Curriculum Vitae

Name:

Takaomi C. Saido

Present occupation
Position:Laboratory Head
Institution:
Laboratory for Proteolytic Neuroscience
RIKEN Center for Brain Science
2-1 Hirosawa, Wako-shi, Saitama 351-0198
Email:
takaomi.saido@riken.jp
Phone:+81-48-467-9715
Fax:+81-48-467-9716
Education
1978-1982
B.A.
1982-1985 & 1986-1988
Ph. D
1985-1986
Visiting Scholar

University of Tsukuba
University of Tokyo Graduate School
Cornell University

Academic appointments
1988-1997
Research Scientist, Tokyo Metropolitan Institute of Medical Science
1992
Visiting Scientist, Scripps Institute1997-2018
Laboratory Head, RIKEN Brain Science Institute1997-2012
Visiting Professor, Yokohama City Medical School
1997-2006
Visiting Professor, Tohoku University School of Medicine
1999-2009
Visiting Professor, University of Tsukuba School of Medicine
2004
Visiting Professor, University of Nagoya School of Medicine
2005
Visiting Professor, Institute for Frontier Medical Sciences, University of
Kyoto
2006
Visiting Professor, Graduate School of Agricultural and Life Sciences,
University of Tokyo
2008-present Visiting Professor, Waseda University
2009-2010
Visiting Professor, Japan Women’s College
2017-present Visiting Professor, Keio University
2018-present Laboratory Head, RIKEN Center for Brain ScienceAwards and honors

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1985
1995
2002
2003
2003
2004
2007
2015

Rotary International Fellowship
Young Investigator Award, Japanese Biochemical Society
Journal of Biochemistry Excellent Paper Prize
BSI Flagship Prize
Neuroscience Research Excellent Paper Prize
Outstanding contributor award, Alzheimer Research ForumToshihiko Tokizane Memorial Award
Ando Momofuku Memorial Award

Memberships and committee assignments in professional societies
1982Japanese Biochemical Society
1984-1986
Japanese Biophysical Society
1993Japanese Pharmaceutical Society
1994Society for Neuroscience, USA
1996Councilor, Japanese Society for Dementia (councilor)
1996Japanese Society for Proteases and Inhibitors
1997Japanese Society for Neuroscience
1998Japanese Society for Neurochemistry
Major research interests
Metabolism of amyloid β peptide in brain
Pathophysiological roles of calpain in the brain
Animal models of Alzheimer's disease
Presymptomatic markers for brain aging and Alzheimer’s disease

Publications in international journals (in English only)
1. Toyoshima, S. Saido, T.C., Makishima, F., Osawa, T. (1983). Induction of increased
calcium uptake in liposomes having membrane proteins of chicken erythrocytes by
S-adenosylmethionine. Biochem. Biophys. Res. Commun. 114, 1126-1131.
2. Seki, H., Saido, T.C., Iseki, K., Whitney, F., Wong, S. (1984). Uptake kinetics of
micro-organisms in the sulfuretum of Saanich Inlet, British Columbia, Canada. Arch.
Hydrobiol., 100, 73-82.
3. Saido, T.C., Toyoshima, S., Osawa, T. (1987). Protein-O-carboxylmethyltransferase
from cytosol and membranes of chicken erythrocytes. J. Biochem. 102, 319-326.
4. Magae, J., Osada, H., Fujiki, H., Saido, T.C., Suzuki, K., Nagai, K., Yamasaki, M.,
Isono, K. (1990). Morphological changes of human myeloid leukemia K562 cells by
a protein phosphatase inhibitor, tautomycin. Proc. Japan Acad. 66, 209-212.
5. Osada, S., Mizuno, K., Saido, T.C., Akita, Y., Suzuki, K., Kuroki, T., Ohno, S.
(1990). A phorbol ester receptor/protein kinase, nPKCη, a new member of the

3protein kinase C family predominantly expressed in lung and skin. J. Biol. Chem.
265, 22434-22440.
6. Sorimachi, H., Ohmi, S., Emori, Y., Kawasaki, H., Saido, T.C., Ohno, S., Minami,Y., Suzuki, K. (1990). A novel member of the calcium-dependent cysteine proteasefamily. Biol. Chem. Hoppe-Seyler 371, 171-176.
7. Kobayashi, Y., Yamamoto, K., Saido, T.C., Kawasaki, H., Oppenheim, J.T.,
Matsushima, K. (1990). Identification of calcium-activated neutral protease as aprocessing enzyme of human interleukin 1 α. Proc. Natl. Acad. Sci. USA 87, 55485552.
8. Ohno, S., Akita, Y., Hata, A., Osada, S., Kubo, K., Konno, Y., Akimoto, K., Mizuno,
K., Saido, T.C., Kuroki, T., Suzuki, K. (1991). Structural and functional diversities
of a family of signal transducing protein kinases, protein kinase C; two distinct
classes of PKC, conventional cPKC and novel nPKC. Advances in Enzyme
Regulation 31, 287-303.
9. Mori, A., Aizawa, H., Saido, T.C., Kawasaki, H., Mizuno, K., Murofushi, H., Suzuki,
K., Sakai, H. (1991). Site-specific phosphorylation by protein kinase C inhibits
assembly-promoting activity of microtubule-associated protein. Biochemistry 30,
9341-9346.
10. Mizuno, K., Kubo, K., Saido, T.C., Akita, Y., Osada, S., Kuroki, T., Ohno, S.,
Suzuki, K. (1991). Structure and properties of a ubiquitously expressed protein
kinase C, nPKCδ. Eur. J. Biochem. 202, 931-940.
11. Saido, T.C., Mizuno, K., Suzuki, K. (1991). Proteolysis of protein kinase C by
calpain: effect of acidic phospholipids. Biomed. Biochim. Acta 50, 485-489.
12. Osada, S., Mizuno, K., Saido, T.C., Suzuki, K., Kuroki, T., Ohno, S. (1992). A new
member of protein kinase C family, nPKCθ, predominantly expressed in skeletal
muscle. Mol. Cell. Biol. 12, 3930-3938.
13. Suzuki, K., Saido, T.C., Hirai, S. (1992). Modulation of cellular signals by calpain.
Ann. N. Y. Acad. Sci. 674, 218-227.
14. Saido, T.C., Mizuno, K., Konno, Y., Osada, S., Ohno, S., Suzuki, K. (1992).
Purification and characterization of protein kinase C ε from rabbit brain.
Biochemistry 31, 482-490.
15. Saido, T.C., Nagao, S., Shiramine, M., Tsukaguchi, M., Sorimachi, H., Murofushi,
H., Tsuchiya, T., Ito, H., Suzuki, K. (1992). Autolytic transition of µ-calpain as
resolved by antibodies distinguishing between the pre- and post-autolysis forms. J.
Biochem. 111, 81-86.
16. Saido, T.C., Shibata, M., Takenawa, T., Murofushi, H., Suzuki, K. (1992). Positive
regulation of µ-calpain action by polyphosphoinositides. J. Biol. Chem. 267, 2458524590.
17. Mizuno, K., Saido, T.C., Ohno, S., Tamaoki, T., Suzuki, K. (1993). Staurosporinerelated compounds, K252a and UCN-01, inhibit both cPKC and nPKC. FEBS Lett.
330, 114-116.
18. Sorimachi, H., Toyama-Sorimachi, N., Saido, T.C., Kawasaki, H., Sugita, H.,
Miyasaka, M., Arahata, K., Suzuki, K. (1993). Muscle-specific calpain, p94, isdegraded by autolysis immediately after translation, resulting in disappearance frommuscle. J. Biol. Chem. 268, 10593-10605.
19. Yamaura, I., Tani, E., Saido, T.C., Suzuki, K., Minami, N., Maeda, Y. (1993).
Calpain-calpastatin system of canine basilar artery in vasospasm. J. Neurosurg. 79,
537-543.
20. Saido, T.C., Suzuki, H., Yamazaki, H., Tanoue, K., Suzuki, K. (1993). In situ
capture of µ-calpain activation in platelets. J. Biol. Chem. 268, 7422-7426.

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21. Saido, T.C., Yokota, M., Nagao, S., Yamaura, I., Tani, E., Tsuchiya, T., Suzuki, K.,
Kawashima, S. (1993). Spatial resolution of fodrin proteolysis in postischemic brain.
J. Biol. Chem. 268, 25239-25243.
22. Satake, A., Itoh, K., Shimmoto, M., Saido, T.C., Sakuraba, H., Suzuki, Y. (1994).
Distribution of lysosomal protective protein in human tissues. Biochem. Biophys.
Res. Commun., 205, 38-43
23. 23 Akita, Y., Ohno, S., Yajima, Y., Konno, Y., Saido, T.C., Mizuno, K., Chida, K.,
Osada, S., Kuroki, T., Kawashima, S., Suzuki, K. (1994). Overexpression of Ca2+independent protein kinase C isozyme, nPKCε increases the secretion of prolactin
from thyrotropin-releasing hormone-stimulated rat pituitary GH4C1 cells. J. Biol.
Chem. 269, 4653-4660.
24. Yokota, M., Saido, T.C., Miyaji, K., Tani, E., Kawashima, S., Suzuki, K. (1994).
Stimulation of protein-tyrosine phosphorylation in gerbil hippocampus after global
forebrain ischemia. Neurosci. Lett. 168, 69-72.
25. Nagao, S., Saido, T.C.( corresponding author), Akita, Y., Tsuchiya, T., Suzuki, K.,
Kawashima, S. (1994). Calpain-calpastatin interactions in epidermoid carcinoma
KB cells. J. Biochem. 115, 1178-1184.
26. Sorimachi, H., Saido, T.C., Suzuki, K. (1994). New era of calpain research,
discovery of tissue-specific calpains. FEBS Lett., 343, 1-5.
27. Saito, Y., Saido, T.C., Sano, K., Kawashima, S. (1994). The calpain-calpastatin
system is regulated differentially during human neuroblastoma cell differentiation to
Schwannian and neuronal cells. FEBS Lett., 353, 327-331.
28. Saido, T.C., Nagao, S., Shiramine, M., Tsukaguchi, M., Yoshizawa, T., Sorimachi,
H., Ito, H., Tsuchiya, T., Kawashima, S., Suzuki, K. (1994). Distinct kinetics ofsubunit autolysis in mammalian m-calpain activation. FEBS Lett. 346, 263-267.
29. Saido, T.C., Sorimachi, H., Suzuki, K. (1994). Calpain: new perspectives inmolecular diversity and physiological-pathological involvement. FASEB J., 8, 814822.
30. Saido, T.C., Yokota, M., Maruyama, K., Yamao-Harigaya, W., Tani, E., Ihara, Y.,
Kawashima, S. (1994). Spatial resolution of the primary β-amyloidogenic process
induced in postischemic brain. J. Biol. Chem. 269, 15253-15257.
31. Hong, D.-h., Huan, J., Ou, B.-r., Yeh, J.-y., Saido, T.C., Cheeke, P.R., Forsberg,
N.E. (1995). Protein kinase C isoforms in muscle cells and their regulation byphorbol ester and calpain. Biochim. Biophys. Acta, 1267, 45-54.
32. Yoshida, K., Inui, M., Harada, K., Saido, T.C., Sorimachi, Y., Ishihara, T.,
Kawashima, S., Sobue, K. (1995). Reperfusion of rat heart after brief ischemia
induces proteolysis of calspectin (non-erythroid spectrin or fodrin) by calpain. Circ.
Res., 77, 603-610.
33. Mizuno, K., Noda, K., Ueda, Y., Hanaki, H., Saido, T.C., Ikuta, T., Kuroki, T.,
Tamaoki, T., Hirai, S., Osada, S., Ohno, S. (1995). UCN-01, an anti-tumor drug, isa selective inhibitor of the conventional PKC subfamily. FEBS Lett. 359, 259-261.
34. Blomgren, K., Kawashima, S., Saido, T.C., Karlsson, J.-O., Hagberg, H. (1995).
Subcellular distribution of calpains and fodrin degradation after neonatal hypoxic
ischemia. Brain Res., 684, 143-149.
35. Blomgren, K., McRae, A., Bona, E., Gilland, E., Saido, T.C., Karlsson, J.-O.,
Hagberg, H. (1995). Degradation of fodrin and MAP2 after neonatal cerebral
hypoxic-ischemia. Brain Res., 684, 136-142.
36. Bednarski, E., Vanderklish, P., Gall, C., Saido, T.C., Bahr, B.A., Lynch, G. (1995).
Translational suppression of calpain I reduces NMDA-induced spectrin proteolysis
and pathophysiology in cultured hippocampal slices. Brain Res., 694, 147-157.

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37. Vanderklish P., Saido, T.C., Gall, C., Arai, A., Lynch, G. (1995). Proteolysis ofspectrin by calpain accompanies theta-burst stimulation in cultured hippocampal
slices. Mol. Brain Res., 32, 25-35.
38. Harigaya, Y., Shoji, M., Kawarabayashi, T., Kanai, M., Nakamura, T., Iizuka, T.,
Igeta, Y., Saido, T.C., Sahara, N., Mori, H., Hirai, S. (1995). Modified amyloid βprotein ending at 42 or 40 with different solubility accumulates in the brain of
Alzheimer’s disease. Biochem. Biophys. Res. Commun., 211, 1015-1022.
39. Yokota, M., Saido, T.C., Tani, E., Kawashima, S., Suzuki, K. (1995). Three distinct
phases of fodrin proteolysis induced in postischemic hippocampus: involvement of
calpain and unidentified protease. Stroke, 26, 1901-1907.
40. Igarashi, K., Kaneda, M., Yamaji, A., Saido, T.C., Kikkawa, U., Ono, Y., Inoue, K.,
Umeda, M. (1995). A novel phosphatidylserine-binding peptide motif defined by ananti-idiotypic monoclonal antibody: localization of phosphatidylserine-specificbinding sites on protein kinase C and phosphatidylserine decarboxylase. J. Biol.
Chem., 270, 29075-29078.
41. Martin, S.J., O'Brien, G.A., Nishioka, W.K., Mahboubi, A., Saido, T.C., Green, D.R.
(1995). Proteolysis of fodrin (nonerythroid spectrin) during apoptosis. J. Biol.
Chem., 270, 6425-6428.
42. Saito, Y., Maruyama, K., Saido, T.C., Kawashima, S. (1995). N23K, a genetransiently up-regulated during neuronal differentiation, encodes a precursor protein
for a newly identified neuropeptide Nociceptin. Biochem. Biophys. Res. Commun.,
217, 539-545.
43. Eto, A., Akita, Y., Saido, T.C. (corresponding author), Suzuki, K., Kawashima, S.
(1995). The role of calpain-calpastatin system in thyrotropin releasing hormoneinduced selective down-regulation of a protein kinase C isozyme, nPKCε, in rat
pituitary GH4C1 cells. J. Biol. Chem., 270, 25115-25120.
44. Du, X., Saido, T.C. (two first authors), Tsubuki, S., Indig, F.E., Williams, M..J.,
Ginsberg, M.H. (1995). Calpain cleavage of the cytoplasmic domain of the integrin
β3 subunit. J. Biol. Chem., 270, 24146-26152.
45. Saido, T.C., Iwatsubo, T., Mann, D.M.A., Shimada, H., Ihara, Y., Kawashima, S.
(1995). Dominant and differential deposition of distinct β-amyloid peptide species,
AβN3(pE), in senile plaques. Neuron, 14, 457-466.
46. Yamashima, T., Saido, T.C., Takita, M., Miyazawa, A., Yamano, J., Miyakawa, A.,
Nishijo, H., Ono, T., Yamashita, J., Yoshioka, T. (1996). Transient brain ischemia
provokes Ca2+ mobilization, PIP2 overexpression and calpain activation prior todelayed CA-1 neuronal death in monkeys. Eur. J. Neurosci., 8, 1932-1944.
47. Kume, H., Maruyama, K., Tomita, T., Iwatsubo, T., Saido, T.C., Obata, K. (1996).
Molecular cloning of a novel basic helix-loop-helix protein from the rat brain.
Biochem. Biophys. Res. Commun., 219, 526-530.
48. Inomata, M., Hayashi, M., Ohno-Iwashita, Y., Tsubuki, S., Saido, T.C., Kawashima,
S. (1996). Involvement of calpain in integrin-mediated signal transduction. Arch.
Biochem. Biophys., 328, 129-134.
49. Kanai, Y., Kanai-Azuma, M., Noce, T., Saido, T.C., Shiroishi, T., Hayashi, Y.,
Yazaki, K. (1996). Identification of two Sox17 mRNA isoforms, with and without
the HMG-box region, and their differential expression in mouse spermatogenesis. J.
Cell Biol., 133, 667-681.
50. Lemere, C.A., Blusztajn, J.K., Yamaguchi, H., Wisniewski, T., Saido, T.C., Selkoe,
D.J. (1996). Sequence of deposition of heterogeneous amyloid β-peptides and apo E
in Down syndrome: implications for initial events in amyloid plaque formation.
Neurobiol. Disease, 3, 16-32.

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51. Yokota, M., Saido, T.C., Tani, E., Yamaura, I., Minami, N. (1996). Cytotoxic
fragment of amyloid precursor protein accumulates in hippocampus after global
forebrain ischemia. J. Cereb. Blood Flow Metabol., 16, 1219-1223.
52. Saito, Y., Maruyama, K., Kawano, J., Yamagishi, K., Saido, T.C., Kawashima, S.
(1996). Molecular cloning and characterization of a novel form of neuropeptide
precursor gene as a developmentally regulated molecule. J. Biol. Chem., 271,
15615-15622.
53. Saido, T.C., Yamao-Harigaya, W., Iwatsubo, T., Kawashima, S. (1996). Aminoand carboxyl-terminal heterogeneity of β-amyloid peptides deposited in humanbrain. Neurosci. Lett., 215, 173-176.
54. Iwatsubo, T., Saido, T.C., Mann, D.M.A., Lee, V.M.-Y., Trojanowski, J.Q. (1996).
Full-length Aβ(1-42(43)) as well as amino-terminally modified and truncatedAβ42(43) deposit in diffuse plaques. Am. J. Pathol., 149, 1823-1830.
55. Lemere, C.A., Lopera, F., Kosik, K.S., Lendon, C.L., Ossa, J., Saido, T.C.,
Yamaguchi, H., Ruiz, A., Martinez, A., Madrigal, L., Hincapie, L., Arango L., J.C.,
Anthony, D.C., Koo, E.H., Goate, A.M., Selkoe, D..J., Arango V., J.C. (1996). The
E280A Presenilin 1 mutation leads to a distinct Alzheimer’s disease phenotype:
Increased Aβ42 deposition and severe cerebellar pathology. Nature Medicine, 2,1146-1150.
56. Maruyama, K., Tomita, T., Shinozaki, K., Kume, H., Asada, H., Saido, T.C., Ishiura,
S, Iwatsubo, T., Obata, K. (1996). Familial Alzheimer’s disease-linked mutations at
Val717 of amyloid precursor protein are specific for the increased secretion ofAβ42(43). Biochem. Biophys. Res. Commun., 227, 730-735.
57. Blomgren, K., McRae, A., Elmered, A., Kawashima, S., Saido, T.C., Ono, T.,
Hagberg, H. (1997). The calpain proteolytic system in neonatal hypoxic-ischemia.
Ann. New York Acad. Sci., 825, 104-119.
58. Kuda, T., Shoji, M., Arai, H., Kawashima, S., Saido, T.C. (1997). Reduction ofplasma glutamyl aminopeptidase activity in sporadic Alzheimer’s disease. Biochem.
Biophys. Res. Commun., 231, 526-530.
59. Tomita, T., Maruyama, K., Saido, T.C., Kume, H., Shinozaki, K., Tokuhiro, S.,
Capell, A., Walter, J., Gruenberg, J., Haass, C., Iwatsubo, T., Obata, K. (1997). The
presenilin 2 mutation (N141I) linked to familial Alzheimer’s disease (Volga Germanfamilies) increases the secretion of amyloid β protein ending at Aβ42(43). Proc. Nat.
Acad. Sci. USA, 94, 2025-2030.
60. Mann, D.M.A., Iwatsubo, T., Pickering-Brown, S.M., Owen, F., Saido, T.C., Perry,
R.H. (1997). Preferential Deposition of amyloid β protein (Aβ) in the form of Aβ40
in Alzheimer's disease is associated with a gene dosage effect of the apolipoprotein
E E4 allele. Neurosci. Lett., 221, 81-84.
61. Mann, D.M.A., Pickering-Brown, Byatt, N.N., Wright, A.E., Owen, F., Iwatsubo,T., Saido, T.C. (1997). An intronic polymorphism in the presenilin-1 gene does not
influence the amount or molecular form of the amyloid β protein deposited in
Alzheimer’s disease. Neurosci. Lett., 222, 57-60.
62. Saito, Y., Maruyama, K., Saido, T.C., Kawashima, S. (1997). Overexpression of aneuropeptide nociceptin/orphanin FQ precursor gene, N23K/N27K, induces neurite
outgrowth in mouse NS20Y cells. J. Neurosci. Res, 48, 397-406.
63. Saido, T.C. (1998). Alzheimer's disease as proteolytic disorders: Anabolism andcatabolism of β-amyloid. Neurobiol. Aging, 19, S69-S75.
64. Saido, T.C., Kawashima, S., Tani, E., Yokota, M. (1997). Up- and down-regulationof calpain inhibitor polypeptide, calpastatin, in postischemic hippocampus.
Neurosci. Lett., 227, 75-78.

