Calsequestrin, an intracellular calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a putative laminin-binding protein of the extracellular matrix
- PMID: 2302244
- DOI: 10.1016/0006-291x(90)90895-t
Calsequestrin, an intracellular calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a putative laminin-binding protein of the extracellular matrix
Abstract
Calsequestrin was isolated from chicken fast-twitch skeletal muscle, and partial amino terminal sequence was determined. The sequence (NH2) EEGLNFPTYDGKDRVIDLNE shows high identity with known mammalian calsequestrins contained in the Protein Identification Resource data bank (1). Most importantly, this 20 amino acid sequence shares complete identity with the amino terminus of aspartactin, a putative laminin-binding protein of the extracellular matrix (2, 3). The possible relationship of aspartactin to calsequestrin is discussed.
Similar articles
-
Amino acid sequence of chicken calsequestrin deduced from cDNA: comparison of calsequestrin and aspartactin.Biochem Biophys Res Commun. 1990 Aug 16;170(3):1089-95. doi: 10.1016/0006-291x(90)90504-g. Biochem Biophys Res Commun. 1990. PMID: 2390076
-
Frog cardiac calsequestrin. Identification, characterization, and subcellular distribution in two structurally distinct regions of peripheral sarcoplasmic reticulum in frog ventricular myocardium.Circ Res. 1991 Aug;69(2):344-59. doi: 10.1161/01.res.69.2.344. Circ Res. 1991. PMID: 1860177
-
Protein profiles of sarcoplasmic reticulum from normal and dystrophic mouse muscle.J Neurol Sci. 1986 Feb;72(2-3):159-69. doi: 10.1016/0022-510x(86)90004-3. J Neurol Sci. 1986. PMID: 2940342
-
Sarcoplasmic reticulum calsequestrins: structural and functional properties.Mol Cell Biochem. 1994 Jun 15;135(1):61-70. doi: 10.1007/BF00925961. Mol Cell Biochem. 1994. PMID: 7816057 Review.
-
Control of muscle ryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen.Clin Exp Pharmacol Physiol. 2009 Mar;36(3):340-5. doi: 10.1111/j.1440-1681.2008.05094.x. Clin Exp Pharmacol Physiol. 2009. PMID: 19278523 Review.
Cited by
-
Calsequestrin is a component of smooth muscles: the skeletal- and cardiac-muscle isoforms are both present, although in highly variable amounts and ratios.Biochem J. 1994 Jul 15;301 ( Pt 2)(Pt 2):465-9. doi: 10.1042/bj3010465. Biochem J. 1994. PMID: 8042990 Free PMC article.
-
Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3.Mol Cell Biol. 1995 Oct;15(10):5470-81. doi: 10.1128/MCB.15.10.5470. Mol Cell Biol. 1995. PMID: 7565698 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases