메뉴 건너뛰기




Volumn 22, Issue 1, 2015, Pages 1-14

Redox-sensitive structure and function of the first extracellular loop of the cell-cell contact protein claudin-1: Lessons from molecular structure to animals

Author keywords

[No Author keywords available]

Indexed keywords

CLAUDIN 1; CYSTEINE; DISULFIDE; OLIGOMER; RECOMBINANT PROTEIN; SYNTHETIC PEPTIDE;

EID: 84919333080     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2013.5706     Document Type: Article
Times cited : (30)

References (65)
  • 2
    • 70350399482 scopus 로고    scopus 로고
    • Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis
    • Angelow S and Yu ASL. Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis. J Biol Chem 284: 29205-29217, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 29205-29217
    • Angelow, S.1    Yu, A.S.L.2
  • 3
    • 0141920729 scopus 로고    scopus 로고
    • The claudin-like Megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila
    • Behr M, Riedel D, and Schuh R. The claudin-like Megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila. Dev Cell 5: 611-620, 2003.
    • (2003) Dev Cell , vol.5 , pp. 611-620
    • Behr, M.1    Riedel, D.2    Schuh, R.3
  • 7
    • 70350142141 scopus 로고    scopus 로고
    • The tetraspan protein Dni1p is required for correct membrane organization and cell wall remodelling during mating in Schizosaccharomyces pombe
    • Clemente-RamosJA,Martin-Garcia R, SharifmoghadamMR, Konomi M, Osumi M, and Valdivieso MH. The tetraspan protein Dni1p is required for correct membrane organization and cell wall remodelling during mating in Schizosaccharomyces pombe. Mol Microbiol 73: 695-709, 2009.
    • (2009) Mol Microbiol , vol.73 , pp. 695-709
    • Clemente-Ramos, J.A.1    Martin-Garcia, R.2    Sharifmoghadam, M.R.3    Konomi, M.4    Osumi, M.5    Valdivieso, M.H.6
  • 8
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio OR, Van Itallie C, Rahner C, and Anderson JM. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am J Physiol Cell Physiol 284: C1346-C1354, 2003.
    • (2003) Am J Physiol Cell Physiol , vol.284 , pp. C1346-C1354
    • Colegio, O.R.1    Van Itallie, C.2    Rahner, C.3    Anderson, J.M.4
  • 11
    • 84863244656 scopus 로고    scopus 로고
    • Sur7 promotes plasma membrane organization and is needed for resistance to stressful conditions and to the invasive growth and virulence of Candida albicans
    • Douglas LM, Wang HX, Keppler-Ross S, Dean N, and Konopka JB. Sur7 promotes plasma membrane organization and is needed for resistance to stressful conditions and to the invasive growth and virulence of Candida albicans. MBio 3: 2012.
    • (2012) MBio , pp. 3
    • Douglas, L.M.1    Wang, H.X.2    Keppler-Ross, S.3    Dean, N.4    Konopka, J.B.5
  • 12
    • 0032498622 scopus 로고    scopus 로고
    • Pheromone-regulated genes required for yeast mating differentiation
    • Erdman S, Lin L, Malczynski M, and Snyder M. Pheromone-regulated genes required for yeast mating differentiation. J Cell Biol 140: 461-483, 1998.
    • (1998) J Cell Biol , vol.140 , pp. 461-483
    • Erdman, S.1    Lin, L.2    Malczynski, M.3    Snyder, M.4
  • 15
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or-2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse M, Sasaki H, Fujimoto K, and Tsukita S. A single gene product, claudin-1 or-2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol 143: 391-401, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 17
    • 84878506887 scopus 로고    scopus 로고
    • Claudins and the modulation of tight junction permeability
    • Guenzel D and Yu AS. Claudins and the modulation of tight junction permeability. Physiol Rev 93: 525-569, 2013.
    • (2013) Physiol Rev , vol.93 , pp. 525-569
    • Guenzel, D.1    Yu, A.S.2
  • 19
    • 27744459366 scopus 로고    scopus 로고
    • Identification of intra-and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2
    • Henriksen U, Fog JU, Litman T, and Gether U. Identification of intra-and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2. J Biol Chem 280: 36926-36934, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 36926-36934
    • Henriksen, U.1    Fog, J.U.2    Litman, T.3    Gether, U.4
  • 20
    • 0347926509 scopus 로고    scopus 로고
    • Loss and recovery of the blood-nerve barrier in the rat sciatic nerve after crush injury are associated with expression of intercellular junctional proteins
    • Hirakawa H, Okajima S, Nagaoka T, Takamatsu T, and Oyamada M. Loss and recovery of the blood-nerve barrier in the rat sciatic nerve after crush injury are associated with expression of intercellular junctional proteins. Exp Cell Res 284: 196-210, 2003.
    • (2003) Exp Cell Res , vol.284 , pp. 196-210
    • Hirakawa, H.1    Okajima, S.2    Nagaoka, T.3    Takamatsu, T.4    Oyamada, M.5
  • 21
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S, and Tsukita S. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J Cell Biol 171: 939-945, 2005.
    • (2005) J Cell Biol , vol.171 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Tsukita, S.6
  • 24
    • 84896306826 scopus 로고    scopus 로고
    • Differential pathways of claudin oligomerization and integration into tight junctions
    • Koval M. Differential pathways of claudin oligomerization and integration into tight junctions. Tissue Barriers 1: e24518, 2013.
    • (2013) Tissue Barriers , vol.1
    • Koval, M.1
  • 28
    • 77955445789 scopus 로고    scopus 로고
    • Identification of phosphorylation-dependent interaction partners of the adapter protein ADAP using quantitative mass spectrometry: SILAC vs. O-18-Labeling
    • Lange S, Sylvester M, Schuemann M, Freund C, and Krause E. Identification of phosphorylation-dependent interaction partners of the adapter protein ADAP using quantitative mass spectrometry: SILAC vs. O-18-Labeling. J Proteome Res 9: 4113-4122, 2010.
    • (2010) J Proteome Res , vol.9 , pp. 4113-4122
    • Lange, S.1    Sylvester, M.2    Schuemann, M.3    Freund, C.4    Krause, E.5
  • 29
    • 84880163557 scopus 로고    scopus 로고
    • Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines
    • Li J, Angelow S, Linge A, Zhuo M, and Yu ASL. Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines. Am J Physiol Cell Physiology 305: C190-C196, 2013.
    • (2013) Am J Physiol Cell Physiology , vol.305 , pp. C190-C196
    • Li, J.1    Angelow, S.2    Linge, A.3    Zhuo, M.4    Yu, A.S.L.5
  • 30
    • 13444266488 scopus 로고    scopus 로고
    • A simple and fast secondary structure prediction method using hidden neural networks
    • Lin K, Simossis VA, Taylor WR, and Heringa J. A simple and fast secondary structure prediction method using hidden neural networks. Bioinformatics 21: 152-159, 2005.
    • (2005) Bioinformatics , vol.21 , pp. 152-159
    • Lin, K.1    Simossis, V.A.2    Taylor, W.R.3    Heringa, J.4
  • 32
    • 67849130555 scopus 로고    scopus 로고
    • PEP-FOLD: An online resource for de novo peptide structure prediction
    • Maupetit J, Derreumaux P, and Tuffery P. PEP-FOLD: an online resource for de novo peptide structure prediction. Nucleic Acids Res 37: W498-W503, 2009.
    • (2009) Nucleic Acids Res , vol.37 , pp. W498-W503
    • Maupetit, J.1    Derreumaux, P.2    Tuffery, P.3
  • 34
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita K, Furuse M, Fujimoto K, and Tsukita S. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci U S A 96: 511-516, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 37
    • 77953021608 scopus 로고    scopus 로고
    • Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules
    • Piehl C, Piontek J, Cording J, Wolburg H, and Blasig IE. Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules. Cell Mol Life Sci 67: 2131-2140, 2010.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2131-2140
    • Piehl, C.1    Piontek, J.2    Cording, J.3    Wolburg, H.4    Blasig, I.E.5
  • 39
  • 40
    • 3242766027 scopus 로고    scopus 로고
    • Tight junction proteins ZO-1, occludin, and claudins in developing and adult human perineurium
    • Pummi KP, Heape AM, Grenman RA, Peltonen JTK, and Peltonen SA. Tight junction proteins ZO-1, occludin, and claudins in developing and adult human perineurium. J Histochem Cytochem 52: 1037-1046, 2004.
    • (2004) J Histochem Cytochem , vol.52 , pp. 1037-1046
    • Pummi, K.P.1    Heape, A.M.2    Grenman, R.A.3    Peltonen, J.T.K.4    Peltonen, S.A.5
  • 41
    • 67649381830 scopus 로고    scopus 로고
    • Development and characterization of a human single-chain antibody fragment against claudin-3: A novel therapeutic target in ovarian and uterine carcinomas
    • Romani C, Comper F, Bandiera E, Ravaggi A, Bignotti E, Tassi RA, Pecorelli S, and Santin AD. Development and characterization of a human single-chain antibody fragment against claudin-3: a novel therapeutic target in ovarian and uterine carcinomas. Am J Obstet Gynecol 201: 2009.
    • (2009) Am J Obstet Gynecol , pp. 201
    • Romani, C.1    Comper, F.2    Bandiera, E.3    Ravaggi, A.4    Bignotti, E.5    Tassi, R.A.6    Pecorelli, S.7    Santin, A.D.8
  • 42
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, and Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5: 725-738, 2010.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 44
    • 2442619064 scopus 로고    scopus 로고
    • The tight junction: A multifunctional complex
    • Schneeberger EE and Lynch RD. The tight junction: a multifunctional complex. Am J Physiol Cell Physiol 286: C1213-C1228, 2004.
    • (2004) Am J Physiol Cell Physiol , vol.286 , pp. C1213-C1228
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 46
    • 79960716090 scopus 로고    scopus 로고
    • Claudin family proteins in Caenorhabditis elegans
    • Simske JS and Hardin J. Claudin family proteins in Caenorhabditis elegans. Methods Mol Biol 762: 147-169, 2011.
    • (2011) Methods Mol Biol , vol.762 , pp. 147-169
    • Simske, J.S.1    Hardin, J.2
  • 47
    • 74549219792 scopus 로고    scopus 로고
    • Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family
    • Steed E, Rodrigues NT, Balda MS, and Matter K. Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family. BMC Cell Biol 10: 95, 2009.
    • (2009) BMC Cell Biol , vol.10 , pp. 95
    • Steed, E.1    Rodrigues, N.T.2    Balda, M.S.3    Matter, K.4
  • 48
    • 0025411364 scopus 로고
    • Intrinsic mechanisms of antinociception in inflammation-local opioid receptors and beta-endorphin
    • Stein C, Gramsch C, and Herz A. Intrinsic mechanisms of antinociception in inflammation-local opioid receptors and beta-endorphin. J Neurosci 10: 1292-1298, 1990.
    • (1990) J Neurosci , vol.10 , pp. 1292-1298
    • Stein, C.1    Gramsch, C.2    Herz, A.3
  • 49
    • 0023030826 scopus 로고
    • Identification of Zo-I: A high-molecular-weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson BR, Siliciano JD,Mooseker MS, and Goodenough DA. Identification of Zo-I: a high-molecular-weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J Cell Biol 103: 755-766, 1986.
    • (1986) J Cell Biol , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 50
    • 50849106067 scopus 로고    scopus 로고
    • A second disulfide bridge from the N-terminal domain to extracellular loop 2 dampens receptor activity in GPR39
    • Storjohann L, Holst B, and Schwartz TW. A second disulfide bridge from the N-terminal domain to extracellular loop 2 dampens receptor activity in GPR39. Biochemistry 47: 9198-9207, 2008.
    • (2008) Biochemistry , vol.47 , pp. 9198-9207
    • Storjohann, L.1    Holst, B.2    Schwartz, T.W.3
  • 52
    • 26944451622 scopus 로고    scopus 로고
    • Role of C-terminal regions of the C-terminal fragment of Clostridium perfringens enterotoxin in its interaction with claudin-4
    • Takahashi A, Kondoh M, Masuyama A, Fujii M, Mizuguchi H, Horiguchi Y, and Watanabe Y. Role of C-terminal regions of the C-terminal fragment of Clostridium perfringens enterotoxin in its interaction with claudin-4. J Control Release 108: 56-62, 2005.
    • (2005) J Control Release , vol.108 , pp. 56-62
    • Takahashi, A.1    Kondoh, M.2    Masuyama, A.3    Fujii, M.4    Mizuguchi, H.5    Horiguchi, Y.6    Watanabe, Y.7