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65. Russo, C., Saido, T.C., DeBusk, L.M., Tabaton, M., Gambetti, P., Teller, J.K.
(1997). Heterogeneity of water-soluble amyloid β-peptide in Alzheimer's disease
and Down's syndrome brains. FEBS Lett. 409, 411-416.
66. Yamazaki, T., Haass, C., Saido, T.C., Omura, S., Ihara, Y. (1997). Specific increasein amyloid β-protein42 secretion ratio by calpain inhibition. Biochemistry 36,
8377-8383.
67. Kouchi, Z., Saido, T.C., Ohyama, H., Maruta, H., Suzuki, K., Tanuma, S. (1997).
The restrictive proteolysis of α-fodrin to a 120 kDa fragment is not catalyzed bycalpains during thymic apoptosis. Apoptosis 2, 84-89.
68. Yamazaki, M., Suga, Y., Ishidoh, K., Saido, T.C., Kawashima, S., Suzuki, K.,
Kominami, E., Ogawa, H. (1997). Cytoplasmic processing of human profilaggrin by
active µ-calpain. Biochem. Biophys. Res. Commun., 235, 652-656.
69. Didier, M., Xu, M., Berman, S.A., Saido, T.C., Bursztajn, S. (1997). Involvementof three glutamate receptor ε subunits in the formation of N-methyl-D-aspartate
receptors mediating excitotoxicity in primary cultures of mouse cerebellar granulecells. Neuroscience, 78, 1129-1146.
70. Yan, S.D., Fu, J., Soto, C., Chen, X., Zhu, H., Al-Mohanna, F., Collison, K., Zhu,
A., Stern, E., Saido, T., Tohyama, M., Ogawa, S., Roher, A., Stern, D. (1997).
ERAB: A novel intracellular amyloid-β peptide binding protein which mediates
neurotoxicity in Alzheimer's disease. Nature 389, 689-695.
71. Schoenwaelder, S.M., Kulkarni, S., Salem, H.H., Imajoh-Ohmi, S., YamaoHarigaya, W., Saido, T.C., Jackson, S.P. (1997). Distinct substrate specificities andfunctional roles for the 78 and 76 kDa forms of µ-calpain in human platelets. J. Biol.
Chem., 272, 24876-24884.
72. Shin, R.-W., Ogino, K., Kondo, A., Saido, T.C., Trojanowski, J.Q., Kitamoto, T.,
Tateishi, J. (1997). Amyloid β-protein (Aβ) 1-40 but not Aβ1-42 contributes
experimental formation of Alzheimer disease amyloid fibrils in rat brain. J.
Neurosci. , 17, 8187-8193.
73. Tekirian, T.L., Saido, T.C., Markesbery, W.R., Russell, M..J., Wekstein, D.R., Patel,E., Geddes, J.W. (1998). Amino terminus heterogeneity of Parenchymal andCerebrovascular β-amyloid deposits in aged human, canine, and polar bear brains.
J. Neuropathol. Exp. Neurol., 57, 76-94.
74. Sorimachi, Y., Harada, K., Saido, T.C., Ono, T., Kawashima, S., Yoshida, K. (1997).
Downregulation of calpastatin in rat heart after brief ischemia and reperfusion. J.
Biochem. 122, 743-748.
75. Inomata, M., Nomura, K., Takehana, M., Saido, T.C., Kawashima, S., Shumiya, S.
(1997). Evidence for involvement of calpain in the cataractgenesis in Shumiya
Cataract Rat. Biochim. Biophys. Acta, 1362, 11-23.
76. Schmidt, M.L., Lee, V.M.-Y., Saido, T.C., Perl, D., Schuck, T., Iwatsubo, T.,
Trojanowski, J.Q. (1998). Amyloid plaques in Guam ALS and Parkinsonismdementia complex contain species of Aβ similar to those found in the amyloid
plaques of Alzheimer’s disease. Acta Neurophatol., 1362, 11-23.
77. Oyama, F., Sawamura, N., Kobayashi, K., Morishima-Kawashima, M., Kuramochi,T., Ito, M., Tomita, T., Maruyama, K., Saido, T.C., Iwatsubo, T., Capell, A., Walter,J., Grunberg, J., Ueyama, Y., Haass, C., Ihara, Y. (1998). Mutant presenilin 2transgenic mouse: Effect on an age-dependent increase of amyloid β-protein (Aβ)42in brain. J. Neurochem., 71, 313-322.

878. Frautschy, S.A., Yang, F., Irrizarry, M., Hyman, B., Saido, T.C., Hsiao, K., Cole,
G.M. (1998). Microglial response to amyloid plaques in APPsw transgenic mice.
Am. J. Pathol., 152, 307-317.
79. Tokuhiro, S., Tomita, T., Iwata, H., Kosaka, T., Saido, T.C., Maruyama, K.,
Iwatsubo, T. (1998). The presenilin 1 mutation (M146V) linked to familial
Alzheimer's disease attenuates the neuronal differentiation of NTera 2 cells.
Biochem. Biophys. Res. Commun, 244, 751-755.
80. Shinozaki, K., Maruyama, K., Kume, H., Tomita, T., Saido, T.C., Iwatsubo, T.,
Obata, K. (1998). The presenilin 2 loop domain interacts with the µ-calpain Cterminal region. Int. J. Mol. Med., 1, 797-799.
81. Sudoh, S., Kawamura, Y., Sato, S., Wang, R., Saido, T.C., Oyama, F., Sakaki, Y.,
Komano, H., Yanagisawa, K. The presenilin 1 mutations linked to familial
Alzheimer's disease elevate a production of N-terminally truncated Aβ42 variant,Aβ11-42, which is generated through distinct processing pathway from Aβ1-42.
(1998). J. Neurochem, 1535-1543.
82. Funato, H., Yoshimura, M., Yamazaki, T., Saido, T.C., Ito, Y., Yokofujita, J.,
Odaka, R., Ihara, Y. (1998). Astrocytes containing amyloid β-protein (Aβ-positive
granules are associated with Aβ40-positive diffuse plaques in the aged human brain.
Am. J. Pathol., 152, 983-992.
83. Kimura, Y., Koga, H., Araki, N., Mugita, N., Fujita, N., Takeshima, H., Nishi, T.,
Yamashima, T., Saido, T.C., Yamasaki, T., Moritake, K., Saya, H., Nakao, M.
(1998). The involvement of calpain-dependent proteolysis of the tumor suppressor
NF2 (merlin) in schwannomas and meningiomas. Nature Med., 8, 915-922.
84. Ono, Y., Shimada, H., Sorimachi, H., Richard, I., Saido, T.C., Beckmann, J.S.,
Ishiura, S., Suzuki, K. (1998). Functional defects of a muscle-specific calpain, p94,
caused by mutations associated with Limb-Girdle muscular dystrophy type 2A. J.
Biol. Chem., 273, 17073-17078.
85. Yamaguchi, H., Sugihara, S., Ogawa, A., Saido, T.C., Ihara, Y. (1998). Diffuse
plaques associated with astroglial amyloid β protein, possibly showing adisappearing stage of senile plaques. Acta Neuropathol., 95, 217-222.
86. Meredith, J.Jr., Mu, Z., Saido, T.C., Du, X. (1998). Cleavage of the cytoplasmic
domain of the integrin β3 subunit during endothelial cell apoptosis. J. Biol. Chem.,
273, 19525-19531.
87. Akiyama, H., Mori, H., Saido, T.C., Kondo, H., Ikeda, K., McGeer, P.L. (1998).
Occurrence of the diffuse deposits with numerous amyloid β-protein(Aβ)-containing
glial cells in the cerebral cortex of patients with Alzheimer's disease. Glia, 4, 324331.
88. Tomita, T., Tokuhiro, S., Hashimoto, T., Aiba, K., Saido, T.C., Maruyama, K.,
Iwatsubo, T. (1998). Molecular dissection of domains in mutant presenilin 2 thatmediate overproduction of amyloidogenic forms of amyloid β peptides. J. Biol.
Chem., 273, 21153-21160.
89. Frautschy, S.A., Horn, D.L., Sigel, J.J., Harris-White. M.E., Mendoza, J.J., Yang,F., Saido, T.C., Cole, G.M. (1998). Protease inhibitor coinfusion with amyloid βprotein results in enhanced deposition and toxicity in rat brain. J. Neurosci., 18,8311-8321.
90. Hiwasa, T., Nakamura, Y., Ozaki, T., Kondo, K., Saido, T., Nakagawara, A. andSakiyama, S. (1998). Down-regulation of protein kinase α and γ and enhanced TPAinduced neurite formation in DAN-transfected neuroblastoma cells. FEBS Lett., 440,
25-28.

