temperature sensing
is not affected by the concentration of the probe, thus reducing the dependency of sensing on measurement
conditions. In this study, we performed in vivo temperature sensing using β-NaYF4 nanoparticles co-dopedwith Yb3+, Ho3+, and Er3+ (NaYF4: Yb3+, Ho3+, Er3+ NPs), which displayed two emission peaks at 1150 nm(Ho3+) and 1550 nm (Er3+) in the >1000 nm near-infrared wavelength region, where the scattering andabsorption of light by biological tissues are at the minimum.
First, the Yb3+, Ho3+, and Er3+ concentrations were respectively fixed at 20, 3, and 0.5 mol% after several
trials (Wortmann L. et al. 2017). Ho3+ emission increased with increasing temperature, whereas the Er3+emission remained almost consistent in the physiological temperature range. The change in the luminescenceintensity ratio of the emission peaks of Ho3+ and Er3+ (IHo/IEr) in the NaYF4: Yb3+, Ho3+, Er3+
nanothermometer differs corresponding to the thickness of the tissue. Therefore, the relationship between
IHo/IEr ratio and temperature needs to be calibrated by the depth of the nanothermometer in vivo. Finally, thetemperature-dependent change in the IHo/IEr was evident at the peritoneal cavity level, which is deeper than
the subcutaneous tissue level. The designed experimental system for temperature imaging will open thewindow to novel luminescent nanothermometers for in vivo deep tissue temperature sensing.
References :Kamimura M. et al. J. Mater. Chem. B (2017) 5: 1917–1925.
Wortmann L. et al. J. Lumin. (2018) 198: 236–242.

― 111 ―

P-38
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Evaluation of brain targeted drug delivery with microbubbles and ultrasoundBȳĭǹͣ 1Ę֒ Ă 1EӘƔӃҋȑ 1EJohan Unga1EțŃϬѥ 1E
Ʌ ʎŉ 1EɹɀΉ҇ 1Eëɀßֲ 111ɗāǹȕ Ӥȕք

1

BDaiki Omata , Ryo Suzuki , Fumiko Hagiwara1, Johan Unga1, Lisa Munakata1,
Tadamitsu Shima1, Saori Kageyama1, Kazuo Maruyama1
1

Faculty of Pharma-science, Teikyo UniversityMҢ̒ÝБЋNӯΥrҮȞՁw֠wϠՁиŽƕȦuŨʄdӯΥҮ֡֝ (Blood Brain Barrier,
BBB) WȓǕdjEҧλʓwĚŠȑϠՁċǷxҮ}զոd^rWǍַqQFҮϿʗw΍ЅuƬ\EҮuȬd͜GtӤϠզոΒwТсWհE̠ՠqxՅׁΓrËÙ½Ã×ϰRj˽ΒWΔБ`pRF^xEՅׁΓϖȰuϮcËÙ½Ã×wˍŽǔǰ (ÐÀ³Þ¦ÔÛ) ŦϰbEBBB wընʓÿհ`f˽ΒqQF^quʭGxEՅׁΓϰRjԗ˻Ý΍Ѕ¦¨³Íw͛їБˊbEȘȝʓw‫נ‬RËÙ½Ã×w֟ЇհpXjF^wËÙ½Ã×ŦϰbjҮӤϠզոu֡bpEËÙ½Ã×rՅׁΓĠϰd^rqE
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ddY Ë¨uּҪœʻåbjFВʀuË¨ҮwƤƈϫuѮ‫׉‬ӟЋuՅׁΓ (ƲΓ˶ 3 MHzEϖȰɲɥ 0.5 W/cm2EDuty ¤× 50%E҈աbƲΓ˶ 10 HzEϖȰ̎֠ 3 Š) ϖȰbjFӯΥύΛʀEҮƞşbEŜѯšϜŐϔϑ‫׏‬ʆ֛uԌȨd^rqEҮ}զոƢҦtϠՁwǹ
X`unRpԙĥbjFͨuEddY Ë¨uËÙ½Ã×ּҪœʻåbEВluҮƤƈϫuȬbpՅׁΓϖȰbjFhwʀEÏ´×ӤϠrbp½Û¨Ã×ÞʻåbEɍƤwҮ}wиӰ֏γȝd^rqEӯΥҮ֡֝wընʓˉѶ̎֠unRpԙĥbjFMѯ̻ÝғȨNŠȑ֏wϺtӪŉ͟Ԭ´¨µÕÛʻåbҮŘϢšϜԌȨbjѯ̻EՅׁΓϖȰbjҮƤƈϫuURpERewŠȑ֏w´¨µÕÛʻåbjǥƨuURp

ӪŉWԌȨ`jFËÙ½Ã×rՅׁΓwĠϰʀu½Û¨Ã×Þʻåbjѯ̻E3 ̎֠ʀu½Û¨Ã×ÞʻådrɍƤwҮ}wиӰ֏u̢ʞtɐWԟtVmjF^wѯ̻VEËÙ½Ã×rՅׁΓĠϰd^rqE2000 kDa wӤϠҮœ}զոqX^rEU
{ӯΥҮ֡֝wընʓÿհxƢէЋqQ^rWЪƽ`jFąʀEԝѫtϡʓԙĥbpRZ^rqEȘŎʓw‫נ‬RËÙ½Ã×rՅׁΓŦϰbjҮӤϠզոΒw͛їuntWŗɾ`FMԫՙN̫ТсwßքxEJSPS дТԺ (JP15J10508, JP17H07119)E˸քдȕгхǹȕʮϸЋǠАɵʬø͘ (ɜʬ 25 ɝ؅30 ɝ)EAMED (JP16dm0107115) wŹʬƟ\j― 112 ―

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P-39
  *  '03ŋĦÏ(éAnalysis of gallstone component using FE-SEM and EDS
B;̫̤ 1E̮‫ ̈ק‬11ƇͰдȕʸӱǹȕǹȕ֧ ŉдȕТсд
BHajime Mizumoto1, Liming Li1

1

Graduate School of Photonic Science, Chitose Institute of Science and Technology (CIST)̫́ăwҡСī̢Ϩx 10%qQEҡСЁxŸ‫ש‬rruǬŸdFҡСx̠ ЃRЀwßn

