FEBS Letters | |
Specific binding of CAP‐50 to calcyclin | |
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
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