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胰岛素诱导骨骼肌细胞膜中5'-核苷酸酶活性降低。

Insulin-induced decrease in 5'-nucleotidase activity in skeletal muscle membranes.

作者信息

Klip A, Ramlal T, Douen A G, Burdett E, Young D, Cartee G D, Holloszy J O

机构信息

Department of Cell Biology, Hospital for Sick Children, Toronto, Canada.

出版信息

FEBS Lett. 1988 Oct 10;238(2):419-23. doi: 10.1016/0014-5793(88)80524-6.

Abstract

Insulin releases inositol phosphoglycans from myocytes in culture [(1986) Science 233, 967-972], which display insulinomimetic activity. Because 5'-nucleotidase is anchored to the membrane through inositol-containing phospholipid glycans, we investigated whether insulin could release the enzyme from the membrane. Membranes prepared from hindquarter muscles of rats perfused with insulin showed a 23% decrease in 5'-nucleotidase activity. Isolated membranes from muscle exposed to insulin in vitro also showed a small but reproducible decrease (9%) in 5'-nucleotidase activity relative to unexposed controls. Phospholipase C from Staphylococcus aureus released 60% of the membrane-bound 5'-nucleotidase. We propose that insulin may activate an endogenous phospholipase C that cleaves phospholipid-glycan-anchored proteins.

摘要

胰岛素可从培养的心肌细胞中释放出肌醇磷酸聚糖[(1986年)《科学》233卷,967 - 972页],这些肌醇磷酸聚糖具有胰岛素模拟活性。由于5'-核苷酸酶通过含肌醇的磷脂聚糖锚定在膜上,我们研究了胰岛素是否能使该酶从膜上释放。用胰岛素灌注大鼠后肢肌肉制备的膜显示5'-核苷酸酶活性降低了23%。体外暴露于胰岛素的肌肉分离膜相对于未暴露的对照,5'-核苷酸酶活性也出现了小幅度但可重复的降低(9%)。金黄色葡萄球菌的磷脂酶C释放出了60%的膜结合5'-核苷酸酶。我们推测胰岛素可能激活一种内源性磷脂酶C,该酶可切割磷脂聚糖锚定蛋白。

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