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ϰRγȝӰREíuϓͦʬŠunRpŠ̸ӰmjF¤ÛÄ×uxE¢Ø¨³ÙÞ×ѯСEÀÖ×ÀÛѯСE‫ר‬ӂСw 3 м‫ב‬wҡСġϰbjFjEӵ‫͛־‬խVҡСwʬŠƪȝdjuE͟θϠՁwԌȨӰmjF͟θϠՁuxE¢Ø¨³ÙÞ×ƙ{ÀÖ×ÀÛġϰbjF

ҡСƙ{͟θϠՁw‫׏‬ʆ֛ϵŃ͹ՒbEҡСɵʬwͦɢunRpғȨbjFȞ‫ל‬ѯ̻rbpxE
FE-SEM ϰRjŠ̸qxE¢Ø¨³ÙÞ×ѯСw‫׏‬ʆ֛ϵŃVxE¢Ø¨³ÙÞ×uՄǋdÄØÞµϢw͛խЧԟqXj(Fig.1)FÀÖ×ÀÛѯСƙ{‫ר‬ӂСqxEÀÖ×ÀÛ×¦ÍƭѸБϢw͛խЧԟqXj (Fig.2)FjE͟θϠՁqQ¢Ø¨³ÙÞ×w‫׏‬ʆ֛ϵŃVEÄØÞµϢw͛խЧԟqXEÀÖ×ÀÛVxѸБϢw͛խЧԟd^rWqXjF

EDS ϰRjŠ̸qxE¢Ø¨³ÙÞ×ѯСVECaENaES tswϓͦʬŠW͕ş`jF
jEÀÖ×ÀÛѯСƙ{‫ר‬ӂСqxECaENaESEAlEP tswϓͦʬŠW͕ş`jF

Fig.1 Microscopic image of cholesterol stoneFig.2 Microscopic image of bilirubin stone― 113 ―

P-40nrHrũŰśƕ­|ƙÈƌ5ĖïĎľŌś»(ĹÃËďË(ŢéÿËƆļĮ5zïĎľŌ(ĳÏƍ%ľŌ«(²ġďË(Çôñ

Analysis of viscoelastic properties of plant cell wall by the laser-induced surface
deformation microscope: Regulation of tip growth and mechanical propertiesof the cell wall by reactive oxygen species in plant cellsB͒ğĪѡ 1EǹԶĄЦ 2E̫ͥТʌ 3E̬Θƶɞ 3,4EϲüȚ΍ 1,21̵āϬдǹȕ Тс˘հͦ͛ ѺƨТс֧ Þ®ÞÂÙÛ³¤Û¨&³»Ù§ÞТсªÛ®ÞE2 ̵āϬдǹȕ Ϭȕքъßք ƂȕдE3 ̵āϬдǹȕ Тс˘հͦ͛ ѺƨТс֧ÎÞ§ÛÂÙÛ³ªÛ®ÞE4 ̵āϬдǹȕ ϬɌȕք ʍϰϮϠдȕд
1
2

Water Frontier Science & Technology Research Center, Tokyo University of Science,

Department of Chemistry, Tokyo University of Science, 3Imaging Frontier Center, Tokyo Universityof Science, 4Department of Applied Biological Science, Tokyo University of Science͔ϠxE̠ӵȿu˶Њ nm wƓwѫҥǮЇո`fpUEЇϮϭǫʍѐwնкqhwŶȕЋʓՁŨʄdFʭGxE¦Ù¹·©·w͇ͺ 1Eӄњє 2 Ï´×͔Ϡ«¸£ wČ͇w
͙ʓˉmjňшʬ֜uEΚʓ֊Ѩм(ROS)wп͙ЋtϮʬWʋԃqQ^r̈VubjF^quØÎÞ®EAFM ϰRpѫҥǮwѝɳʓWԑγ`pRFbVbEØÎÞ®ϰRjԑγqxEѭ҇jxѫҥ 1 İuU\ďʞwę҉qwԑγxäƢҦqQEAFM ԑγqx
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bjEµm ¨ Þ×wȬԱwŽЋѝɳʓֽ˗ԏԑγƢҦtØÞ¥ÞԡՄӵ‫־‬ǵę‫׬‬LISD‫׏׭‬ʆ
֛ 3,4 ͔ϠѫҥuţpʍϰbE«¸£Č͇wňшʬ֜̎wѫҥǮwѝɳʓϡʓEROS w

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ʳΒw͔Ϡѫҥ}wʍϰwƢҦʓrEROS Ċԫ֤ȡűwɹׂ ƭj͙ʓňшʬ֜wŨʄunRpԭԨdF[1] S. Takeda et al. Science, 319, 1241 (2008). [2] Kaya et al., Plant Cell 26, 1069 (2014). [3] T. Morisaku
and H. Yui, Analyst, 143, 2397 (2018). [4] T. Morisaku, et al. Anal. Sci., in press.

― 114 ―

P-41űŢƙÈƌ5Ė¤xƚ°ŎĠĕâ(BoeQpñſ­(š·%ôōŢá

Super-resolution imaging by STED microscopy of the chromatin-structural changes indeveloping cerebral cortexBɜ֎ƶɑ 1EΓɜ̇ß 1Eϱêt 1EŸӥӣ 11ϯ͘ʸӱѺƨТсʱ½Î´×Тсք֝

BKazumi Hirano1, Masakazu Namihira1, Minami Tanaka1, Kaoru Kato1
1

National Institute of Advanced Industrial Science and Technology (AIST) Ƽõ‫ב‬wǹҮЍՁwǸ͜tЮѮѫҥ‫¸׬‬ÒÞÙÛ‫׭‬xEңϮ̧wЮѮɟѫҥVЇϮͶ֭ĤȓЋuϯϮ`F^wЮѮɟѫҥV¸ÒÞÙÛ}wŠƂնкuURpEмGwտĔȑWϡʈЋtЇϪ͜ɭrFĢTyEЮѮɟѫҥuϡϺЋuЇϪdտĔȑ‫׬‬Sox2EPax6 ts‫׭‬xŠƂնкqЇϪWĚãbEß˽E¸ÒÞÙÛqϡϺЋuЇϪdտĔȑ‫׬‬Dlx2 ts‫׭‬xŠƂնкqЇϪWǬŸdF^wStտĔȑЇϪwŨʄuxE¿¨µÛ H3 ®Û¾Ձ̪шwÎ°×Ƃª°×ƂĮ‫ז‬uÙË°Û͛խǵ˜W֍ԃtɺų̻jbpR^rWПpRF^qwЮѮЇϮŨʄdÙË°Û͛խǵ˜u֡dТсuURpEǸ˶wѫҥVʃj DNA®Û¾ՁȞ‫˹̰ל‬rbjÙË°ÛŋϾ·֥ΒtswŠȑϮϠȕЋʳΒWԎ̸wêʊqQ
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ɕȯɠɎȥɣȸĢĳȎɎȥȴȵȧɄɣȷȹȌǲǷȠ LPS ȎȦȸɛɉɡɄú

