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 |