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兔壁细胞中主要的钙调蛋白结合蛋白是Ca2+/钙调蛋白依赖性蛋白激酶II。

The major calmodulin-binding protein in rabbit parietal cells is Ca2+/calmodulin-dependent protein kinase II.

作者信息

Funasaka M, Fox L M, Tang L H, Modlin I M, Goldenring J R

机构信息

Department of Surgery, Yale University School of Medicine, New Haven, Connecticut.

出版信息

Biochem Int. 1992 Sep;27(6):1101-9.

PMID:1332720
Abstract

Parietal cell secretion can be stimulated by both histaminergic and cholinergic agonists. We have recently found that inhibition of calmodulin-dependent protein kinase II (CaMK II) activity can abolish cholinergic but not histaminergic stimulation of parietal cell secretion (Am. J. Physiol. 262:G118-122). We have investigated the presence of calmodulin-binding proteins and CaMK II in isolated rabbit parietal cells. Calmodulin-binding proteins with apparent molecular masses of 50, 60, 85, 100, and 240 kDa were observed. The major calmodulin-binding species was a 50 kDa band which was enriched in 50,000 g. microsomal membranes. The 50 kDa calmodulin binding comigrated with immunoreactivity for CaMK II. Partial purification of the microsomal CaMK II demonstrated a 250 kDa oligomer. The results demonstrate that CaMK II is the major calmodulin-binding protein in parietal cells and is associated primarily with light microsomal membranes.

摘要

壁细胞分泌可被组胺能和胆碱能激动剂刺激。我们最近发现,抑制钙调蛋白依赖性蛋白激酶II(CaMK II)活性可消除胆碱能而非组胺能对壁细胞分泌的刺激(《美国生理学杂志》262:G118 - 122)。我们研究了分离的兔壁细胞中钙调蛋白结合蛋白和CaMK II的存在情况。观察到表观分子量为50、60、85、100和240 kDa的钙调蛋白结合蛋白。主要的钙调蛋白结合条带是一条50 kDa的条带,在50,000 g微粒体膜中富集。50 kDa的钙调蛋白结合与CaMK II的免疫反应性共迁移。微粒体CaMK II的部分纯化显示出一个250 kDa的寡聚体。结果表明,CaMK II是壁细胞中主要的钙调蛋白结合蛋白,并且主要与轻微粒体膜相关。

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