Specific binding of CAP‐50 to calcyclin

FEBS Letters

Mizutani, Akihiro¹  Tokumitsu, Hiroshi¹  Watanabe, Yasuo¹  Hidaka, Hiroyoshi¹  Minami, Hiroyuki¹  Watanabe, Masato¹ 

[1] Department of Pharmacology, Nagoya School of Medicine, Showa-ku, Nagoya 466, Japan

关键词: EF-hand protein;    Calcyclin;    Annexin;    CAP-50;    CAP-50;    calcyclin-associated protein of Mr 50;    000;    W-77;    (S)-p-(2-aminoethyloxy)-N-[2-(4-benzyloxycalbonylpiperazin-yl)-1-(p-methyloxybenzyl)]-N-methylbenzenesulfonamide dihydrochloride;    W-7;    N-(6-aminohexyl)-5-chloro-1-naphtalene-sulfonamide;    W-66;    N-(2-aminoethyl)-N-[2-(4-chlorocinnamylamino)-ethyl]-5-isoquinoline-sulfonamide;    PS;    phosphatidylserine;    DTT;    dithiothreitol;    BPB;    Bromophenol blue;    Tricine;    Tris(hydroxymethyl)methylglycine;   

DOI  :  10.1016/0014-5793(92)80671-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺-binding proteins which have two or four EF-hand structures, by a co-precipitation assay with phospholipid (phosphatidylserine). Among nine Ca²⁺-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 Ca²⁺-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 Ca²⁺/calcyclin.

【 授权许可】

Unknown