  • 53
    • 0034448329 scopus 로고    scopus 로고
    • Ionic permeability of the frog sciatic nerve perineurium: Parallel studies of potassium and lanthanum penetration using electrophysiological and electron microscopic techniques
    • Todd BA, Inman C, Sedgwick EM, and Abbott J. Ionic permeability of the frog sciatic nerve perineurium: parallel studies of potassium and lanthanum penetration using electrophysiological and electron microscopic techniques. J Neurocytol 29: 551-567, 2000.
    • (2000) J Neurocytol , vol.29 , pp. 551-567
    • Todd, B.A.1    Inman, C.2    Sedgwick, E.M.3    Abbott, J.4
  • 54
  • 55
    • 33845370795 scopus 로고    scopus 로고
    • Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities
    • Van Itallie CM, Rogan S, Yu A, Vidal LS, Holmes J, and Anderson JM. Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities. Am J Physiol Renal Physiol 291: F1288-F1299, 2006.
    • (2006) Am J Physiol Renal Physiol , vol.291 , pp. F1288-F1299
    • Van Itallie, C.M.1    Rogan, S.2    Yu, A.3    Vidal, L.S.4    Holmes, J.5    Anderson, J.M.6
  • 57
    • 0018407408 scopus 로고
    • Modification of permeability of frog perineurium to [C-14]-sucrose by stretch and hypertonicity
    • Weerasuriya A, Rapoport SI, and Taylor RE. Modification of permeability of frog perineurium to [C-14]-sucrose by stretch and hypertonicity. Brain Res 173: 503-512, 1979.
    • (1979) Brain Res , vol.173 , pp. 503-512
    • Weerasuriya, A.1    Rapoport, S.I.2    Taylor, R.E.3
  • 58
    • 4544311402 scopus 로고    scopus 로고
    • Selective decrease in paracellular conductance of tight junctions: Role of the first extracellular domain of claudin-5
    • Wen HJ, Watry DD, Marcondes MCG, and Fox HS. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol Cell Biol 24: 8408-8417, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 8408-8417
    • Wen, H.J.1    Watry, D.D.2    Marcondes, M.C.G.3    Fox, H.S.4
  • 59
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • Wienken CJ, Baaske P, Rothbauer U, Braun D, and Duhr S. Protein-binding assays in biological liquids using microscale thermophoresis. Nat Commun 1: 100, 2010.
    • (2010) Nat Commun , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 60
    • 67650553423 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3
    • Winkler L, Gehring C, Wenzel A, Mueller SL, Piehl C, Krause G, Blasig IE, and Piontek J. Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3. J Biol Chem 284: 18863-18872, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 18863-18872
    • Winkler, L.1    Gehring, C.2    Wenzel, A.3    Mueller, S.L.4    Piehl, C.5    Krause, G.6    Blasig, I.E.7    Piontek, J.8
  • 61
    • 33846786558 scopus 로고    scopus 로고
    • Targeted and reversible disruption of the blood-testis barrier by an FSH mutant-occludin peptide conjugate
    • Wong CH, Mruk DD, Lee WM, and Cheng C. Targeted and reversible disruption of the blood-testis barrier by an FSH mutant-occludin peptide conjugate. FASEB J 21: 438-448, 2007.
    • (2007) FASEB J , vol.21 , pp. 438-448
    • Wong, C.H.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.4
  • 62
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 40, 2008.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 63
    • 0020525719 scopus 로고
    • Ethical guidelines for investigations of experimental pain in conscious animals
    • Zimmermann M. Ethical guidelines for investigations of experimental pain in conscious animals. Pain 16: 109-110, 1983.
    • (1983) Pain , vol.16 , pp. 109-110
    • Zimmermann, M.1
  • 65
    • 84861972468 scopus 로고    scopus 로고
    • Claudin-derived peptides are internalized via specific endocytosis pathways
    • Zwanziger D, Staat C, Andjelkovic AV, and Blasig IE. Claudin-derived peptides are internalized via specific endocytosis pathways. Ann NY Acad Sci 1257: 29-37, 2012.
    • (2012) Ann NY Acad Sci , vol.1257 , pp. 29-37
    • Zwanziger, D.1    Staat, C.2    Andjelkovic, A.V.3    Blasig, I.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.