Adjuvant effect of LPS to Phagocytosis in macrophages.
ǹƚ ˄ó 1 ‫י ̫ͥװ‬īȑ 1,21ƇӚɌ͘ǹȕɌȕТсдϮƵϭǫдȕȯˮ‫װ‬2 ƇӚɌ͘ǹȕňհɌȕքϮƵдȕд‫װ‬
Takuya Otomo1‫װ‬Kahoko Hashimoto1,2

1

Chiba Institute of Technology, Graduate School of Engineering, Department of Life and Environmental

Sciences, 2Faculty of Advanced Engineering, Department of Life Science.
 һϕŋϾƜʍwêʊЋɺųrbpłZËÙÂÞ§x‫װ‬ʼƔwƞ՜ÝŠԎӰR‫ͣװ‬Ϣѫҥƪ͜‫װ‬T ѫҥuȬbpʼƔ˛ЪӰS‫ײ‬ËÙÂÞ§x‫װ‬ѫҥӵ‫־‬w PRR Šȑ TLR4 (Toll
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ΰȴx 12 ̎֠ʀVԅj‫^ײ‬w LPS uūψw̎֠ĤȓЋtǵƂx̀ɼТсqwǤƱrßҽd‫^ײ‬wʼƔƞ՜Ҧwΰȴx‫װ‬ËÙÂÞ§w LPS uūψwѯ̻rbpw‫װ‬ʼƔŠԎҦwĩհ‫װ‬QRxƞ՜ҦwĚãu֡åbpRrғT‫ײ‬jÂÙÞ¤µÎµÖÞԎ̸u‫װ‬LPS uūψump‫װ‬ȳ`t¤©wËÙÂÞ§ִǌWЧԟ`j‫ײ‬ßքwѫҥִǌx‫װ‬ѫҥœwȳҥwǬŸtsӿֵ`Ǭbj (SSC ĴwǬŸ) ‫ײ‬ѫҥ¤©wΰȴx‫װ‬ʼƔƞ՜wնкqȳҥwҶʬŠrbpѫҥՁҶWϰRjj‫װ‬ѫҥҶ‫־‬пuΰȴWjrғT‫ ײ‬LPS ūψxʼƔwƞ՜ҦǬǹ`fß˽‫װ‬ʼƔʻåfe LPS ūψwq ѫҥ¤©wΰȴrѫҥœȳҥwǬŸWj^rV‫װ‬ѫҥҶϲ̴wȳҥk\WƔǋqxtRrғTj‫ײ‬jѫҥwӿֵ`wǬŸx‫װ‬ѫҥ¤©wΰȴĕmjѫҥҶϲ̴wȳҥwǬŸWƔǋqQ‫װ‬ŸTp LPS WÞµÂ§ÞԡȲdrRSǤƱuSt‫װ‬ϺϠƞ՜ÞµÂ£¬ÞÍ ǬŸbjjrғT‫ײ‬ §Ò½ÛµqQ LPS uËÙÂÞ§wΚʓƂu֡bp‫װ‬ŠȑѫҥȕЋtԎ̸V‫װ‬
LPS WȲZËÙÂÞ§wΚʓƂxʼƔ˛ЪҦwǵƂuɹׂЪdr÷γb‫װ‬ʼƔ˛ЪҦϧʃbjËÙÂÞ§r T ѫҥrwŐǟ‫ח‬Ӱmj‫ײ‬T ѫҥWϯϮd¤µÛ֏wǵŽxʼƔ˛ЪҦwǬΰrbpԙĥbj‫ײ‬ċâwԎ̸V‫װ‬
LPS  IFN- (Interferon- ) uʼƔ˛ЪѫҥwΚʓƂx‫װ‬ʼƔwƞ՜‫װ‬
ŠԎU{ T ѫҥ}wʼƔ˛ЪuȬbpɹׂƙd^rẄVutmj‫^ײ‬unRpÂÙ
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Imaging intracellular temperature of mouse brain sliceBɂքɯǠ 1Eֲ̊‫ נ‬1E΅ԯӻù 1Eȳɀ֬ǻ 1EӀΘ‫נ‬ʌ 11̵āǹȕǹȕ֧ӤȕѠТсд

BKohki Okabe1, Yutaka Hoshi1, Yuji Ikegaya1, Ryuta Koyama1, Takashi Funatsu1
1

Graduate School of Pharmaceutical Sciences, The University of TokyoβɥxEĊԫÖ©ÍrRmjϮϬͦҦu֍ǹtɹׂåTpRF^quʭGxϮѫҥœuռʍƢҦtӪŉʓÊÖËÞβɥªÛ¤Þ‫׬‬Fluorescent polymeric thermometer, FPT‫֟׭‬ЇbE^wʍѐȝ֏ЋӪŉÎÞ§ÛΒu͕şd^rqϮѫҥœwβɥγȝϮѫҥwβɥÎÞ§ÛոʬbjFβɥWѫҥwͦҦΚʓuΨZ֡ådǋȑrbpΔБִpR
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̆xEЮѮΚŽĤȓЋЋqQ^rЇԅbjFċâwѯ̻VEʭGxӦӯ̎uURpЮѮΚŽuЮѮѫҥœwЇϚWβɥʠƟʓ TRPV4 ΚʓƂbE^Wѫҥœ}w;wΛōԡՄbEҮΡұ}հȽdrw˼ԆÏ´×˛ЪdF̫ТсqxEЮѮѫҥœuU\βɥÎÞ§ÛΒ֟ЇbEЮѮΚŽЮѮЀϬuU\ѫҥœβɥǵƂw֡åЇԅbjF^wѯ̻xEѫҥœuU\βɥǵŽWϮϬΚŽuԴϥbpR^rɲZˬˉbpUEβɥˊ͟rbj˼ԆwϮϬȕÝϮϠȕwЇȽW̧ɾ`F― 117 ―

