Ocludina
| |
| PDB, Estrutura do dominio superenrolado da ocludina humana (aa. 416-522) | |
Ocludina
| |
| Identificadores | |
| Símbolo | OCLN ; BLCPMG |
| Entrez | 100506658 |
| OMIM | |
| PDB | 1XAW, 3G7C 1WPA, 1XAW, 3G7C |
| RefSeq | NP_001192183 |
| UniProt | Q16625 |
| Outros datos | |
| Número EC | 2.1.1.67 |
| Locus | Cr. 5 68.79 – 68.85 Mb |
A ocludina é unha proteína que nos humanos está codificada polo xene OCLN.[1][2] É unha proteína integral de membrana de 65 kDa e 522 aminoácidos localizada nas unións herméticas que unen unhas células con outras. Foi descrita por primeira vez en 1993 por Shoichiro Tsukita.[3] Xunto coas proteínas claudinas, as ocludinas son os principais compoñentes das unións herméticas.
Estrutura[editar | editar a fonte]
Segundo a hidrofilidade global da molécula, esta atravesa a membrana catro veces, formando dous bucles extracelulares e expoñendo no citosol os seus extremos N-terminal e C-terminal. A interacción da ocludina con varias proteínas citoplasmáticas da placa de unión ocorre polo seu extremo C-terminal, mentres que os bucles extracelulares crese que están implicados na regulación da permeabilidade paracelular e a adhesión celular. A fosforilación/desfosforilación xoga un papel fundamental na regulación da ocludina e das unións herméticas. [4]
Asociación con enfermidades[editar | editar a fonte]
Os trastornos na regulación da ocludina son un importante aspecto de diversas doenzas, xa que se distorsionan as barreiras celulares. As estratexias para previr ou reverter esta regulación á baixa poden ser un importante recurso terapéutico. Está implicada en diarreas, cancro, doenzas inflamatorias, alerxias, diabetes, esclerose múltiple, entre outras.[4]
Interaccións[editar | editar a fonte]
A ocludina interacciona coa proteína 2 das unións herméticas,[5][6][7] YES1[8] e coa proteína 1 das unións herméticas.[9][10]
Notas[editar | editar a fonte]
- ↑ Ando-Akatsuka Y, Saitou M, Hirase T, Kishi M, Sakakibara A, Itoh M, Yonemura S, Furuse M, Tsukita S (May 1996). "Interspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologues". J Cell Biol 133 (1): 43–47. PMC 2120780. PMID 8601611. doi:10.1083/jcb.133.1.43.
- ↑ "Entrez Gene: OCLN occludin".
- ↑ Furuse M, Hirase T, Itoh M, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S (1993). "Occludin: a novel integral membrane protein localizing at tight junctions". J. Cell Biol. 123 (6 Pt 2): 1777–1788. PMC 2290891. PMID 8276896. doi:10.1083/jcb.123.6.1777.
- ↑ 4,0 4,1 Feldman, Gemma J.; Mullin, James M; Ryan, Michael P (2005). "Occludin: Structure, function and regulation". Advanced Drug Delivery Reviews (en inglés) 57 (6): 883– 917. ISSN 0169-409X. PMID 15820558. doi:10.1016/j.addr.2005.01.009.
- ↑ Peng, Bi-Hung; Lee J Ching; Campbell Gerald A (Dec 2003). "In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis". J. Biol. Chem. 278 (49): 49644–49651 issn = 0021–9258. PMID 14512431. doi:10.1074/jbc.M302782200.
- ↑ Itoh, M; Morita K; Tsukita S (Feb 1999). "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin". J. Biol. Chem. 274 (9): 5981–5986. ISSN 0021-9258. PMID 10026224. doi:10.1074/jbc.274.9.5981.
- ↑ Wittchen, E S; Haskins J; Stevenson B R (Dec 1999). "Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3". J. Biol. Chem. 274 (49): 35179–35185. ISSN 0021-9258. PMID 10575001. doi:10.1074/jbc.274.49.35179.
- ↑ Chen, Yan-Hua; Lu Qun; Goodenough Daniel A; Jeansonne Beverly (Apr 2002). "Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells". Mol. Biol. Cell 13 (4): 1227–1237 issn = 1059–1524. PMC 102264. PMID 11950934. doi:10.1091/mbc.01-08-0423.
- ↑ Fanning, A S; Jameson B J; Jesaitis L A; Anderson J M (Nov 1998). "The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton". J. Biol. Chem. 273 (45): 29745–29753 issn = 0021–9258. PMID 9792688. doi:10.1074/jbc.273.45.29745.
- ↑ Rao, Radhakrishna K; Basuroy Shyamali, Rao Vijay U, Karnaky Jr Karl J, Gupta Akshay (Dec 2002). "Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress". Biochem. J. (England) 368 (Pt 2): 471–81. ISSN 0264-6021. PMC 1222996. PMID 12169098. doi:10.1042/BJ20011804.
