Calcium-dependent translocation of sorcin to membranes: Functional relevance in contractile tissue Journal Article


Authors: Meyers, M. B.; Zamparelli, C.; Verzili, D.; Dicker, A. P.; Blanck, T. J. J.; Chiancone, E.
Article Title: Calcium-dependent translocation of sorcin to membranes: Functional relevance in contractile tissue
Abstract: Sorcin, a 22 kDa calcium binding protein present in abundance in cardiac tissue and in multi-drug resistant cells and previously described as a soluble protein, is now shown to undergo a calcium-dependent translocation process from the cytosol to cellular membranes in both systems. The translocation process takes place also in E. coli BL21 cells that express recombinant sorcin, r-sorcin, and can be exploited in the purification of the protein. Calcium binding to purified r-sorcin occurs at micromolar concentrations of the metal and is accompanied by a conformational change that renders the protein soluble in the non-ionic detergent Triton X-114. This finding suggests that lipids are the target of sorcin on cellular membranes. The possible significance of the calcium-dependent translocation of sorcin in the specialized functions of sorcin-expressing cells is discussed. © 1995.
Keywords: unclassified drug; nonhuman; protein conformation; animal; animal tissue; calcium; animalia; molecular sequence data; escherichia coli; cell membrane; base sequence; calcium binding protein; calcium-binding proteins; dna primers; membrane transport; heart; biological transport; myocardium; multidrug resistance; polyethylene glycols; membrane lipid; drug resistance, multiple; rabbits; detergents; rabbit; oryctolagus cuniculus; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; calcium-dependent membrane association; sorcin
Journal Title: FEBS Letters
Volume: 357
Issue: 3
ISSN: 0014-5793
Publisher: Wiley Blackwell  
Date Published: 1995-01-09
Start Page: 230
End Page: 234
Language: English
DOI: 10.1016/0014-5793(94)01338-2
PUBMED: 7835417
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 28 August 2018 -- Source: Scopus
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  1. Adam P. Dicker
    15 Dicker