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BKazuki Niwa, Kaori Hattori, Daiji Fukuda
National Institute of Advanced Industrial Science and Technology (AIST)ӪŉwStÃÙÞ¶tŉ¦·×ŠŉԑγdǥƨEիəxŠŉѨȑьŦϰbpŉΓ
֜_ruŠֶbEŉ´³®uγȝdFbVbǊʽ͈ȑьwΓ֜Š˳ѨȑrØǛ´³®ϰRǥƨEhiwİťw´³®uȻZŉ¦·×xΓ֜_ruŠ\pΰȴdFÂ×®ьwŉȕѨȑϰRǥƨEƮƝEƜȰьuExŉ¦·×xΰӶdFhwjEŠŉѨȑьŦϰd^rtZŉ¦·×wΓ֜ʛǤʃ^rWqXyE
ǹɚt͕şʠɥw˭ǂW̧ɾqXF‫נ‬ʠɥtŉ͕şǈqĊӵЋtŉָȑǬıє‫׬‬PMT‫׭‬xEŉw̠ȳƌęqQŉȑ‫״‬nenԑ
γd^rWqXEÂµÛÛ®Þϰw͕şǈrbpɠZŦϰ`pRFbVb PMT x͕şbjŉȑ‫״‬nzrnwΓ֜ʛǤγȝd^rxqXtRFŉȑwΓ֜xEɭ E=h6 uEº×ÞrʛǤrГ֡WQFÂµÛÛ³Ûd֯uEŉȑwº×ÞВ˗ԑγd^rWqXyEс͙u‫נ‬ʠɥtŠŉγȝWȞϪqX^rutFŉȑ‫״‬İwº×ÞxEĢTyΓ֜ 550 nm q 2.3 eV qQFnE˶ØµÙÛÉ×µwº×Þԑγd˽ΒWQyEƌßŉȑwº×ÞВ˗ԑγd^ruŠŉγȝWƢҦutF^ w  S t ʆ ȴ t  º ×  Þ w γ ȝ  Ƣ Ҧ u d  w W E Յ Ĕ Ȳ Ր и ш ª Û ¤ (TES;
superconducting Transition Edge Sensor)qQFՅĔȲĜŚƐdrEՅָȲՐишuURpəĔȲϢʡVՅĔȲϢʡuʒψuՐиdWEhwβɥɚx˶ÌÖ

×ÀÛqQFhwjEՅĔȲĜu‫״‬İwŉȑWϖȰ`Ehwŉȑwº×ÞuՅĔȲĜwβɥWâ̆d֯wʿ
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FjEŉȑx TES uƮƝ`pϚuǵ˜``TdyΓ֜ʛǤƭ͕ş`wqEɠ
RΓ֜іǎuj‫נ‬ʠɥʓҦȞϪqXFȞ֯E2500 nm кɥwՠՂǷuʠɥ̢bpR

F^wSu TES xE͙pʠɥw‫נ‬RŠŉ͕şǈrbpʍϰdƢҦʓˉmpRF̫ЇӵqxETES uŠŉγȝwȞ֯rEŠŉÎÞ§Û}wʍϰԚ‫ל‬unRpѬĆdF
Niwa K, Numata T, Hattori K, Fukuda D, Scientific Reports 7:45660 (2017)― 122 ―

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ÏƍƋkhldT98Ƙ§(8BQp(çOp\Bŭ^7Ip(ôōŢéRole of actin bundling protein, fascin, on lammelipodia of growth coneBϲêt 1,2EӦüӼѢ 3Eɜ֏ƶɒ 1EТɊӂͣ 4EɂɉȔ΍ 3EŸӦӤ 11

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Kaoru Katoh1
1

National Institute of Advanced Industrial Science and Technology (AIST), 2 Grad. Sch. Life & Env.

Sci., Univ. Tsukuba, 3Grad. Schl. Inform. Sci & Tech. Univ., Hokkaido 4 Gunma Pref.Coll. Health Sci
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1

Department of Bioscience and Informatics, Keio University
2

Department of Applied Chemistry, Keio UniversityËº¦ÍÛ‫׿‬Mg2+‫؀‬wǻYvѹҳͰҴtʑ‫ח‬v 2 ĦֻÛpPDѹҳŕpv֙ѶΥʙvԴѣDÌµ¢Û¶ÖtT[ ATP ϼϻѹҳŕpv ATP ίՉDȷҳĝtT[®Û¾ՐѓĝͥսvȜȡƄsrtγYֱloQEiDѹҳŢԆv‫׀‬t͏ŕ Mg2+ϕɫVѰ 0.6
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Microscopic world observed with optical microscopy‫ۑ‬ຍ⸨⸅ 11⏘ᴗᢏ⾡⥲ྜ◊✲ᡤࣂ࢖࣓࢜ࢹ࢕࢝ࣝ◊✲㒊㛛‫ۑ‬Kaoru Katoh1

