Troponina I tipo 2
(Redirección desde «TNNI2»)
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| PDB 1a2x | |
Troponina I tipo 2 (músculo esquelético, rápida)
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| Identificadores | |
| Símbolo | TNNI2 |
| Símbolos alt. | AMCD2B, DA2B, FSSV |
| Entrez | 7136 |
| HUGO | 11946 |
| OMIM | |
| RefSeq | NM_003282 |
| UniProt | P48788 |
| Outros datos | |
| Locus | Cr. 11 p15.5 |
A troponina I, músculo esquelético rápido ou troponina I tipo 2 (TNNI2) é unha proteína que nos humanos está codificada polo xene TNNI2 do cromosoma 11.[1][2] É unha das tres isoformas da troponina I; as outras dúas son TNNI1 e TNNI3. Esta isoforma exprésase nos músculos esqueléticos de contracción rápida nos adultos. Tamén se atopou na cartilaxe, epitelio corneal e glándula mamaria, e nos ratos atopouse no músculo liso vascular.[2] Únese á actina dos filamentos finos musculares mantendo inhibida a contracción muscular (cando o calcio se une á troponina C esta inhibición desaparece). A troponina é un complexo de tres subunidades: troponina C, I e T.
As mutacións no seu xene dan lugar a miopatía e artrogripose distal de tipo 2B.[2]
Notas
[editar | editar a fonte]- ↑ Tiso N, Rampoldi L, Pallavicini A, Zimbello R, Pandolfo D, Valle G, Lanfranchi G, Danieli GA (Mar 1997). "Fine mapping of five human skeletal muscle genes: alpha-tropomyosin, beta-tropomyosin, troponin-I slow-twitch, troponin-I fast-twitch, and troponin-C fast". Biochem Biophys Res Commun 230 (2): 347–50. PMID 9016781. doi:10.1006/bbrc.1996.5958.
- ↑ 2,0 2,1 2,2 "Entrez Gene: TNNI2 troponin I type 2 (skeletal, fast)".
Véxase tamén
[editar | editar a fonte]Bibliografía
[editar | editar a fonte]- Kinoshita S, Adachi W, Sotozono C; et al. (2001). "Characteristics of the human ocular surface epithelium.". Progress in retinal and eye research 20 (5): 639–73. PMID 11470454. doi:10.1016/S1350-9462(01)00007-6.
- Wade R, Eddy R, Shows TB, Kedes L (1990). "cDNA sequence, tissue-specific expression, and chromosomal mapping of the human slow-twitch skeletal muscle isoform of troponin I.". Genomics 7 (3): 346–57. PMID 2365354. doi:10.1016/0888-7543(90)90168-T.
- Huang TS, Bylund DB, Stull JT, Krebs EG (1974). "The amino acid sequences of the phosphorylated sites in troponin-I from rabbit skeletal muscle.". FEBS Lett. 42 (3): 249–52. PMID 4369265. doi:10.1016/0014-5793(74)80738-6.
- Moir AJ, Ordidge M, Grand RJ; et al. (1983). "Studies of the interaction of troponin I with proteins of the I-filament and calmodulin.". Biochem. J. 209 (2): 417–26. PMC 1154108. PMID 6847627.
- Grand RJ, Levine BA, Perry SV (1982). "Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin.". Biochem. J. 203 (1): 61–8. PMC 1158193. PMID 7103951.
- Chong PC, Hodges RS (1982). "Photochemical cross-linking between rabbit skeletal troponin subunits. Troponin I-troponin T interactions.". J. Biol. Chem. 257 (19): 11667–72. PMID 7118902.
- Zhu L, Perez-Alvarado G, Wade R (1994). "Sequencing of a cDNA encoding the human fast-twitch skeletal muscle isoform of troponin I.". Biochim. Biophys. Acta 1217 (3): 338–40. PMID 8148383. doi:10.1016/0167-4781(94)90297-6.
- Lanfranchi G, Muraro T, Caldara F; et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization.". Genome Res. 6 (1): 35–42. PMID 8681137. doi:10.1101/gr.6.1.35.
- Jha PK, Leavis PC, Sarkar S (1997). "Interaction of deletion mutants of troponins I and T: COOH-terminal truncation of troponin T abolishes troponin I binding and reduces Ca2+ sensitivity of the reconstituted regulatory system.". Biochemistry 35 (51): 16573–80. PMID 8987992. doi:10.1021/bi9622433.
- Stefancsik R, Jha PK, Sarkar S (1998). "Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: potential role for coiled coil interaction.". Proc. Natl. Acad. Sci. U.S.A. 95 (3): 957–62. PMC 18637. PMID 9448267. doi:10.1073/pnas.95.3.957.
- Vassylyev DG, Takeda S, Wakatsuki S; et al. (1998). "Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution.". Proc. Natl. Acad. Sci. U.S.A. 95 (9): 4847–52. PMC 20176. PMID 9560191. doi:10.1073/pnas.95.9.4847.
- Jha PK, Sarkar S (1998). "A recombinant monocysteine mutant (Ser to Cys-155) of fast skeletal troponin T: identification by cross-linking of a domain involved in a physiologically relevant interaction with troponins C and I.". Biochemistry 37 (35): 12253–60. PMID 9724539. doi:10.1021/bi980025z.
- Moses MA, Wiederschain D, Wu I; et al. (1999). "Troponin I is present in human cartilage and inhibits angiogenesis.". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 2645–50. PMC 15822. PMID 10077564. doi:10.1073/pnas.96.6.2645.
- Mullen AJ, Barton PJ (2000). "Structural characterization of the human fast skeletal muscle troponin I gene (TNNI2).". Gene 242 (1–2): 313–20. PMID 10721725. doi:10.1016/S0378-1119(99)00519-3.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241. PMID 12477932. doi:10.1073/pnas.242603899.
- Sung SS, Brassington AM, Grannatt K; et al. (2003). "Mutations in genes encoding fast-twitch contractile proteins cause distal arthrogryposis syndromes". Am. J. Hum. Genet. 72 (3): 681–90. PMC 1180243. PMID 12592607. doi:10.1086/368294.
- Li Q, Liu Y, Shen PY; et al. (2003). "Troponin I binds polycystin-L and inhibits its calcium-induced channel activation". Biochemistry 42 (24): 7618–25. PMID 12809519. doi:10.1021/bi034210a.
- Thijssen VL, Ausma J, Gorza L; et al. (2005). "Troponin I isoform expression in human and experimental atrial fibrillation". Circulation 110 (7): 770–5. PMID 15289369. doi:10.1161/01.CIR.0000138849.03311.C6.