9
91. Ishidoh, K., Saido, T.C., Kawashima, S., Hirose, M., Watanabe, S., Sato, N.,
Kominami, E. (1998). Multiple processing of procathepsin L to cathepsin L in vivo.
Biochem. Biophys. Res. Commun., 252, 202-207.
92. Kitagawa, K., Matsumoto, M., Saido, T.C., Ohtuki, T., Kuwabara, K., Yagita, Y.,
Mabuchi, T., Yanagihara, T., Hori, M. (1999). Species differences in fodrin
proteolysis in the ischemic brain. J. Neurosci. Res., 643-649.
93. Honda, T., Yasutake, K., Nihonmatsu, N., Merchen, M., Takahashi, H., Murayama,O., Murayama, M., Sato, K., Omori, A., Tsubuki, S., Saido, T.C., Takashima, A.
(1999). Dual roles of proteasome in the metabolism of presenilin 1. J. Neurochem.,
72, 255-261.
94. Hosoda, R., Saido, T.C., Otvos, L.Jr., Arai, T., Mann, D.M.A., Lee, V.M.-Y.,
Trojanowski, J.Q., Iwatsubo, T. (1998). Quantitation of modified amyloid β peptides
in Alzheimer disease and down syndrome brains J. Neuropathol. Exp. Neurol., 57,
1089-1095.
95. Yokota, M., Tani, E., Tsubuki, S., Yamaura, I., Nakagaki, I., Hori, S., Saido, T.C.
(1999). Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage.
Brain research, 819, 8-14.
96. Kubo, H., Matsushita, M., Kotani, M., Kawasaki, H., Saido, T.C., Kawashima, S.,
Katagiri, C., Suzuki, A. (1999). Molecular basis for oviductin-mediated processing
from gp43 to gp41, the predominant glycoproteins of Xenopus egg envelopes. Dev.
Genet., 25, 123-129.
97. Eto, A., Saido, T.C., Fukushima, K., Tomioka, S., Imai, S., Nishizawa, T., Hanada,
N. (1999). Inhibitory effect of a self-derived peptide on glycosyltransferase of
Streptococcus mutans. Possible novel anticaries measures. J. Biol. Chem., 274,
15797-15802.
98. Saido, T.C. (2000). Involvement of polyglutamine endolysis followed bypyroglutamate formation in the pathogenesis of triplet repeat/polyglutamineexpansion diseases. Med. Hypotheses, 54, 427-429.
99. Ray, S.K., Shields, D.C., Saido, T.C., Matzelle, D.C., Wilford, G.G., Hogan, E.L.,
Banik, N.L. (1999). Calpain activity and translational expression increased in spinal
cord injury. Brain Res., 816, 375-380.
100. Nakagawa, Y., Nakamura, M., McIntosh, T.K., Rodriguez, A., Berlin J.A., Smith,D.H., Saatman, K.E., Raghupathi, R., Clemens, J., Saido, T.C., Schmidt, M.L., Lee,
V.M.-Y., and Trojanowski, J.Q. (1999). Traumatic brain injury in young PDAPP
transgenic mice induces marked ipsilateral hippocampal atrophy and diminished Aβ
deposition during aging. J. Comp. Neurol., 411, 390-398.
101. Kulkarni, S., Saido, T.C., Suzuki, K., Fox, J.E.B. (1999). Calpain mediates
integrin-induced signals at a point upstream of rho family members. J. Biol. Chem.,
274, 21265-21275.
102. Blomgren, K., Hallin, U., Anderson, A.-L., Puka-Sundvall, M., Bahr, B.A.,
McRae, A., Saido, T.C., Kawashima, S., Hagberg, H. (1999). Calpastatin is upregulated in response to hypoxia and is a suicide substrate to calpain after neonatal
cerebral hypoxia-ischemia. J. Biol. Chem., 274, 14046-14052.
103. Koike, H., Seki, H., Kouchi, Z., Ito, M., Kinouchi, T., Sorimachi, H., Saido, T.C.,
Maruyama, K., Suzuki, K., Ishiura, S. (1999). Thimet oligopeptidase cleaves thefull-length Alzheimer amyloid precursor protein at beta-secretase cleavage site in
COS cells. J. Biochem., 126, 235-242.
104. Koriyama, H., Kouchi, Z., Umeda, T., Saido, T.C., Ishiura, S., Suzuki, K. (1999).
Proteolytic activation of protein kinase δ and ε by caspase-3 in U937 cells duringchemotherapeutic agent-induced apoptosis. Cell. Signal., 11, 831-838.

10105. Koike, H., Tomioka, S., Sorimachi, H., Saido, T.C., Maruyama, K., Okuyama, A.,
Fujisawa-Sehara, A., Ohno, S., Suzuki, K., Ishiura, S. (1999). MDC9 has an αsecretase activity responsible for processing the amyloid precursor protein.
Biochem. J., 343, 371-375.
106. Fukumoto, H., Tomita, T., Matsunaga, H., Ishibashi, Y., Saido, T.C., Iwatsubo, T.
(1999). Primary cultures of neuronal and non-neuronal rat brain cells secrete similar
proportions of amyloid β peptides ending at Aβ40 and Aβ42. NeuroReport, 10,2965-2969.
107. Shields, D.C., Schaecher, K.E., Saido, T.C., Banik, N. (1999). A putative
mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain.
Proc. Natl. Acad. Sci. U.S.A., 96, 11486-11491.
108. Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E.,
Kawashima-Morishima, M., Lee, H.-.J., Hama, E., Sekine-Aizawa, Y., Saido, T.C.
(2000). Identification of the major Aβ1-42-degrading catabolic pathway in brain
parenchyma: Suppression leads to biochemical and pathological deposition. Nat.
Med., 6, 143-151.
109. Shimokata, H., Yamada, Y., Nakagawa, M., Okubo, R., Saido, T.C., Funakoshi,A., Miyasaka, K., Ohota, S., Tsujimoto, G., Tanaka, M., Ando, F., Niino, N. (2000).
Distribution of geriatric disease-related genotypes in the National Institute forLongevity Sciences, Longitudinal Study of Aging (NILS-LSA). J. Epiderm., S4655.
110. Russo, C., Schettini, G., Saido, T.C., Hulette, C., Lippa, C., Lannfelt, L., Ghetti,
B., Gambetti, P., Tabaton, M., Teller, J.K. (2000). Preferential deposition oftruncated amyloid- β peptides in brain of presenilin 1 gene mutation carriers.
Nature, 405, 531-532.
111. Nakagawa, Y. , Reed, L., Nakamura, M., McIntosh, T.K., Smith, D.H., Saatman,
K.E., Raghupathi, R., Clemens, J., Saido, T.C., Lee,V.M.-Y., Trojanowski, J.Q.
(2000). Brain trauma in aged transgenic mice induces regression of established Aβ
deposit. Exper. Neurol., 163, 244-252.
112. Lankiewicz, S., Luetjens, C.M., Bui, N.T., Krohn, A. J., Poppe, M., Cole, G.C.,
Nicholson, D.W., Saido, T.C., Prehn, H.M. (2000). Activation of calpain I converts
excitotoxic neuron death into a caspase-independent cell death. J. Biol. Chem.,
275, 17064-17071.
113. Takeuchi, A., Irizarry, M.C., Duff, K., Saido, T.C., Hsiao, Ashe K., Hasegawa, M.,
Mann D.M.A., Hyman, B.T., Iwatsubo, T. (2000). Age-related Aβ deposition intransgenic mice overexpressing both Alzheimer mutant presenilin 1 and βamyloid precursor protein is not associated with global neuronal loss. Am. J. Pathol.,157, 331-339.
114. Hiwasa, T., Arase, Y., Kikuno, K., Hasegawa, R., Sugaya, S., Kita, K., Saido, T.,
Yamamori, H., Maki, M., Suzuki, N. (2000). Increase in ultraviolet sensitivity byoverexpression of calpastatin in ultraviolet-resistant UVr-1 cells derived fromultraviolet-sensitive human RSa cells. Cell Death Differ., 7, 531-537.
115. Iwata, N., Tsubuki, S., Hama, E., Takaki, Y., Shirotani, K., Saido, T.C. (2000).
Clearance of amyloid β-peptide from brain: transport or metabolism? Nat. Med., 6,718-719.
116. Harigaya, Y., Saido, T.C., Eckman, C.B., Prada, C.-M., Shoji, M., Younkin, S.
(2000). Amyloid beta protein starting pyroglutamate at position 3 is a major
component of the amyloid deposits in the Alzheimer’s disease brain. Biochem.
Biophys. Res. Commun., 276, 422-427.

