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首页> 外文期刊>Biochemistry >Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein.
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Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein.

机译：Copine的生化特性：一种普遍存在的Ca2 +依赖性磷脂结合蛋白。

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The copines are a novel group of Ca(2+)-dependent, phospholipid-binding proteins first isolated from Paramecium tetraurelia [Creutz, C. E., et al. (1998) J. Biol. Chem. 273, 1393-1402] and found in a wide range of organisms, from plants to humans. They have a Ca(2+) and phospholipid-binding domain consisting of two C2 domains and a core domain in the C-terminal portion that is homologous to the A domain found in certain integrins. We provide here the first description of the properties and distribution of a native mammalian copine, copine I. This protein is expressed in all major adult rat organs as demonstrated by probing Western blots of rat organ homogenates with anticopine antibodies. The highest levels of copine are found in the spleen. A protocol for purifying copine to homogeneity from bovine spleen is described. Purified native copine is a 58 kDa monomer that exhibits Ca(2+) self-association to form higher-order multimers, and Ca(2+)-dependent, phospholipid binding activity with preference for negatively charged phospholipids over neutral phospholipids and selectivity for Ca(2+) over Mg(2+). Half-maximal association with vesicles enriched in phosphatidylserine occurs at Ca(2+) concentrations between 1 and 10 microM. Copine I exhibits Mn(2+) binding activity that is strongly competed by Mg(2+) and partially competed by Ca(2+), suggesting that the copine I A domain may be a functional MIDAS metal binding site similar to that found in integrins [Lee, J. O., et al. (1995) Cell 80, 631-638]. Roles for copine in binding membranes and target proteins or small molecules are discussed.
机译：copines是一组新的Ca（2+）依赖性磷脂结合蛋白，它们首先从四草​​履虫中分离[Creutz，C.E。等人。 （1998）生物化学杂志。化学273，1393-1402]，并发现了从植物到人类的各种生物。它们具有由两个C2结构域和在C末端部分的核心结构域组成的Ca（2+）和磷脂结合结构域，该核心结构域与某些整联蛋白中的A结构域同源。我们在这里提供了天然哺乳动物copine Copine I的特性和分布的第一个描述。该蛋白在所有主要成年大鼠器官中都有表达，这是通过用抗copine抗体探测大鼠器官匀浆的Western印迹证明的。在脾脏中发现了最高水平的copine。描述了从牛脾中纯化copine至同质的方案。纯化的天然copine是58 kDa单体，表现出Ca（2+）自缔合以形成更高阶的多聚体，以及Ca（2+）依赖的磷脂结合活性，与中性磷脂相比，带负电的磷脂优先，对Ca的选择性更高（2+）超过Mg（2+）。在Ca（2+）浓度介于1和10 microM之间发生与富含磷脂酰丝氨酸的囊泡的半最大关联。 Copine I表现出由Mg（2+）强烈竞争而Ca（2+）部分竞争的Mn（2+）结合活性，表明Copine IA域可能是类似于整合素中发现的功能性MIDAS金属结合位点[李，乔，等。 （1995）Cell 80，631-638]。讨论了copine在结合膜和靶蛋白或小分子中的作用。

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