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Specific binding of CAP‐50 to calcyclin
Author(s) -
Minami Hiroyuki,
Tokumitsu Hiroshi,
Mizutani Akihiro,
Watanabe Yasuo,
Watanabe Masato,
Hidaka Hiroyoshi
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80671-3
Subject(s) - chemistry , annexin , calcium binding protein , calmodulin , phosphatidylserine , binding protein , biochemistry , ef hand , plasma protein binding , function (biology) , biophysics , phospholipid , microbiology and biotechnology , calcium , biology , in vitro , membrane , enzyme , organic chemistry , gene
CAP‐50, a calcyclin‐associated protein with an apparent molecular mass or 50 kDa, was purified and proved to be a novel annexin [Tokumitsu, H. et al. (1992) J. Biol. Chem. 267, 8919–8924]. We examined the binding of CAP‐50 to other Ca 2+ ‐binding proteins which have two or four EF‐hand structures, by a co‐precipitation assay with phospholipid (phosphatidylserine). Among nine Ca 2+ ‐binding proteins (calcyclin, S‐100 proteins, p11, calgizzarin, calvasculin, calmodulin and troponin C) examined, only calcyclin interacted with CAP‐50. These results clearly show that the interaction of CAP‐50 to calcyclin is specific, i.e. other Ca 2+ ‐binding proteins with the EF‐hand structure could not substitute for calcyclin, thereby suggesting the possible role in specific regulation of the function of CAP‐50 by Ca 2+ /calcyclin.