11117. Saido, T. C. (2000). Degradation of amyloid-β peptide: a key to Alzheimer
pathogeneis, prevention, and therapy. NeuroSci. News, 5(3) 52-62.
118. Lee, H.-J., Tomioka, M., Takaki, Y., Masumoto, H., Saido, T.C. (2000).
Molecular cloning and expression of aminopeptiase A isoforms from rat
hippocampus. Biochim. Biophys. Acta, 1493, 273-278.
119. Takaki, Y., Iwata, N., Tsubuki, S., Taniguchi, S., Toyoshima, S., Lu, B., Gerard,
N.P., Gerard, C., Lee, H.-J., Shirotani, K., Saido, T.C. (2000). Biochemical
Identification of the neutral endopeptidase family member responsible for the
catabolism of amyloid β peptide in brain. J. Biochem., 128, 897-902.
120. Kawarabayashi, T., Younkin, L.H., Saido, T.C., Shoji, M., K. Hsiao, A., Younkin,
S.G. (2001). Age-dependent changes in brain, cerebrospinal fluid, and plasma
amyloid β protein in the Tg2576 transgenic mouse model of Alzheimer’s disease. J.
Neurosci., 21, 372-381.
121. Koike, H., Kouchi, Z., Kinouchi, T., Maeda, T., Sorimachi, H., Saido, T.C.,
Maruyama, K., Okuyama, A., Suzuki, K., Ishiura, S. (2000). Metabolism of amyloid
precursor protein in COS cells transfected with a beta-secretase candidate.
Cytotechnol., 33, 213-219.
122. Kitagaki, H., Tomioka, S., Yoshizawa, T., Sorimachi, H., Saido, T.C., Ishiura, S.,
Suzuki, K. (2000). Autolysis of calpain large subunit inducing irreversible
dissociation of stoichiometric heterodimer of calpain. Biosci. Biotechnol. Biochem.,
64, 689-695.
123. Shoji, M., Kawarabayashi, T., Sato, M., Sasaki, A., Saido, T.C., Matsubara, E.,
Yomidokoro, Y., Kanai, M., Shizuka, M., Ishiguro, K., Ikeda, M., Harigaya, Y.,
Okamoto, K., Hirai, S. (2000). Age-related amyloid beta protein accumulationinduces cellular death and macrophage activation in transgenic mice. J. Pathol., 191,
93-101.
124. Yamaguchi, A., Yamamoto, N., Akamatsu, N., Saido, T.C., Kaneda, M., Umeda,
M., Tanoue, K. (2000). PS-liposome and ox-LDL bind to different sites of theimmunodominant domain (#155-183) of CD 36: a new study with GS95, a new antiCD36 monoclonal antibody. Thromb. Res., 97, 317-326.
125. Maruyama, K., Usami, M., Kametani, F., Tomita, T., Iwatsubo, T., Saido, T.C.,
Mori, H., Ishiura, S. (2000). Molecular interactions between presenilin and calpain:
inhibition of m-calpain protease activity by presenilin-1, 2 and cleavage ofpresenilin-1 by m-, mu-calpain, Int. J. Mol. Med., 5, 269-273.
126. Taniguchi, S., Fujita, Y., Takahashi, H., Hayashi, S., Kakita, A., Murayama, S.,
Saido, T.C., Hisanaga, S., Iwatsubo, T., Hasegawa, M. (2001). Degradation of p35
to p25 in postmortem human and rat brains. FEBS Lett, 46-50.
127. Sekine-Aizawa, Y., Hama, E., Watanabe, K., Tsubuki, S., Kanai-Azuma, M.,
Kanai, Y., Arai, H., Aizawa, H., Iwata, N., Saido, T.C. (2001). Matrix
metalloproteinase (MMP) system in brain: Identification and characterization ofbrain-specific MMP highly expressed in cerebellum. Eur. J. Neurosci., 13, 935-948.
128. Bialkowska, K., Kulkarni, S., Du, X., Goll, D.E., Saido, T.C., Fox, J.E.B. (2000).
Evidence that beta3 integrin-induced Rac activation involves the calpain-dependent
formation of integrin clusters that are distinct from the focal complexes and focal
adhesions that form as Rac and RhoA become active. J. Cell Biol., 151, 685-695.
129. Shirotani, K., Tsubuki, S., Iwata, N., Takaki, Y., Harigaya, W., Maruyama, K.,
Kiryu-Seo, S., Kiyama, H., Iwata, H., Tomita, T., Iwatsubo, T., Saido, T.C. (2001).
Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly andefficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J. Biol.
Chem., 276, 21895-21901.

12
130. Choi, W.-S., Lee, E.-H., Chung, C.-W., Jung, Y.-K., Jin, B.K., Kim, S.U., Oh,
T.H., Saido, T.C., Oh, Y..J. (2001). Cleavage of Bax is mediated by caspasedependent or -independent calpain activation in dopaminergic neuronal cells:
Protective role of Bcl-2. J. Neurochem., 77, 1531-1541.
131. Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N.P., Gerard, C.,
Hama, E., Lee, H.-J., Saido, T.C. (2001). Metabolic regulation of brain Aβ byneprilysin. Science, 292, 1550-1552.
132. Kaneko, T., Yamashima, T., Tohma, Y., Nomura, M., Imajoh-Ohmi, S., Saido,
T.C., Nakao, M., Saya, H., Yamamoto, H., Yamashita, J. (2001). Calpain-dependent
proteolysis of merlin occurs by oxidative stress in meningiomas: a novel hypothesis
for tumorigenesis. Cancer, 92, 2662-2672.
133. Hama, E., Shirotani, K., Masumoto, H., Sekine-Aizawa., Y., Aizawa, H., Saido,
T.C. (2001). Clearance of extracellular and cell-associated amyloid β peptide byviral expression of neprilysin in primary culture. J. Biochem., 130, 721-726.
134. Russo, C., Schettini, G., Saido, T.C., Gambetti, P., Tabaton, M., Teller, J.T. (2001).
N-Terminally truncated amyloid β peptides and Alzheimer's disease. Neurobiol.
Aging, 22, 345.
135. Kitazume, S., Tachida, Y., Oka, R., Shirotani, K., Saido, T.C., Hashimoto, Y.
(2001). Alzheimer’s β-secretase, β-site amyloid precursor protein-cleaving enzyme,
is responsible for cleavage secretion of a golgi-resident sialyltransferease. Proc. Natl.
Acad. Science, USA, 98, 13554-13559.
136. Kim ,J.E., Han, B.S., Choi, W.S., Eom, D.S., Lee, E.H., Oh, T.H., Markelonis,
G.J., Saido, T.C., Lee, G.E., Chung, I.K., Oh, Y.J.(2001) Temporospatial sequenceof cellular events associated with etoposide-induced neuronal cell death : role ofantiapoptotic protein Bcl-XL. J. Neurosci. Res., 66, 1074-1082.
137. Fukami, S., Watanabe, K., Iwata, N., Haraoka, J., Lu, B., Gerard, N.P., Gerard, C.,
St. George-Hyslop, P., Saido, T.C. (2002). Aβ-degrading endopeptidase, neprilysin,in mouse brain: Synaptic and axonal localization inversely correlating with Aβ
pathology. Neurosci. Res., 43, 39-56.
138. Shirotani, K., Tsubuki, S., Lee, H.-J., Maruyama, K., Saido, T.C. (2002).
Generation of amyloid β peptide with pyroglutamate at position 3 in primary corticalneurons. Neurosci. Lett., 327, 25-28.
139. Fukami, S., Iwata, N., Saido, T.C. (2002). Therapeutic strategies of Alzheimer’s
disease through manipulation of Aβ metabolism: a focus on Aβ-degrading enzyme,
neprilysin. Drug Development Research, 56, 171-183.
140. Takahashi, M., Fukami, S., Iwata, N., Inoue, K., Itohara, S., Itoh, H., Haraoka, J.,
Saido, T.C. (2002). In vivo glioma growth requires host-derived matrix
metalloproteinase 2 for maintenance of angioarchitecture. Pharmacol. Res., 46, 155163.
141. Iwata, N., Takaki, Y., Fukami, S., Tsubuki, S., Saido, T.C. (2002). Region-specificreduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon
aging. J. Neurosci. Res., 70, 493-500.
142. Hattori, C., Asai, M., Oma, Y., Kino, Y., Sasagawa, N., Saido, T.C., Maruyama,
K., Ishiura, S. (2002). BACE1 interacts with nicastrin. Biochem. Biophys. Res.
Commun., 293, 1228-1232.
143. Tomioka, M., Shirotani, K., Iwata, N., Lee, H.J., Yang, F., Cole, G.M., Seyama,
Y. Saido, T.C. (2002). In vivo role of caspases in excitotoxic neuronal death:generation and analysis of transgenic mice expressing baculovirus caspase inhibitor,
p35, in postnatal. Brain Res. Mol. Brain Res., 108, 18-32.

13144. Mori, C., Spooner, E.T., Wisniewski, K.E., Wisniewski, T.M., Yamaguchi, H.,
Saido, T.C., Tolan, D.R., Selkoe, D.J., Lemere, C.A. (2002). Intracellular Aβ42
accumulation in Down syndrome brain. Amyloid, 9, 88-102.
145. Kuwano, K., Nisimura, I., Uetsuki, T., Saido, T.C., Yoshikawa, K. (2002).
Activation of calpain in cultured neurons overexpressing Alzheimer amyloid
precursor protein. Brain Res. Mol. Brains Res., 107, 166-175.
146. Dare, E., Tofighi, R., Vettori, M.V., Momoi, T., Poli, D., Saido, T.C., Mutti, A.,
Ceccatelli, S. (2002). Styrene 7,8-oxide induces caspase activation and regular DNA
fragmentation in neuronal cells, Brain Res., 933, 12-22
147. Kitazume, S., Tachida, Y., Oka, R., Kotani, N., Ogawa, K., Suzuki, M., Dohmae,N., Takio, K., Saido, T.C., Hashimoto, Y. (2003). Characterization of α2,6siaryltransferase cleavage by Alzheimer’s β-secretase (BACE1). J. Biol. Chem., 278,
14865-14871.
148. Saito, T., Takaki, Y., Iwata, N., Trojanowski, J., Saido T.C. (2003). Perspectives:
Alzheimer’s disease, neuropeptide, neuropeptidase, and Aβ metabolism. Science(SAGE-KE), http:// sageke.sciencemag.org/cgi/content/full/sageke;2003/3/pe1.
149. Kitazume, S., Saido T.C., Hashimoto, Y. (2003). Alzheimer’s β-secretase cleaves
a glycosyltransferase as a physiological substrate. Glycoconjugate J., 278, 1486514871.
150. Tsubuki, S., Takaki, Y., Saido, T.C. (2003) Dutch, Flemish, Italian, and Arctic
mutations of APP and resistance of Aβ to physiologically relevant proteolytic
degradation. Lancet, 361, 1957-1958.
151. Zhang, J., Miyamoto, K., Hashioka, S., Hao, H. P., Murao, K., Saido, T.C.,
Nakanishi, H. (2003). Activation of µ-calpain in developing cortical neurons
following methylmercury treatment. Develop. Brain Res., 142, 105-110.
152. Porn-Ares, I., Saido, T.C., Tommy, A., Ares, M. P.S. (2003) Oxidized low-density
lipoprotein induces calpain-dependent cell death and ubiquitination of caspase-3 in
HMEC-1 endothelial cells. Biochem. J., 374, 403-411.
153. Yokota, M., Saido, T.C., Kamitani, H., Tabuchi, S., Satokata, I., Watanabe, T.
(2003). Calpain induces proteolysis of neuronal cytoskeleton in ischemic gerbil
forebrain. Brain Res., 984, 122-132.
154. Rami, A., Volkmann, T., Agarwal, R., Schoninger, S., Nuernberger, F., Saido,
T.C., Winckler, J. (2003). β2-adrenergic receptor responsiveness of the calpaincalpastatin system and attenuation of neuronal death in rat hippocampus after
transient global ischemia. Neurosci. Res., 47, 373-382.
155. Wang, D.-S., Iwata, N., Hama, E., Saido, T.C., Dickson, D.W. (2003). Oxidized
neprilysin in aging and Alzheimer’s disease brains. Biochem. Biophys. Res.
Commun., 310, 236-241.
156. Yamashima, T., Tonchev, A.B., Tsukada, T., Saido, T.C., Imajoh-Ohmi, S.,
Momoi, T., Kominami, E. (2003). Sustained calpain activation associated withlysosomal rapture executes necrosis of the postischemic CA1 neurons in primates.
Hippocampus, 13, 791-800.
157. Inoue, H., Tsukita, K., Iwasato, T., Suzuki, Y., Tomioka, M., Tateno, M., Nagao,
M., Kawata, A., Saido, T.C., Miura, M., Misawa, H., Itohara, S., Takahashi, R.
(2003). The crucial role of caspase-9 in the disease progression of transgenic ALS
mouse model. EMBO J., 22, 6665-6674.
158. Wakutani, Y., Watanabe, K., Adachi, Y., Wada-Isoe, K., Urakami, K., Ninomiya,
H., Saido, T.C., Hashimoto, T., Iwatsubo, T., Nakashima, K. (2004). Novel amyloid