1 National Institute of Advanced Industrial Science and Technology (AIST)ගᏛ㢧ᚤ㙾ࡣ”࣐࢖ࢡࣟ” ࢫࢥ࣮ࣉ࡜࠸࠺ྡ๓ࡢ㏻ࡾࠊ࣐࢖ࢡ࣓࣮ࣟࢱ࣮ࣞ࣋ࣝࡢ⌧㇟ࡢほᐹ࡟౑ࢃࢀࡿගᏛჾᲔ࡛ࡍࠋࣞࣥࢬ㸦ᑐ≀ࣞࣥࢬ㸧ࡢ↔Ⅼ㊥㞳ࢆ fo ࡍࡿ࡜ࠊfo 㹼 2 fo ࡢ⠊ᅖ࡟ヨᩱࢆ⨨ࡃ࡜ࠊᣑ኱ീ㸦ᐇീ㸧ࡀᚓࡽࢀࡲࡍࠋࡇࡢീࢆ᥋║ࣞࣥࢬࢆ⹸║㙾ࡢࡼ࠺࡟౑ࡗ࡚ᣑ኱ࡋほᐹࡍࡿࡢࡀ᭱ࡶ༢⣧࡞㢧ᚤ㙾࡛ࡍ㸦ୗᅗ㸧ࠋࡇࡢࣉࣞࢮࣥࡣࠊᚋ࡟⥆ࡃㅮ⩏ࡢ࢖ࣥࢺࣟࢲࢡࢩࣙ
ࣥ࡜ࡋ࡚ࠊ᭱ࡶ༢⣧࡞ࣞࣥࢬᵓᡂࡢ㢧ᚤ㙾㸦ୗᅗ㸧ࢆ♧ࡋࡓ࠺࠼࡛ࠊᵝࠎ࡞✀㢮ࡢගᏛ㢧ᚤ㙾࡛࡝ࡢࡼ࠺࡞ࢧࣥࣉࣝࡀࠊ࡝ࡢࡼ࠺࡟ぢ࠼ࡿࡢ࠿ࠊᴫㄝࡋࡲࡍࠋᫎീࢆぢࡿࡇ࡜࡟ࡼࡗ࡚ࠊࡇࡢᚋ
࡟⥆ࡃࠊྛ✀ࡢ㢧ᚤ㙾ࡢ࢖࣓࣮ࢪࣥࢢ࡟㛵ࡍࡿㅮ⩏ࢆ⌮ゎࡋࡸࡍࡃࡍࡿࡇ࡜ࢆ≺࠸ࡲࡍࠋᫎീࡣࠊ
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⏕ࡀ᧜ᙳࡋࡓṔྐⓗព⩏ࡢ࠶ࡿ⏬ീ௨እࡣࠊ⚾⮬㌟ࡢᡭ࡛᧜ᙳࡋࡓ⏬ീࡢࡳࢆ౑⏝ࡋࡲࡍࠋᅗ㸸ගᏛ㢧ᚤ㙾ࡢᶍᘧᅗࠋ  ᑐ≀ࣞࣥࢬ࡛ࠊヨᩱࢆᣑ኱ࡋࡓᐇീࢆసࡿࠋࡇࡢᐇീࢆ᥋║ࣞࣥࢬ࡛ᣑ኱ࡋほᐹࡍࡿࠋ― 127 ―

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Diascopic microscopy with focus on Bright field, Phase contrast and DICBáȖіǼͅɭēЬ¸¢Û
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Hamamatsu Photonics K.K.
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― 132 ―K-7ගᏛ㢧ᚤ㙾ࡢศゎ⬟࡜㉸ゎീ㢧ᚤ㙾esol tio limit o optical microscope a d s perresol tio microscope‫ۑ‬ຍ⸨⸅ 11⏘ᴗᢏ⾡⥲ྜ◊✲ᡤࣂ࢖࣓࢜ࢹ࢕࢝ࣝ◊✲㒊㛛‫ۑ‬Kaoru Katoh1

1 National Institute of Advanced Industrial Science and Technology (AIST)ගᏛ㢧ᚤ㙾ࡢศゎ⬟ࡣࠊගࡢἼ㛗࡜ࣞࣥࢬࡢ㛤ཱྀᩘ࡛ࡁࡲࡾࠊᨵၿࡍࡿࡇ࡜ࡀ࡛ࡁ࡞࠸࡜ಙࡌࡽ
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⏝࠸ࡲࡍࠋ― 133 ―

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Airyscan: next-generation microscope detector beyond the confocal pinhole apertureB֡Ɋ̈Ϯ 1, 2
1Þ×²¨ͅɭēЬ ËÙ¨¢ÁÞ ´ÌªÞ×¨2‫ט‬օǹȕ̵ā ϬɌȕТсд ЮѮŠȑͦҦ
BAkio Sekigawa1, 2
1

2

Academia Sales Dept., Carl Zeiss Co., Ltd.

Lab. Molecular Neurosci., Dept. Biological Sci., Tokyo Metropolitan Univ.

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ƢҦubpRF― 134 ―

K-9űŢƙÈƌ

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RdF― 135 ―

K-10STEDűŢƙÈƌäß:hrJpC
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Leica Microsystems, Division of Life Science Research̩ŉіvÕÂ¤Û¨ЯяtTQoDʌѹtDͶдtDѹҳvſʧ˓ſԚȬcitwDԚȬciv²Þ×pPD“‫נ‬ʌ֫”¦¨³ÍvրƄV̩ ֝ԑsԑѶqs
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Dʈ̽v҉ӸŊΝ֬ǡtźSoDՑӸŊTzհՑǺΝ֬‫י‬ǡvӸŊӐѶtSTEDÎÞ§ÛtȰʓaoQEiD̃STED 775 nmØÞ¥ÞϽQ]qpXYɢ‫׏‬30 nmqQRŢԜҴȢϷaoQEŒϠϝЂń         STED Ђń   ʌȷѢ‫׿‬STAR635P‫؀‬vŒϠϝЂńq STED ‫׿‬775 nm‫؀‬Ђń

― 136 ―

K-11
ĕ,,(Ŏ5-3±ƙÈƌB͇̫Пɑ 11ƃ΢շǹȕָȑдȕТсʱ
BTomomi Nemoto1

1

Research Institute for Electronic Science, Hokkaido University

Two-photon excitation fluorescence laser-scanning microscopy (TPLSM) has become general
and widespread to the various fields of life sciences in this decade. Especially in the field of
neuroscience, “in vivo” TPLSM has revealed vital information on neural activity for brain
function. On the other hand, in the era of “connectomics”, visualizations of morphology andactivities of numerous neurons in vaster regions in the living brain are required within a shortperiod.
Recently, we have developed we developed novel TPLSM that uses a 1064 nm gain-switchedlaserdiode-based light source with average power above 4 W, pulse width of 7.5-picosecond,
repetition rate of 10-MHz, and a high-sensitivity photomultiplier tube [1]. It enabled tovisualize pyramidal neurons in the hippocampal CA1 and in the hippocampal dentate gyrus(Fig. 1). In addition, we have tried adaptive optics to compensate spherical aberrations during“in vivo” observation of deeper layers in living mouse brain. We then improved the fluorescentsignals from Layer V pyramidal neurons and the spatial resolution. By utilizing thesetechniques, we next carried out “in vivo” laser ablation of neural fiber at over 500 m depth
from the brain surface (Fig. 2). Moreover, we have successfully improved the spatial resolutionof TPLSM by taking advantages of STED technology [2]. In this presentation, we will discussthese improvements and future application on the basis of our recent data.

ƥƾǕǓƭƥưƸƥǤǕǘƥǟǕǟǙǥƥǖǍǜǑǛƥǍǎǖǍǝǕǙǘƥǙǒƥǘǑǞǛǍǖƥǒǕǎǑǛƥ
[1] R. Kawakami, et al., Biomed. Opt.

Express, 6 (2015) 891.
[2] K. Otomo,, et al., Biomed. Opt. Express,ƥƾǕǓƭƥƯƸƥǤǕǘƥǟǕǟǙǥƥǕǗǍǓǕǘǓƥǙǒƥǏǙǛǝǕǏǍǖƥǍǘǐƥ
ǔǕǚǚǙǏǍǗǚǍǖƥǘǑǞǛǙǘǜƥǕǘƥǍǘǑǜǝǔǑǝǕǢǑǐƥǗǙǞǜǑƥ

9 (2018) 2476.

― 137 ―

― 138 ―

K-13
cOm(

$-3ľŌ(vęVisualization of cell dynamics using the light of firefly
Bՠ΄ԯŊӻ 11ϯ͘ʸӱѺƨТсʱ½Î´×Тсք֝
BYoshihiro Ohmiya1

1

National Institute of Advanced Industrial Science and Technology (AIST)ѡŅŮ  ɝϮwÖ¦ÐwƻȕҔÖ¨µ³Ø¨xͱk‫ף‬Wŉ^rŉ»¢W
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ТсWհȽbnnQF իəEGFP xȬԱrt®Û¾ՁrӫƨbѫҥœqЇϪ`f^rq‫װ‬ȬԱ®Û¾Ձw
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― 139 ―

K-14
ɉȧȫȧɘɣȸɡȰȌƇȢȠlƊăŉƅāƥƥ○Ȥҷ˻Ʀ 1,2
1ǔѓЯя֯ДΜĄϹƄșЯяʸ ҼлѼсșЯяªÛ®Þ2ǔѓЯя֯ДΜĄϹƄșЯяʸ Ŋ֟ȕɑșЯяªÛ®Þ○Atsushi Miyawaki1,2

