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Activation of acetyl-CoA carboxylase by a glutamate- and magnesium-sensitive protein phosphatase in the isletβ-cell

机译:胰岛β细胞中谷氨酸和镁敏感蛋白磷酸酶激活乙酰辅酶A羧化酶

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摘要

Acetyl-CoA carboxylase(ACC)catalyzes the formation of malonyl-CoA, a precursor in the biosynthesis of long- chain fatty acids, which have been implicated in phys- iological insulin secretion. The catalytic function of ACC is regulated by phosphorylation(inactive)-de- Phosphorylation(active). In this study we investigated Whether similar regulatory mechanisms exist for ACC in The pancreatic isletβ-cell. ACC was quantitated in nor- Mal rat islets, human islets, and clonalβ-cells(HIT-15 Or INS-1)using a[~14C]bicarbonate fixation assay.
机译:乙酰辅酶A羧化酶(ACC)催化丙二酰辅酶A的形成,丙二酰辅酶A是长链脂肪酸生物合成中的前体,长链脂肪酸与生理胰岛素的分泌有关。 ACC的催化功能受磷酸化(非活性)-去磷酸化(活性)的调节。在这项研究中,我们调查了胰腺胰岛β细胞中是否存在类似的ACC调节机制。使用[〜14C]碳酸氢盐固定测定法对正常的大鼠胰岛,人胰岛和克隆β细胞(HIT-15或INS-1)中的ACC进行了定量。

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