14
precursor protein missense mutation in probable Alzheimer’s disease. J. Neurol.
Neurosurg. Psych., 75, 1039-1042.
159. Iwata, N., Mizukami, H., Shirotani, K., Takaki, Y., Muramatsu, S., Gerard, N.,
Gerard, C., Ozawa, K., Saido, T.C. (2004). Presynaptic localization of neprilysin
contributes to efficient clearance of amyloid β peptide in mouse brain. J. Neurosci.,
24, 991-998.
160. Kimura, T., Shuto, D., Kasai, S., Liu, P., Hidaka, K., Hamada, T., Hayashi, Y.,
Hattori, C., Asai, M., Kitazume, S., Saido, T.C., Ishiura, S., Kiso, Y. (2004). KMI358 and KMI-370, highly potent and small-sized BACE1 inhibitors containing
phenylmorstatine. Bioorg. & Med. Chem. Lett., 14, 1527-1531.
161. Kitazume, S., Saido, T.C., Hashimoto, Y. (2004). Alzheimer’s β-secretase cleaves
a glycosyltransferase as a physiological substrate. Glycoconjugate J., 20, 59-62.
162. Hama, E., Shirotani, K., Iwata, N., Saido, T.C. (2004). Effects of neprilysin
chimeric proteins targeted to subcellular compartments on amyloid β peptide
clearance in primary neurons. J. Biol. Chem., 279, 30259-30264.
163. Sato, K., Higuchi, M., Iwata, N., Saido, T.C., Sasamoto, K. (2004). Fluorosubstituted and 13C-labled styrylbenzene derivatives for detecting brain amyloid
plaques. Eur. J. Med. Chem., 39, 573-578.
164. Ladrech, S., Guitton, M., Saido, T.C., Lenoir, M. (2004). Calpain activity in the
Amikacin-damaged rat cochlea. J. Comp. Neurol., 477, 149-160.
165. Funamoto, S., Morishima-Kawashima, M., Tanimura, Y., Hirotani, N., Saido,
T.C., Ihara, Y. (2004). Truncated carboxyl-terminal fragments of β-amyloid
precursor protein are processed to amyloid β-proteins 40 and 42. Biochemistry, 43,
13532-13540.
166. Bialkowska, K., Saido, T.C., Fox, J.E.B. (2004). SH3 domain of spectrin
participates in the activation of Rac in specialized calpain-induced integrin signaling
complexes. J. Cell Science, 118, 381-395.
167. Shin, R.W., Saido T.C. Maeda, M., Kitamoto, T. (2005). Novel α-secretasecleavage of Alzheimer’s amyloid β precursor protein in the endoplasmic reticulumof COS7 cells. Neurosci. Lett., 376, 14-19.
168. Saito, T., Iwata, N., Tsubuki, S., Takaki, Y., Takano, J., Huang, S.-H., Suemoto,T., Higuchi, M., Saido, T.C. (2005). Somatostatin regulates brain amyloid β peptide,Aβ42, through modulation of proteolytic degradation. Nat. Med., 11, 434-439.
169. Qi-Takahara, Yue, Morishima-Kawashima, M., Tanimura, Y., Dolios, G.,
Hirotani, N., Horikoshi, Y., Kametani, F., Maeda, M., Saido, T.C., Wang, R., Ihara,
Y. (2005). Longer forms of amyloid β protein: Implications for the mechanism of
intramembrane cleavage by γ-secretase. J. Neurosci., 25, 436-445.
170. Takano, J., Tomioka, M., Tsubuki, T., Higuchi, M., Iwata, N. Itohara, S., Maki,
M., Saido, T.C. (2005). Calpain mediates excitotoxic DNA fragmentation via
mitochondrial pathways: evidence from calpastatin-mutant mice. J. Biol. Chem.,
280, 16175-16184.
171. Higuchi, M., Tomioka, M., Takano, J., Shirotani, K., Iwata, N., Masumoto, H.,
Maki, M., Itohara, S., Saido, T.C. (2005). Distinct mechanistic roles of calpain andcaspase activation in neurodegeneration as revealed in mice over-expressing their
specific inhibitors. J. Biol. Chem., 280, 15229-15237.
172. Higuchi, M., Iwata, N., Matsuba, Y., Sato, K., Sasamoto, K., Saido T.C. (2005).
19
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17
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Saido, T.C. (2014) Single App knock-in mouse models of Alzheimer’s disease. Nat.
Neurosci., 17, 661-663.
249. Nilsson, P., Saido, T.C. (2014) Dual roles for autophagy: Degradation andsecretion of Alzheimer’s disease Aβ peptide. Bioessays, 36, 570-578.
250. Nilsson, P., Saido, T.C. (2014) New mouse model of Alzheimer’s. ACS Chem.
Neurosci., 5, 499-502.
251. Kudo-Sakamoto, Y., Akazawa, H., Ito, K., Takano, J., Yano, M., Yabumoto, C.,
Naito, A.T., Oka, T., Lee, J.K., Sakata, Y., Suzuki, J., Saido, T.C., Komuro, I. (2014)

21
Calpain-dependent cleavage of N-cadherin is involved in the progression of postmyocardial infarction remodeling. J. Biol. Chem., 289, 19408-19491.
252. Nilsson, P., Sekiguchi, M., Akagi, T., Izumi, S., Komori, T., Hui, K., Sörgjerd, K.,
Tanaka, M., Saito, T., Iwata, N., Saido, T.C. (2015) Autophagy-Related Protein 7
Deficiency in Amyloid β (Aβ) Precursor Protein Transgenic Mice Decreases Aβ in
the Multivesicular Bodies and Induces Aβ Accumulation in the Golgi. Am. J.
Pathol., 185, 305-313.
253. Thal, D.R., Walter, J., Saido, T.C., Fändrich, M. (2015) Neuropathology andbiochemistry of Aβ and its aggregates in Alzheimer’s disease. Acta Neuropathol.,
129, 167-182.
254. Kizuka, Y., Kitazume, S., Fujinawa, R., Saito, T., Iwata, N., Saido, T.C., Nakano,M., Yamaguchi, Y., Hashimoto, Y., Staufenbiel, M., Hatsuta, H., Murayama, S.,
Manya, H., Endo, T., Taniguchi, N. (2015) An aberrant sugar modification of
BACE1 blocks its lysosomal targeting in Alzheimer’s disease. EMBO Mol. Med.,7, 175-189.
255. Machado, V.M., Morte, M.I., Carreira, B.P., Azevedo, M.M., Takano, J., Iwata,N., Saido, T.C., Asmussen, H., Horwitz, A.R., Carvalho, C.M., Araújo, I.M. (2015)
Involvement of calpains in adult neurogenesis: implications for stroke. Front Cell
Neurosci., 9:22. doi: 10.3389/fncel.2015.00022. eCollection 2015.
256. Nilsson, P., Loganathan, K., Sekiguchi, M., Winblad, B., Iwata, N., Saido, T.C.,
Tjernberg, L.O. (2015) Loss of neprilysin alters protein expression in the brain of
Alzheimer’s disease model mice. Proteomics, 10, 13275-13286.
257. Hama, H., Hioki, H., Namiki, K., Hoshida, T., Kurokawa, H., Ishidate, F., Kaneko,
T., Akagi, T., Saito, T., Saido, T., Miyawaki, A. (2015) ScaleS: an optical clearing
palette for biological imaging. Nat. Neurosci., 18, 1518-1529.
258. Zhang, H., Wu, L., Pchitskaya, E., Zakharova, O., Saito, T., Saido, T.,
Bezprozvanny, I. (2015) Neuronal store-operated calcium entry and mushroom
spine loss in amyloid precursor protein knock-in mouse model of Alzheimer’s
disease. J. Neurosci., 35, 13275-13286.
259. Huang, Y., Skwarek-Maruszewska, A., Horré, K., Vandewyer, E., Wolfs, L.,
Snellinx, A., Saito, T., Radaelli, E., Corthout, N., Colombelli, J., Lo, A.C., Van
Aerschot, L., Callaerts-Vegh, Z., Trabzuni, D., Bossers, K., Verhaagen, J., Ryten,M., Munck, S., D'Hooge, R., Swaab, D.F., Hardy, J., Saido, T.C., De Strooper, B.,
Thathiah, A. (2015) Loss of GPR3 reduces the amyloid plaque burden and improves
memory in Alzheimer’s disease mouse models. Sci. Transl. Med., 7: 309ra164. doi:
10.1126/scitranslmed.aab3492.
260. Kizuka, Y., Nakano, M., Kitazume, S., Saito, T., Saido, T.C., Taniguchi, N. (2016)
Bisecting GlcNAc modification stabilizes BACE1 protein under oxidative stressconditions. Biochem. J. 473, 21-30.
261. Nagata, K., Kiryu-Seo, S., Tamada, H., Okuyama-Uchimura, F., Kiyama, H.,
Saido, T.C. (2016) ECEL1 mutation implicates impaired axonal arborization of
motor nerves in the pathogenesis of distal arthrogryposis. Acta Neuropathol. 132,
111-26.
262. Howatt, D.A., Balakrishnan, A., Moorleghen, J.J., Muniappan, L., Rateri, D.L,.
Uchida, H.A., Takano, J., Saido, T.C., Chishti, A.H., Baud, L., Subramanian, V.
(2016) Leukocyte calpain deficiency reduces angiotensin II-induced inflammation
and atherosclerosis but not abdominal aortic aneurysms in mice. Arterioscler.
Thromb. Vasc. Biol., 36, 835-845.
263. Veugelen, S., Saito, T., Saido, T.C., Chávez-Gutiérrez, L., De Strooper, B. (2016)
Familial Alzheimer’s disease mutations in presenilin generate amyloidogenic Aβ
peptide seeds. Neuron, 90, 410-416.
264. Saito T, Matsuba Y, Yamazaki N, Hashimoto S, Saido TC.* (2016) Calpain
Activation in Alzheimer's Model Mice Is an Artifact of APP and Presenilin
Overexpression. J Neurosci., 36, 9933-9936.
265. Masuda A, Kobayashi Y, Kogo N, Saito T, Saido TC*, Itohara S. (2016) Cognitive
deficits in single App knock-in mouse models. Neurobiol Learn Mem.

