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一种人血小板钙ATP酶的结构、功能及亚细胞定位

Structure, function and subcellular localization of a human platelet Ca2+-ATPase.

作者信息

Dean W L

机构信息

Department of Biochemistry, University of Louisville, Kentucky.

出版信息

Cell Calcium. 1989 Jul;10(5):289-97. doi: 10.1016/0143-4160(89)90055-9.

Abstract

Human platelets contain a Ca2+-ATPase in internal membranes that is essential for Ca2+ homeostasis. This Ca2+ pump has enzymatic properties quite similar to the sarcoplasmic reticulum (SR) Ca2+ pumps. Antibodies against the SR Ca2+ pump crossreact with the human platelet protein. However, the platelet Ca2+-ATPase is approximately 10 kD larger than the SR pumps and exhibits a larger mRNA coding for the protein in a megakaryocyte tumor cell line. In addition, the platelet Ca2+-pump may be localized in specialized internal membrane structures that function in Ca2+ uptake and release. These results suggest that the platelet Ca2+-ATPase may represent a new class of internal membrane Ca2+-pumps.

摘要

人类血小板在内膜中含有一种Ca2+ -ATP酶,它对Ca2+ 稳态至关重要。这种Ca2+ 泵具有与肌浆网(SR)Ca2+ 泵非常相似的酶特性。针对SR Ca2+ 泵的抗体与人类血小板蛋白发生交叉反应。然而,血小板Ca2+ -ATP酶比SR泵大约大10 kD,并且在巨核细胞瘤细胞系中表现出编码该蛋白的更大的mRNA。此外,血小板Ca2+ 泵可能定位于专门的内膜结构中,这些结构在Ca2+ 的摄取和释放中起作用。这些结果表明,血小板Ca2+ -ATP酶可能代表了一类新的内膜Ca2+ 泵。

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