クローディン2

クローディン2（英: claudin-2）は、約23 kDa（キロダルトン）の膜タンパク質である。細胞膜を4回貫通しており、N末端とC末端は細胞質にある。C末端のチロシン-バリンを含む保存されたPDZ結合モチーフを介してタイトジャンクション裏打ちタンパク質のZO-1と結合する。 クローディン2は、クローディンファミリーの一つでタイトジャンクションの主要構成成分である。特に、肝臓や腎臓に発現が多い。leakyタイプのクローディンに分類され、カチオンをよく通す。 クローディン2のノックアウトマウスは一見正常だが、腎臓の近位尿細管のタイトジャンクションにおける水と塩化ナトリウムの再吸収が低下しているため、塩負荷時の飲水量が上昇する。 クローディン2は1998年に京都大学の月田承一郎らのグループによって報告された。 ^ a b c GRCh38: Ensembl release 89: ENSG00000165376 - Ensembl, May 2017 ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000047230 - Ensembl, May 2017 ^ Human PubMed Reference: ^ Mouse PubMed Reference: ^ Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol, 147(6): 1351-63, 1999. PMID 10601346 ^ a b Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita Sh. Claudin-1 and-2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol, 141(7): 1539-50, 1998. PMID 9647647 ^ Morita K, Sasaki H, Fujimoto K, Furuse M, Tsukita Sh. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA, 96(2): 511-6, 1999. PMID 9892664 ^ Furuse M, Furuse K, Sasaki H, Tsukita Sh. Conversion of zolulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol, 153(2): 263-72, 2001. PMID 11309408 ^ Amasheh S, Meiri N, Gitter AH, Schöneberg T, Mankertz J, Schulzke JD, Fromm M. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci, 115(Pt 24): 4969-76, 2002. PMID 12432083 ^ Muto S, Hata M, Taniguchi J, Tsuruoka S, Moriwaki K, Saitou M, Furuse K, Sasaki H, Fujimura A, Imai M, Kusano E, Tsukita Sh, Furuse M. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc Natl Acad Sci USA, 107(7): 8011-6, 2010. PMID 20385797 “Tight junctions of the blood-brain barrier”. Cell. Mol. Neurobiol. 20 (1): 57–76. (2000). doi:10.1023/A:1006995910836. PMID 10690502.  “The roles of claudin superfamily proteins in paracellular transport”. Traffic 2 (2): 93–8. (2001). doi:10.1034/j.1600-0854.2001.020203.x. PMID 11247307.  “Multifunctional strands in tight junctions”. Nat. Rev. Mol. Cell Biol. 2 (4): 285–93. (2001). doi:10.1038/35067088. PMID 11283726.  “Claudin-based barrier in simple and stratified cellular sheets”. Curr. Opin. Cell Biol. 14 (5): 531–6. (2002). doi:10.1016/S0955-0674(02)00362-9. PMID 12231346.  “Tight junction proteins”. Prog. Biophys. Mol. Biol. 81 (1): 1–44. (2003). doi:10.1016/S0079-6107(02)00037-8. PMID 12475568.  “Role of claudins in tumorigenesis”. Adv. Drug Deliv. Rev. 57 (6): 919–28. (2005). doi:10.1016/j.addr.2005.01.006. PMID 15820559.  “HIV tat and neurotoxicity”. Microbes Infect. 8 (5): 1347–57. (2006). doi:10.1016/j.micinf.2005.11.014. PMID 16697675.  “Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus”. PLOS Pathog. 3 (8): e108. (2007). doi:10.1371/journal.ppat.0030108. PMC 1959368. PMID 17784784. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1959368/.  “Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin”. J. Cell Biol. 141 (7): 1539–50. (1998). doi:10.1083/jcb.141.7.1539. PMC 2132999. PMID 9647647. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132999/.  “SEMP1, a senescence-associated cDNA isolated from human mammary epithelial cells, is a member of an epithelial membrane protein superfamily”. Gene 226 (2): 285–95. (1999). doi:10.1016/S0378-1119(98)00553-8. PMID 9931503.  “Manner of interaction of heterogeneous claudin species within and between tight junction strands”. J. Cell Biol. 147 (4): 891–903. (1999). doi:10.1083/jcb.147.4.891. PMC 2156154. PMID 10562289. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2156154/.  “Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins”. J. Cell Biol. 147 (6): 1351–63. (1999). doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID 10601346. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2168087/.  “Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer”. Hum. Genet. 107 (3): 249–56. (2000). doi:10.1007/s004390000375. PMID 11071387.  “Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases”. J. Biol. Chem. 276 (30): 28204–11. (2001). doi:10.1074/jbc.M103083200. PMID 11382769.  “Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule”. J. Biol. Chem. 277 (1): 455–61. (2002). doi:10.1074/jbc.M109005200. PMID 11689568.  “A systems proteomics view of the endogenous human claudin protein family”. J Proteome Res 15 (2): 339–359. (2015). doi:10.1021/acs.jproteome.5b00769. PMC 4777318. PMID 26680015. https://archive-ouverte.unige.ch/unige:79118/ATTACHMENT01.