1

RIKEN Center for Brain Science, 2 RIKEN Center for Advanced Photonics

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澤田

平

Ｐ２０

Ｐ１６
Ｐ８

田

Ｐ１８

LS２−３、Ｐ１３、P３０

田

Ｐ３２

島

村 晃大

Ｐ９

島野

村 宏

Ｓ３－６

大

Ｐ１４

Ｋ１２

豊

LS２−４、Ｐ５０

政

部

Ｐ３８
Ｓ３－４

Ｐ１８

一

LS2-2

津 和

Ｐ１４、P２０、P２６、P４０

治

Ｐ１８

保 美香子

Ｐ２

澤

徳

Ｐ１２

保 泰

Ｐ２８

本 憲治

Ｐ７

Ｐ３７

山 正明

P５

Ｐ２７、P２８

崎

Ｐ２４

倉岡

子

光

倉

平
昌

Ｐ２０

和

LS2-2

雄

LS2-1

章一

LS2-2

Ｐ４５

治

川

光

澤
み

LS2-2

LS２−４、Ｐ５０
S1a－１
Ｐ３１、P３８

之

村

Ｓ３－２

田

Ｐ１２

野倉

Ｐ２

Ｋ３、 ６

島 正樹
衣
林 圭
裕昭

P５

口

史

Ｐ２７、P２８

Ｐ２、P６

川 明生

Ｋ８

Ｐ１５

山 翔

Ｐ３７

Ｐ４５
Ｐ４５

山

Ｐ４３

田

Ｓ４－２

公平

髙川

― 144 ―

Ｐ３７、P４４

Ｐ２６

高田 英昭

Ｐ２９

中野 明彦

LS2-1

高橋 和浩

LS2-2

中野 寧

Ｓ４－２

髙橋 圭介

Ｐ７

中村 岳史

Ｐ１２、Ｐ２２

高松 哲郎

Ｓ４－１

中村 百花

Ｐ６

多喜 正泰

Ｓ２－３

中山 俊憲

Ｐ３３

瀧口 優

Ｐ３

波平 昌一

Ｐ４１

武政 徹

Ｐ４７

行方 衣由紀

Ｐ１０

竹内 公平

Ｐ１２

奈良 雅之

Ｐ２３

武田 紘平

Ｐ４７

田島 鉄也

P1

西澤 志乃

Ｐ４６

田代 充

Ｐ２

西脇 大介

P1

田中 悠介

Ｐ１０

丹羽 一樹

Ｐ４８

田中 響

Ｐ１２

田中 直子

Ｐ１６

塗谷 睦生

Ｓ２－１

田中 みなみS３−１、Ｐ４１、P４９

田中 光

Ｐ１０、P１６

根本 知己

Ｋ１１、P１５、P３６

田中 睦生

Ｐ４５

田之倉 優

S1a－２

野田 尚宏

Ｐ１９

田村 康

Ｓ３－５

野々村 賢一

Ｐ２０

に

ぬ

ね

の

つ

は

津田 栄

Ｐ２７

萩原 雄樹

Ｐ２６

土屋 章一

Ｐ２５

萩原 芙美子Ｐ３８

橋本 研志

P１４、Ｐ２６、P４０て出村 茉莉子Ｐ２

橋本 香保子

Ｐ４２

寺林 杏理

Ｐ６

長谷川 明洋

Ｐ３３

照井 翔

Ｐ２２

長谷川 実咲Ｐ１４

長谷部 光泰

Ｐ３６

と

戸井 基道

Ｐ２７

服部 香里

Ｐ４８

東ヶ崎 健

Ｐ４６

服部 淳彦

Ｐ２３

土岐 精一

Ｐ２０

花俣 繁

Ｐ２０

徳永 正之

Ｓ４－２

馬場 嘉信

Ｐ９、P２４

利岡 文美

Ｐ２５

濱 裕

P1

豊田 晴義

Ｐ３

濵口 正悟

Ｐ１０

原田 雅史

Ｓ４－４

な

永井 健治

Ｓ２－４

長崎 晃

Ｐ３２

― 145 ―

Ｐ１４
口 香

P1

光田

平岡 泰

Ｐ２９

光山

泰

Ｐ３４

平

P1

島

文

LS２−３、Ｐ３０

平田

樹

平野 和己

Ｐ４５
Ｐ４１、P４９

P３２

正和

LS2-2

也

S1a－２

川

Ｋ２
井

一

Ｐ２９

代 大

LS2-1

井

LS2-2

本

Ｓ３－４

田 大治

Ｐ４８

本 大

Ｐ２６

永

Ｐ２０

脇

Ｋ１４、P１

山

Ｐ１１

井 裕紀

Ｐ４９

村 章子

Ｐ２８

村田

Ｐ３６

S1

村田 香

Ｐ７

内

P1

史

史

理

－３

津 高志

Ｋ５、S３−３、P２５、P３５、P４３

澤 直子

Ｓ４－２

Ｐ３８

俊紀

Ｐ４０

雄高

Ｐ４３

島 健

P５

田

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田 雅

Ｐ１９

雄一郎

Ｐ１３

本 康

Ｐ２

本多

明

Ｐ３５
宏和

松井

谷中

S1a－１、P５

優

Ｐ２２

子

S1a－１

松井 裕史

Ｐ１８

松

子

Ｐ４６

山口

実

S1a－１

松田

志

Ｐ２９

山田

文

Ｐ４５

松村 義

Ｐ２、P６

山中

松山 哲也

Ｐ７

山本

山 雄介

Ｐ２３

山本

山 一雄

Ｐ３１、P３８Ｐ１８LS２−４、Ｐ５０
郎
子

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み

和

本

Ｐ２７、P２８

由井 宏治

Ｐ２１
LS2-2

S２−２、Ｐ９、P２４
Ｐ４０

代

Ｐ２８

志樹

Ｐ２４

田

Ｐ５

Ｐ３９

田

Ｐ４４

― 146 ―

田

由

Ｐ８

田 和子

LS2-2

P
Rawin Poonperm

Ｐ２９Elisenda Rodriguez

Ｐ４

R
明

Ｐ３９
S

和田 健

Ｐ７

Dasa Siva

Ｐ３１

大

P５

Peter T.C. So

Ｐ３

Mriganka Sur

Ｐ４

I-Hsuan Wang

Ｐ１１

Yi XueＰ３

B

W
Archana Bajpai

Ｐ３４

Benjamin B. Bartelle

Ｐ４

X

Vincent Breton-ProvencherＰ４
E
John T. Elliott

Ｐ１７

Brent French

Ｐ３１

Jingchi Gao

Ｐ１３

Michael Halter

Ｐ１７

Alan Jasanoff

Ｐ４

Unga Johan

Ｐ３８

Kimberly Kelly

Ｐ３１

Alexander Klibanov

Ｐ３１

Jiyoung J. Lee

Ｐ４

Nan Li

Ｐ４

Tiago JS Lopes

Ｐ１１

James Melican

Ｐ４

Gabriele Neumann

Ｐ１１

Kien Xuan NGO

Ｓ１

F

G

H

J

K

L

M

N

－２

― 147 ―










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2017年度決算書 (2017年1月1日～2017年12月31日）

日本バイオイメージング学会
会長

一般会計
収入

船津

高志

印

理事(財務担当） 太田

善浩

印

支出

2016年より繰越
利息
会費
第25回学術集会余剰金
懇親会費
許諾抄録利用料
国際学会参加費4,663,788
11
991,000
577,843
63,0002,160
88,000

バイオイメージング印刷費
ジャパンメディカル英文校正
通信・郵送費
謝金・人件費
男女共同参画奨励賞
会議費214,110
38,914
91,27819,8007,000
100,000
122,160

収入計

6,385,802

振込手数料
学術集会準備金
交通宿泊費
過払い会費返金
HP作成維持費
雑費

6,480
300,000
112,720
6,000
629,300
112,095

特別会計
収入1,759,857

2018年度への繰越

4,625,945

支出計6,385,802

支出

2016年度より繰越

5,000,000

収入計

監査

小計

5,000,000

2018年
監事
監事

月
川西
大幡

徹
久之

国際学会準備金

709,3312018年度への繰越

4,290,669

支出計

日
印
印
― 158 ―

5,000,000

2019年度予算案(2019年1月1日～2019年12月31日）
一般会計
収入
繰り越し
会費

収入計

支出
4,626,337
991,000

バイオイメージング印刷費
Bioimages アップロード費
ホームページ管理費
謝金・人件費
英文校閲費

250,000 広報
300,000 広報
100,000 広報
150,000 庶務、会計
80,000 編集

5,617,337

会議費
通信・郵送費
奨励賞･研究助成
男女共同参画（分担金 他）
学術集会準備金
雑費
予備費

120,000 庶務
100,000 庶務、会計
100,000 賞選考
84,000 男女共同・国際
300,000 集会
30,000 庶務・会計
4,003,337

支出計

特別会計
収入
繰り越し
収入計

5,617,337

支出
4,290,237

2020年度への繰越
国際学会準備金

3,290,237
1,000,000

4,290,237
支出計― 159 ―

4,290,237

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ʥʪҍǪǹȕϬɌȕքϮƵʛǤȕд ϮϠϠϬÝЮѮʛǤȕТсȟœָԜ‫׽‬042-676-5498‫׾‬FAX‫׽‬042-676-5863
E-mail: office@j-bioimaging.org
URL: http://j-bioimaging.org/➨  ᅇ᪥ᮏࣂ࢖࢜࢖࣓࣮ࢪࣥࢢᏛ఍Ꮫ⾡㞟఍ㅮ₇せ᪨㞟        ᗈ࿌ᥖ㍕௻ᴗ୍ぴ㸦ͤ஬༑㡢㡰ࠊᩗ⛠␎㸧⾲ ࢯ࣮ࣛ࣎ࢪࣕࣃࣥᰴᘧ఍♫⾲ ᰴᘧ఍♫ࣇ࢓ࣥࢣࣝ⾲ ࢡ࣐ࣟࢸࢡࣀࣟࢪࢪࣕࣃࣥྜྠ఍♫ᚋ௜ᰴᘧ఍♫࢔࣮ࢺࣞ࢖
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⌮⛉◊ᰴᘧ఍♫蛍光顕微鏡用 品質管理ツール
毎日使っている蛍光顕微鏡、正しく校正していますか？アルゴスライド は取り扱いが簡単
で3年以上安定してご使用頂けます。
従来方式の蛍光ビーズや蛍光板では不可能だった、照明の均一性、強度応答性、スペクトル応答性など、一度に複数の項目を管理することが出来ます。