Véxase tamén[editar | editar a fonte]
Bibliografía[editar | editar a fonte]
- Furuse M; Itoh M; Hirase T; et al. (1994). "Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions". J. Cell Biol. 127 (6 Pt 1): 1617–1626. PMC 2120300. PMID 7798316. doi:10.1083/jcb.127.6.1617.
- Van Itallie CM, Anderson JM (1997). "Occludin confers adhesiveness when expressed in fibroblasts". J. Cell. Sci. 110 (9): 1113–21. PMID 9175707.
- Kimura Y; Shiozaki H; Hirao M; et al. (1997). "Expression of occludin, tight-junction-associated protein, in human digestive tract". Am. J. Pathol. 151 (1): 45–54. PMC 1857944. PMID 9212730.
- Saitou M; Ando-Akatsuka Y; Itoh M; et al. (1997). "Mammalian occludin in epithelial cells: its expression and subcellular distribution". Eur. J. Cell Biol. 73 (3): 222–31. PMID 9243183.
- Haskins J; Gu L; Wittchen ES; et al. (1998). "ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin". J. Cell Biol. 141 (1): 199–208. PMC 2132714. PMID 9531559. doi:10.1083/jcb.141.1.199.
- Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM (1998). "The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton". J. Biol. Chem. 273 (45): 29745–29753. PMID 9792688. doi:10.1074/jbc.273.45.29745.
- Itoh M, Morita K, Tsukita S (1999). "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin". J. Biol. Chem. 274 (9): 5981–5986. PMID 10026224. doi:10.1074/jbc.274.9.5981.
- Jiang WG; Martin TA; Matsumoto K; et al. (1999). "Hepatocyte growth factor/scatter factor decreases the expression of occludin and transendothelial resistance (TER) and increases paracellular permeability in human vascular endothelial cells". J. Cell. Physiol. 181 (2): 319–329. PMID 10497311. doi:10.1002/(SICI)1097-4652(199911)181:2<319::AID-JCP14>3.0.CO;2-S.
- Wittchen ES, Haskins J, Stevenson BR (2000). "Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3". J. Biol. Chem. 274 (49): 35179–35185. PMID 10575001. doi:10.1074/jbc.274.49.35179.
- Kojima T; Sawada N; Chiba H; et al. (2000). "Induction of tight junctions in human connexin 32 (hCx32)-transfected mouse hepatocytes: connexin 32 interacts with occludin". Biochem. Biophys. Res. Commun. 266 (1): 222–229. PMID 10581193. doi:10.1006/bbrc.1999.1778.
- Burns AR; Bowden RA; MacDonell SD; et al. (2000). "Analysis of tight junctions during neutrophil transendothelial migration". J. Cell. Sci. 113 (1): 45–57. PMID 10591624.
- Itoh M; Furuse M; Morita K; et al. (2000). "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): 1351–1363. PMC 2168087. PMID 10601346. doi:10.1083/jcb.147.6.1351.
- Singh U; Van Itallie CM; Mitic LL; et al. (2000). "CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin". J. Biol. Chem. 275 (24): 18407–18417. PMID 10749869. doi:10.1074/jbc.M001530200.
- Marzioni D; Banita M; Felici A; et al. (2001). "Expression of ZO-1 and occludin in normal human placenta and in hydatidiform moles". Mol. Hum. Reprod. 7 (3): 279–285. PMID 11228248. doi:10.1093/molehr/7.3.279.
- Andreeva AY; Krause E; Müller EC; et al. (2001). "Protein kinase C regulates the phosphorylation and cellular localization of occludin". J. Biol. Chem. 276 (42): 38480–38486. PMID 11502742. doi:10.1074/jbc.M104923200.
- Papadopoulos MC; Saadoun S; Woodrow CJ; et al. (2001). "Occludin expression in microvessels of neoplastic and non-neoplastic human brain". Neuropathol. Appl. Neurobiol. 27 (5): 384–395. PMID 11679090. doi:10.1046/j.0305-1846.2001.00341.x.
- Schmidt A, Utepbergenov DI, Krause G, Blasig IE (2001). "Use of surface plasmon resonance for real-time analysis of the interaction of ZO-1 and occludin". Biochem. Biophys. Res. Commun. 288 (5): 1194–1199. PMID 11700038. doi:10.1006/bbrc.2001.5914.
- Pummi K; Malminen M; Aho H; et al. (2001). "Epidermal tight junctions: ZO-1 and occludin are expressed in mature, developing, and affected skin and in vitro differentiating keratinocytes". J. Invest. Dermatol. 117 (5): 1050–1058. PMID 11710912. doi:10.1046/j.0022-202x.2001.01493.x.
- Traweger A; Fang D; Liu YC; et al. (2002). "The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch". J. Biol. Chem. 277 (12): 10201–10208. PMID 11782481. doi:10.1074/jbc.M111384200.
Ligazóns externas[editar | editar a fonte]
- Vivian Tang. "OCCLUDIN in Focus". www.Zonapse.Net. Consultado o 2008-02-10.
- Vivian Tang. "Tight Junction Overview". www.Zonapse.Net. Consultado o 2008-02-10.
- GeneTests/NCBI/NIH/UW de Band-Like Calcification with Simplified Gyration and Polymicrogyria
