Caldesmón
Caldesmón 1
| |
| Identificadores | |
| Símbolo | CALD1 ; CDM; H-CAD; HCAD; L-CAD; LCAD; NAG22 |
| Entrez | 800 |
| OMIM | |
| RefSeq | NP_004333 |
| UniProt | Q05682 |
| Outros datos | |
| Locus | Cr. 7 134.43 – 134.66 Mb |
A proteína caldesmón é unha proteína que se une á calmodulina que está codificada nons humanos no xene CALD1 do cromosoma 7.[1][2]
Igual que a calponina ou a troponina, a proteína caldesmón inhibe tonicamente a actividade de ATPase da miosina. Actúa no músculo liso.
É unha proteína que se une á calmodulina e á actina que xoga un papel esencial na regulación da contracción do músculo liso e da motilidade e secreción de células non musculares, xa que se localiza en estruturas subcelulares relacionadas coa motilidade, cambios de forma e exocitose e endocitose.[3] O dominio conservado desta proteína posúe actividades de unión ao Ca++-calmodulina, actina, tropomiosina, miosina, e fosfolípidos. Esta proteína é un potente inhibidor da MgATPase da miosina activada pola actina-tropomiosina, e serve como factor mediador para a inhibición dependente do Ca++ da contracción do músculo liso. O splicing alternativo deste xene dá lugar a múltiples variantes de transcritos que codifican distintas isoformas.[2]
Inmunoquímica editar
En inmunoquímica de diagnóstico, a caldesmón é un marcador para a diferenciación do músculo liso.
Notas editar
- ↑ Novy RE, Lin JL, Lin JJ (Oct 1991). "Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells". J Biol Chem 266 (25): 16917–24. PMID 1885618.
- ↑ 2,0 2,1 "Entrez Gene: CALD1 caldesmon 1".
- ↑ K. Pritchard, C.J. Moody. Caldesmon: A calmodulin — Binding actin — Regulatory protein. Cell Calcium. Volume 7, Issues 5–6, December 1986, Pages 309–327. [1] DOI 10.1016/0143-4160(86)90035-7.
Véxase tamén editar
Bibliografía editar
- Huber PA (1998). "Caldesmon". Int. J. Biochem. Cell Biol. 29 (8–9): 1047–51. PMID 9415999. doi:10.1016/S1357-2725(97)00004-6.
- Gusev NB (2002). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation". Biochemistry Mosc. 66 (10): 1112–21. PMID 11736632. doi:10.1023/A:1012480829618.
- Wang CL (2002). "Caldesmon and smooth-muscle regulation". Cell Biochem. Biophys. 35 (3): 275–88. PMID 11894847. doi:10.1385/CBB:35:3:275.
- Mani RS, McCubbin WD, Kay CM (1992). "Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin". Biochemistry 31 (47): 11896–901. PMID 1445920. doi:10.1021/bi00162a031.
- Hayashi K; Yano H; Hashida T; et al. (1993). "Genomic structure of the human caldesmon gene". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12122–6. PMC 50710. PMID 1465449. doi:10.1073/pnas.89.24.12122.
- Humphrey MB; Herrera-Sosa H; Gonzalez G; et al. (1992). "Cloning of cDNAs encoding human caldesmons". Gene 112 (2): 197–204. PMID 1555769. doi:10.1016/0378-1119(92)90376-Z.
- Adam LP, Gapinski CJ, Hathaway DR (1992). "Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas". FEBS Lett. 302 (3): 223–6. PMID 1601129. doi:10.1016/0014-5793(92)80446-N.
- Horiuchi KY, Chacko S (1989). "Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin". Biochemistry 27 (22): 8388–93. PMID 3242591. doi:10.1021/bi00422a014.
- der Terrossian E, Deprette C, Lebbar I, Cassoly R (1994). "Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane". Eur. J. Biochem. 219 (1–2): 503–11. PMID 8307018. doi:10.1111/j.1432-1033.1994.tb19965.x.
- Surgucheva I, Bryan J (1996). "Over-expression of smooth muscle caldesmon in mouse fibroblasts". Cell Motil. Cytoskeleton 32 (3): 233–43. PMID 8581978. doi:10.1002/cm.970320307.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548. doi:10.1101/gr.6.9.791.
- Graether SP; Heinonen TY; Raharjo WH; et al. (1997). "Tryptophan residues in caldesmon are major determinants for calmodulin binding". Biochemistry 36 (2): 364–9. PMID 9003189. doi:10.1021/bi962008k.
- Wang Z, Danielsen AJ, Maihle NJ, McManus MJ (1999). "Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex". J. Biol. Chem. 274 (47): 33807–13. PMID 10559276. doi:10.1074/jbc.274.47.33807.
- Adam L; Vadlamudi R; Mandal M; et al. (2000). "Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1". J. Biol. Chem. 275 (16): 12041–50. PMID 10766836. doi:10.1074/jbc.275.16.12041.
- Hall SM, Hislop AA, Pierce CM, Haworth SG (2000). "Prenatal origins of human intrapulmonary arteries: formation and smooth muscle maturation". Am. J. Respir. Cell Mol. Biol. 23 (2): 194–203. PMID 10919986. doi:10.1165/ajrcmb.23.2.3975.
- Nimmrich I; Erdmann S; Melchers U; et al. (2000). "Seven genes that are differentially transcribed in colorectal tumor cell lines". Cancer Lett. 160 (1): 37–43. PMID 11098082. doi:10.1016/S0304-3835(00)00553-X.
- Hisaoka M; Wei-Qi S; Jian W; et al. (2003). "Specific but variable expression of h-caldesmon in leiomyosarcomas: an immunohistochemical reassessment of a novel myogenic marker". Appl. Immunohistochem. Mol. Morphol. 9 (4): 302–8. PMID 11759055. doi:10.1097/00022744-200112000-00003.
- Sobue K, Muramoto Y, Fujita M, Kakiuchi S (Sep 1981). "Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin". Proc. Natl. Acad. Sci. U.S.A. 78 (9): 5652–5. PMC 348816. PMID 6946503. doi:10.1073/pnas.78.9.5652.
Ligazóns externas editar
- Caldesmon Medical Subject Headings (MeSH) na Biblioteca Nacional de Medicina dos EUA.