疑いの排除

簡単にデータを記録、共有可能

取り扱いが容易信頼性の高い検査結果を提供します。
異常検出時には推定要因に素早くアクセ

データを自動で記録し、選択した専用フォ
ルダーに保存します。データは共通の消耗部品等を新たに購入する必要はありません。

スし、回復させます。

フォーマットで保存されます。

通常の光学部品と同じで冷蔵不要で、保管、取り扱いが容易です。

Daybook 品質管理システム は、極めて安定性に優れた検査用ハードウェアと非常に効率的な画像処理ソフトウェアを組み合わせたもので、蛍光顕微鏡向けの迅速で信頼性の高い品質管理ソリューションを提供します。

ハードウェア

お問い合わせソフトウェア〒101- 0052 東 京 都 千 代 田 区 神 田 小 川 町 1 - 1

TEL：03-3258-1238（代） FAX：03-3258-5689
URL：www.klv.co.jp E-mail：toiawase@klv.co.jp●記載内容は、改良のため予告なく変更する場合がございますので、ご了承ください。

Super resolution STED microscopesfrom its inventors

z
z
z

z
z
z

超解像顕微鏡 解像度評価ツール

ナノルーラー

DNA折り紙技術により製造された「ナノルーラー」は2点の蛍光色素が一定の幅（6〜350nm）で発光します。
ナノルーラーは、ドイツGATTAquant社が開発しました。

◎超解像顕微鏡の性能確認◎均一サンプルによる顕微鏡の性能比較◎トラブルシューティング
対象顕微鏡・SIM/STED／共焦点顕微鏡
・STORM／DNA-PAINT
画像例
DNA- Paint ナノルーラー

GATTA-STED 90R ナノルーラー

3つのスポットを持つタイプです。

（幅：40nm、ATTO655）（幅：90nm）（幅、
蛍光色素）
各種ラインナップあり、カスタム対応も可能です。

SIM（90〜160nm）

STED（50〜120nm）

Confocal（270〜350mm）

DNA- PAINT（40〜80mm）

製品の詳しい情報はホームページ、
又はお気軽にご連絡ください。 ナノシード 検 索
株式会社
https：//nanoxeed.co.jp/

ナノシード〒182- 0022 東京都調布市国領町 2-5-15 コクティー3F スモールオフィス
info @ nanoxeed.co.jp
03- 4405- 3913

約

※の

Y

分解能

スピニングディスク共焦点をベースにした超解像技術で光学的に約倍分解能が向上しました。さらにデコンボリューションを行うことで、最終的に光学限界の約 倍の分解能を実現します。
※：デコンボリューションを含めた場合の参考値

アプリケーション例：
細胞の成長円錐
画像ご提供：
産業技術総合研究所 バイオメディカル研究部門 加藤薫先生

超解像ライブセルイメージングに最適の特長である高速リアルタイムイメージングを、超解像でも行うことが可能です。さらに、退色・光毒性を抑えたライブセル
イメージングが可能です。
アプリケーション例：
ミトコンドリアのリアルタイムライブセルイメージング
画像ご提供：
産業技術総合研究所 バイオメディカル研究部門 加藤薫先生

超解像の原理：有効

結像

通常の共焦点顕微鏡の結像関係は、照明系の（点像分布関数）と検出系のとの積で表されます。ピンホールの光軸中心からの位置の結像を考察しますと、図のように照明系のと検出系のの積となり、光軸中心からの位置情報を中心として伝達されていることが分かります。これはすなわちの位置の情報がピ
ンホール上では に拡大されていることと同等になります。これを補正するために、マイクロレンズを用いてピンホールに投影される
個々の焦点を１ ２に光学的に縮小することにより、理想的な結像関係となります。
この場合の分解能は、ピンホールを無限小に小さくした場合の理想的な共焦点顕微鏡とほぼ等しくなり、通常の共焦点顕微鏡の約倍の向上が見込めます。
しかも明るく、高速で、細胞にやさしいの特徴はそのまま維持されます。

●お問い合わせ先

点光源
ピンホール
面

対物
レンズ

試料面

結像

点光源
マイクロレンズ

横河電機株式会社 ライフイノベーション事業本部 バイオソリューションセンター：：〒

石川県金沢市北陽台

粒子や結晶の構造解析・測定に最適！
画像解析ソフトウェアMIPAR
MIPAR（マイパー）はマウスで簡単に操作できるプログラムいらずの画像解析ソフトウェアです。
比類なき検出能力と測定機能を有しており、粒子解析（粒径分布、粒子数、粒子面積）
をはじめ
金属材料、鉱物、医薬、生命科学などの様々な分野にご利用頂けます。

レシピを設定して顕微鏡画像から抽出した各オブジェクトを測定

シャーレ画像から直接オブジェクトを抽出/測定

同じレシピ条件で、細胞の回復を時系列に検出した例＜MIPARの主な機能＞①メニュー操作だけで、セグメント分割、パターン認識、
エッジ抽出、
セルのカウントなど、様々な検出が行えます。
②レシピ（画像検出設定、測定設定）
を自由に作成・保存・編集でき、複数の画像処理に利用できます。

③バッチ機能にて、同じレシピで多数の画像を一括処理できます。

④検出した細胞や粒子の各種測定（面積など）を行い、CSV/TXTファイルで出力します。
WindowsOS（64bit）及びMacに対応

操作方法や見積りのお問い合わせはこちらまで！ ⇒3DオプションでFIB-SEM積層画像を構築

永年/年間ライセンスから選択可
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