PURIFICATION AND CHARACTERIZATION OF A NOVEL CALCIUM-BINDING PROTEIN, S100C, FROM PORCINE HEART

被引：57

作者：

NAKA, M ^{[1
]}

QING, ZX ^{[1
]}

SASAKI, T ^{[1
]}

KISE, H ^{[1
]}

TAWARA, I ^{[1
]}

HAMAGUCHI, S ^{[1
]}

TANAKA, T ^{[1
]}

机构：

[1] MIE UNIV,SCH MED,DEPT MOLEC & CELLULAR PHARMACOL,TSU,MIE 514,JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 1994年 / 1223卷 / 03期

关键词：

S100C; CYTOSKELETON; ANNEXIN I; CALCIUM-BINDING PROTEIN; PROTEIN KINASE C; AFFINITY CHROMATOGRAPHY;

D O I：

10.1016/0167-4889(94)90094-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel Ca2+-binding protein, which we have named S100C (Ohta et al. (1991) FEBS Lett. 295, 93-96), was purified to homogeneity from porcine heart by Ca2+-dependent dye-affinity chromatography. S100C possesses some properties of S100 proteins, such as self-association and exposure of a hydrophobic site upon binding of Ca2+ but it differs from S100 proteins in forms of its isoelectric point (pI = 6.2), cross-reactivity with antibodies, staining by Stains-all, and its Ca2+-dependent interaction with the immobilized dye. S100C bound to cytoskeletal components at physiological concentrations of Ca2+. Moreover, it was found that I-125-labeled S100C interacted with annexin I in a Ca2+-dependent manner. S100C also inhibited the phosphorylation of annexin I by protein kinase C. These data suggest that S100C might act to regulate the cytoskeleton in a Ca2+-dependent manner via interactions with annexin I.

引用

页码：348 / 353

页数：6

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