22
266. Ono, Y., Saido, T.C., Sorimachi, H. (2016) Calpain research for drug discovery:
challenges and potential. Nat. Rev. Drug. Discov., 12, 854-876. doi:
10.1038/nrd.2016.212.
267. Kovacs, L., Han, W., Rafikov, R., Bagi, Z., Offermanns, S., Saido, T.C., Black,
S.M., Su, Y. (2016) Activation of Calpain-2 by Mediators in Pulmonary Vascular
Remodeling of Pulmonary Arterial Hypertension. Am. .J Respi.r Cell Mol. Biol., 54,
384-393.
268. Fujita, K., Motoki, K., Tagawa, K., Chen, X., Hama, H., Nakajima, K., Homma,
H., Tamura, T., Watanabe, H., Katsuno, M., Matsumi, C., Kajikawa, M., Saito, T.,
Saido, T., Sobue, G., Miyawaki, A., Okazawa, H. (2016) HMGB1, a pathogenic
molecule that induces neurite degeneration via TLR4-MARCKS, is a potential
therapeutic target for Alzheimer's disease. Sci. Rep., 2016 Aug 25;6:31895. doi:
10.1038/srep31895.
269. Fazzari, P., Horre, K., Arranz, A.M., Frigerio, C.S., Saito, T., Saido, T.C., De
Strooper, B. (2017) PLD3 gene and processing of APP. Nature. 25, 541, E1-E2.
doi:10.1038/nature21030
270. Guix, F.X., Sannerud, R., Berditchevski, F., Arranz, A.M., Horré, K., Snellinx, A.,
Thathiah, A., Saido T, Saito, T., Rajesh, S., Overduin, M., Kumar-Singh, S., Radaelli,E., Corthout, N., Colombelli, J., Tosi, S., Munck, S., Salas, I.H., Annaert, W., De
Strooper, B. (2017) Tetraspanin 6: a pivotal protein of the multiple vesicular bodydetermining exosome release and lysosomal degradation of amyloid precursor
protein fragments. Mol. Neurodegener., 12(1):25. doi: 10.1186/s13024-017-01650.
271. Batiuk, M.Y., de Vin, F., Duqué, S.I., Li, C., Saito, T., Saido, T., Fiers, M.,
Belgard, T.G., Holt, M.G. (2017) An immunoaffinity-based method for isolating
ultrapure adult astrocytes based on ATP1B2 targetting by the ACSA-2 antibody. J.
Biol. Chem., 292, 8874-8891.
272. Nakazono, T., Lam, T.N., Patel, A.Y., Kitazawa, M., Saito, T., Saido, T.C.,
Igarashi, K.M. (2017) Impaired in vivo gamma oscillations in the medial entorhinal
cortex of knock-in Alzheimer model. Front. Syst. Neurosci., doi:
10.3389/fnsys.2017.00048.
273. Szaruga, M., Munteanu, B., Lismont, S., Veugelen, S., Horré, K., Mercken,
M., Saido, T.C., Ryan, N.S., De Vos, T., Savvides, S.N., Gallardo, R., Schymkowitz,
J., Rousseau, F., Fox, N.C., Hopf, C., De Strooper, B., Chávez-Gutiérrez, L. (2017)
Alzheimer's-causing mutations shift Aβ length by destabilizing γ-secretase-Aβninteractions. Cell, 170, 443-456.
274. Wang, H., Williams, D., Griffin, J., Saito, T., Saido, T.C., Fraser, P.E., Rogaeva,
E., Schmitt-Ulms, G. (2017) Time-course global proteome analyses reveal an
inverse correlation between Aβ burden and immunoglobulin M levels in the
APPNL-F mouse model of Alzheimer disease. PLoS One, 23;12(8):e0182844. doi:
10.1371/journal.pone.0182844.
275. Sasaguri, H., Nilsson, P., Hashimoto, S., Nagata, K., Saito, T., De Strooper, B.,
Hardy, J., Vassar, R., Winblad, B., Saido, T.C. (2017) APP mouse models for
Alzheimer’s disease preclinical studies. EMBO J., 36, 2473-2487.
276. Mano, T., Nagata, K., Nonaka, T., Tarutani, A., Imamura, T., Hashimoto, T.,
Bannai, T., Koshi-Mano, K., Tsuchida, T., Ohtomo, R., Takahashi-Fujigasaki, J.,
Yamashita, S., Ohyagi, Y., Yamasaki, R., Tsuji, S., Tamaoka, A., Ikeuchi, T., Saido,
T.C., Iwatsubo, T., Ushijima, T., Murayama, S., Hasegawa, M., Iwata, A. (2017)
Neuron-specific methylome analysis reveals epigenetic regulation and tau-related
dysfunction of BRCA1 in Alzheimer's disease. Proc. Natl. Acad. Sci. USA, 114,
E9645-E9654.
277. Nagata, K., Takahashi, M., Kryu-Seo, S., Kiyama, H., Saido, T.C. (2017) Distinct
functional consequences of ECEL1/DINE missense mutations in the pathogenesisof congenital contracture disorders. Acta Neuropathol. Commun., 5:83, doi
10.1186/s40478-017-0486-9.
278. Whyte, L.S., Hemsley, K.M., Lau, A.A., Hassiotis, S., Saito, T., Saido, T.C.,
Hopwood, J.J., Sargeant, T.J. (2018) Reduction in open field activity in the absence

