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非传统蛋白激酶C亚型在牛脑细胞核中的定位

Localization of non-conventional protein kinase C isoforms in bovine brain cell nuclei.

作者信息

Rosenberger U, Shakibaei M, Buchner K

机构信息

Arbeitsgruppe Neurochemie, Freie Universität Berlin, Federal Republic of Germany.

出版信息

Biochem J. 1995 Jan 1;305 ( Pt 1)(Pt 1):269-75. doi: 10.1042/bj3050269.

DOI:10.1042/bj3050269
PMID:7826340
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1136459/
Abstract

Using Western blotting and immunofluorescence microscopy we detected the protein kinase C isoforms delta, epsilon and zeta in isolated cell nuclei from bovine cerebral cortex. Both protein kinase C (PKC) delta and PKC epsilon are present in higher concentrations in neuronal than in glial nuclei and are located inside the nucleus and at the nuclear envelope. There they give a punctate staining in immunofluorescence microscopy. PKC zeta is also present both in the nucleoplasm and at the nuclear envelope. PKC eta could not be detected in the cell nuclei and, even in the homogenate of cerebral cortex, this isoform is present only in very low concentrations. The antibody against PKC eta bound strongly to a nucleoplasmic protein with an apparent molecular mass of 99 kDa. The localization of non-conventional PKC isoforms at the cell nucleus strongly indicates that these isoforms are directly involved in the regulation of nuclear processes.

摘要

利用蛋白质印迹法和免疫荧光显微镜技术,我们在牛大脑皮层分离出的细胞核中检测到了蛋白激酶C亚型δ、ε和ζ。蛋白激酶C(PKC)δ和PKCε在神经元细胞核中的浓度高于胶质细胞核,且位于细胞核内部和核膜处。在免疫荧光显微镜下,它们呈现出点状染色。PKCζ也存在于核质和核膜中。在细胞核中未检测到PKCη,即使在大脑皮层匀浆中,这种亚型的含量也非常低。抗PKCη抗体与一种表观分子量为99 kDa的核质蛋白强烈结合。非常规PKC亚型在细胞核中的定位强烈表明,这些亚型直接参与了核过程的调控。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/03ff2c8348b7/biochemj00072-0270-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/c8958bb91732/biochemj00072-0267-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/48b2fd458739/biochemj00072-0267-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/baa0999c5688/biochemj00072-0268-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/bce9ca9bc843/biochemj00072-0269-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/03ff2c8348b7/biochemj00072-0270-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/c8958bb91732/biochemj00072-0267-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/48b2fd458739/biochemj00072-0267-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/baa0999c5688/biochemj00072-0268-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/bce9ca9bc843/biochemj00072-0269-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e0df/1136459/03ff2c8348b7/biochemj00072-0270-a.jpg

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Protein kinase C isoenzymes: divergence in signal transduction?蛋白激酶C同工酶:信号转导中的差异?
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Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. Potential role of PKC in nuclear lamina structural dynamics.
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