23
of memory deficits in the AppNL-G-F knock-in mouse model of Alzheimer's disease.
Behav. Brain Res., 336, 177-181. doi: 10.1016/j.bbr.2017.09.006.
279. Castillo, E., Leon, J., Mazzei, G., Abolhassani, N., Haruyama, N., Saito, T., Saido,T., Hokama, M., Iwaki, T., Ohara, T., Ninomiya, T., Kiyohara, Y., Sakumi, K.,
LaFerla, F.M., Nakabeppu, Y. (2017) Comparative profiling of cortical gene
expression in Alzheimer's disease patients and mouse models demonstrates a link
between amyloidosis and neuroinflammation. Sci. Rep. 7(1):17762. doi:
10.1038/s41598-017-17999-3.
280. Moriguchi, S., Kita, S., Fukaya, M., Osanai, M., Inagaki, R., Sasaki, Y., Izumi, H.,
Horie, K., Takeda, J., Saito, T., Sakagami, H., Saido, T.C, Iwamoto, T., Fukunaga,
K. (2018) Reduced expression of Na+/Ca2+ exchangers is associated with cognitive
deficits seen in Alzheimer's disease model mice. Neuropharmacology. , 131:291303.
281. Kidana, K., Tatebe, T., Ito, K., Hara, N., Kakita, A., Saito, T., Takatori, S., Ouchi,
Y., Ikeuchi, T., Makino, M., Saido, T.C., Akishita, M., Iwatsubo, T., Hori, Y.,
Tomita, T. (2018) Loss of kallikrein-related peptidase 7 exacerbates amyloid
pathology in Alzheimer's disease model mice. EMBO Mol. Med. doi:
10.15252/emmm.201708184.
282. Nagata, K., Mano, T., Murayama, S., Saido, T.C., Iwata, A. (2018) DNA
methylation level of the neprilysin promoter in Alzheimer's disease brains. Neurosci.
Lett. 670(23), 8-13. doi: 10.1016/j.neulet.2018.01.003.
283. Peters, D.G., Pollack, A.N., Cheng, K.C., Sun, D., Saido, T., Haaf, M.P., Yang,
Q.X., Connor, J.R., Meadowcroft, M.D. (2018) Dietary lipophilic iron alters
amyloidogenesis and microglial morphology in Alzheimer's disease knock-in APP
mice. Metallomics, doi: 10.1039/c8mt00004b.
284. Hashimoto, S., Ishii, A., Kamano, N., Watamura, N., Saito, T., Oshima, T.,
Yokosuka, M., Saido, T.C. (2018) Endoplasmic reticulum stress responses in mousemodels of Alzheimer disease: overexpression paradigm versus knock-in paradigm.
J. Biol. Chem. 293, 3118-3125.
285. Salas, I.H., Weerasekera, A., Ahmed, T., Callaerts-Vegh, Z., Himmelreich, U.,
D'Hooge, R., Balschun, D., Saido, T.C., De Strooper, B., Dotti, C.G. (2018) Highfat diet treatment impairs hippocampal long-term potentiation without alterations of
the core neuropathological features of Alzheimer disease. Neurobiol. Dis., 11, 8296.
286. Izumi, H., Shinoda, Y., Saito, T., Saido, T.C., Sato, K., Yabuki, Y., Matsumoto,Y., Kanemitsu, Y., Tomioka, Y., Abolhassani, N., Nakabeppu, Y., Fukunaga, K.
(2018) The disease-modifying drug candidate, SAK3 improves cognitive
impairment and inhibits amyloid beta deposition in App knock-in mice.
Neuroscience, 377, 87-97.
287. Loera-Valencia, R., Piras, A., Ismail, MAM, Manchanda, S., Eyjolfsdottir,
H., Saido, T.C., Johansson, J., Eriksdotter, M., Winblad, B., Nilsson, P. (2018)
Targeting Alzheimer's disease with gene and cell therapies. J. Intern. Med., 284, 236.
288. Shah, D., Latif-Hernandez, A., De Strooper, B., Saito, T., Saido, T., Verhoye, M.,
D’Hooge, R., Van der Linden, A. (2018) Spatial reversal learning defect coincides
with hypersynchronous telencephalic BOLD functional connectivity in APPNL-F/NLF
knock-in mice. Sci. Rep., 8(1):6264. doi: 10.1038/s41598-018-24657-9.
289. Hashimoto, S., Saido, T.C. (2018) Critical review: involvement of endoplasmic
reticulum stress in the aetiology of Alzheimer's disease. Open Biol., 8(4). pii:
180024. doi: 10.1098/rsob.180024.
290. Nagata, K.*, Takahashi, M., Matsuba, Y., Okuyama-Uchimura, F., Sato, K.,
Hashimoto, S., Saito, T., Saido, T.C.* (2018) Generation of single App knock-in
mice reveals deletion mutations protective against the Alzheimer’s disease-like
pathology. Nat. Commun., 9(1) :1800. doi: 10.1038/s41467-018-04238-0.
291. Brown, R., Lam, A.D., Gonzalez-Sulser, A., Ying, A., Jones, M., Chou, R.C.,
Tzioras, M., Jordan, C.Y., Jedrasiak-Cape, I., Hemonnot, A.L., Abou Jaoude, M.,
Cole, A.J., Cash, S.S., Saito, T., Saido, T., Ribchester, R.R., Hashemi, K., Oren, I..
(2018) Circadian and Brain State Modulation of Network Hyperexcitability in24
Alzheimer's Disease. eNeuro. 17;5(2). pii: ENEURO.0426-17.2018. doi:
10.1523/ENEURO.0426-17.2018.
292. Swartzlander, D.B., Propson, N.E., Roy, E.R., Saito, T., Saido, T., Wang, B.,
Zheng, H. (2018) Concurrent cell type-specific isolation and profiling of mousebrains in inflammation and Alzheimer's disease. JCI Insight. 3(13). pii: 121109. doi:
10.1172/jci.insight.121109.
293. Sasaguri, H., Nagata, K., Sekiguchi, M., Fujioka, R., Matsuba, Y., Hashimoto, S.,
Sato, K., Kurup, D., Yokota, T., Saido, T.C. (2018) Introduction of pathogenic
mutations into the mouse Psen1 gene by Base Editor and Target-AID. Nat.
Commun., 9(1):2282. doi: 10.1038/s41467-018-05262-w.
294. Sakakibara, Y., Sekiya, M., Saito, T., Saido, T.C., Iijima, K.M. (2018) Cognitiveand emotional alterations in App knock-in mouse models of Aβ amyloidosis. BMC
Neurosci. 19(1):46. doi: 10.1186/s12868-018-0446-8.
295. Chen, L., Saito, T., Saido, T.C., Mody, I. (2018) Novel Quantitative Analyses of
Spontaneous Synaptic Events in Cortical Pyramidal Cells Reveal Subtle
Parvalbumin-Expressing Interneuron Dysfunction in a Knock-In Mouse Model of
Alzheimer's Disease. eNeuro, 5(4). pii: ENEURO.0059-18.2018. doi:
10.1523/ENEURO.0059-18.2018.
296. Tanaka, H., Kondo, K., Chen, X., Homma, H., Tagawa, K., Kerever, A., Aoki, S.,
Saito, T., Saido, T., Muramatsu SI, Fujita K, Okazawa H. (2018) The intellectual
disability gene PQBP1 rescues Alzheimer's disease pathology. Mol. Psychiatry. doi:
10.1038/s41380-018-0253-8.
297. Mehla, J., Deibel, S.H., Faraji, J., Saito, T., Saido, T.C., Mohajerani, M.H.,
McDonald, R.J. (2018) Looking beyond the standard version of the Morris watertask in the assessment of mouse models of cognitive deficits. Hippocampus, in press.
298. Salas, I.H., Callaerts-Vegh, Z., D’Hooge, R., Saido, T.C., Dotti, CG., De Strooper,B. (2018) Increased insoluble Amyloid-β induces negligible cognitive deficits in old
AppNL/NL knock-in mice. J. Alzheimers Dis., 66, 801-809. doi: 10.3233/JAD180410.
299. Kiryu-Seo, S., Nagata, K., Saido, T.C., Kiyama, H. (2018) New Insights of a
Neuronal Peptidase DINE/ECEL1: Nerve Development, Nerve Regeneration and
Neurogenic Pathogenesis. Neurochem. Res., doi: 10.1007/s11064-018-2665-x.
300. Saito, T., Saido, T.C. (2018) Neuroinflammation in mouse models of Alzheimer's
disease. Clin. Exp. Neuroimmunol., 9(4), 211-218. doi: 10.1111/cen3.12475.
301. Purro, S.A., Farrow, M.A., Linehan, J., Nazari, T., Thomas, D.X., Chen, Z.,
Mengel, D., Saito, T., Saido, T., Rudge, P., Brandner, S., Walsh, D.M., Collinge, J.
(2018) Transmission of amyloid-β protein pathology from cadaveric pituitary
growth hormone. Nature, 564, 415-419. doi: 10.1038/s41586-018-0790-y
302. Wang, S,. Yabuki, Y., Matsuo, K., Xu, J., Izumi, H., Sakimura, K., Saito, T., Saido,
T.C., Fukunaga, K. (2018) T-type calcium channel enhancer SAK3 promotes
dopamine and serotonin releases in the hippocampus in naive and amyloid precursor
proteinknock-in
mice.
PLoS
One,
13(12):
e0206986.
doi:
10.1371/journal.pone.0206986.
303. Mehla, J., Deibel, S.H., Faraji, J., Saito, T., Saido, T.C., Mohajerani, M.H.,
McDonald, R.J. (2019) Looking beyond the standard version of the Morris watertask in the assessment of mouse models of cognitive deficits. Hippocampus, 29(1),3-14. doi: 10.1002/hipo.22999.
304. Petrache, A.L., Rajulawalla, A., Shi, A., Wetzel, A., Saito, T., Saido, T.C., Harvey,
K., Ali, A.B. (2019) Aberrant excitatory-inhibitory synaptic mechanisms inentorhinal cortex microcircuits during the pathogenesis of Alzheimer’s disease.
Cereb. Cortex., 29(4), 1834-1850. doi: 10.1093/cercor/bhz016.
305. Yamakage, Y., Tsuiji, H., Kohno, T., Ogino, H., Saito, T., Saido, T.C., Hattori, M.
(2019) Reducing ADAMTS-3 inhibits amyloid β deposition in App knock-in mouse.
Biol. Pharm. Bull., 42 (3), 354-356.
306. Sakakibara, Y., Sekiya, M., Saito, T., Saido, T.C., Iijima, K.M. (2019) Amyloidβ plaque formation and reactive gliosis are required for induction of cognitive
deficits in App knock-in mouse models of Alzheimer's disease. BMC Neurosci.,
20(1):13. doi: 10.1186/s12868-019-0496-6.

25

Editorial
1. Aβ Metabolism and Alzheimer’s Disease. (Saido, T.C. ed.), Landes Bioscience(Georgetown, Tex), also available at www.eurekah.com (2003).
Books and book chapters
1. Suzuki, K., Sorimachi, H., Hata, A., Ohno, S., Emori, Y., Kawasaki, H., Saido, T.C.,
Imajoh-Ohmi, S., Akita, Y. (1990). Calcium-dependent protease, a novel molecularspecies, regulation of gene expression, and activation at the cell membrane. in
Neurotoxicity of Excitatory Amino Acids (Guidotti, A. ed.), Raven Press (New
York), pp. 79-93.
2. Saido, T.C., Shiramine, M., Tsukaguchi, M., Ito, H., Nagao, S., Tsuchiya, T., Suzuki,
K. (1992). Autolytic activation of µ-calpain as probed by an active form-specificantibody. in Recent Advances in Cellular and Molecular Biology, Vol. 4 (Wegmann,
R.J., and Wegmann, M.A. eds.), Peeters Press (Leuven), pp. 375-380.
3. Saido, T.C., Suzuki, K. (1993). Calpain: new aspects in activation processes andphysiological roles. in Innovations in Proteases and their inhibitors (Aviles, F.X.
ed.), Walter de Gruyter (Berlin), pp. 197-214.
4. Saido, T.C., Yokota, M., Tani, E., Kawashima, S. (1997). Post-secretory catabolismof β-amyloid in brain. in Alzheimer’s Disease: Biology, Diagnosis andTherapeutics (Iqbal, K., Winblad, B., Nishimura, T., Takeda, M., Wisniewski, H.M.,
eds.), John Wiley & Sons Ltd. (Chichester), pp. 337-346.
5. Fox, J.E.B., Saido, T.C. (1999). Calpain in signal transduction. in Calpain:
Pharmacology and Toxicology of a calcium-dependent cellular protease (Wang,
K.K.W., Yuen, P.-w., eds.), Taylor & Francis. (Brisotol), pp. 103-126.
6. Saido, T.C., Iwata, N. (2000). Catabolism of amyloid-β peptide in brain parenchyma.
in Neuroscientific Basis of Dementia (Tanaka, C., Ihara, Y., and McGeer, P.L., eds.),
Birkhauser Verlag, pp. 249-256.
7. Lee, H.-J., Suzuki, K., Saido, T.C. (2000). Genes of Mammalian Proteinase. in Roleof Proteases in the Pathophysiology of Neurodegenerative Disease (Banik, N.L.
ed.) Plenum Press, New York.
8. Iwata, N., Saido, T.C. (2001). Alzheimer's disease as a proteolytic disorder:
catabolism and processing of amyloid β peptide. in Mapping the progress of
Alzheimer’s and Parkinson’s disease (Mizuno, Y. ed.) Kluwer Academic/Plenum
Publishers, New York.
9. Saido, T.C. (2003). Aβ metabolism: from Alzheimer research to brain aging control.
In Aβ Metabolism and Alzheimer’s Disease (Saido, T.C. ed) Landes Bioscience(Georgetown, Tex) www.eurekah.com (2002).
10. Saido, T.C., Nakahara, H. (2003). Proteolytic degradation of Aβ by neprilysin andother peptidases. In Aβ Metabolism and Alzheimer’s Disease (Saido, T.C. ed)
Landes Bioscience (Georgetown, Tex) www.eurekah.com (2002).
*There are 92 other scientific publications including two books in Japanese.