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本文引用的文献

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ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis.ICE/CED3样蛋白酶作为控制异常凋亡的治疗靶点。
Nat Biotechnol. 1996 Mar;14(3):297-301. doi: 10.1038/nbt0396-297.
2
Activation of protein kinase C delta by the c-Abl tyrosine kinase in response to ionizing radiation.电离辐射诱导下，c-Abl酪氨酸激酶对蛋白激酶Cδ的激活作用。
Oncogene. 1998 Apr 2;16(13):1643-8. doi: 10.1038/sj.onc.1201698.
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DNA-dependent protein kinase: DNA binding and activation in the absence of Ku.DNA依赖蛋白激酶：在无Ku情况下的DNA结合与激活
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4
Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.细胞色素c和dATP依赖的Apaf-1/半胱天冬酶-9复合物的形成启动凋亡蛋白酶级联反应。
Cell. 1997 Nov 14;91(4):479-89. doi: 10.1016/s0092-8674(00)80434-1.
5
Binding of Ku and c-Abl at the kinase homology region of DNA-dependent protein kinase catalytic subunit.Ku与c-Abl在DNA依赖性蛋白激酶催化亚基的激酶同源区域的结合。
J Biol Chem. 1997 Oct 3;272(40):24763-6. doi: 10.1074/jbc.272.40.24763.
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Double strand break repair.双链断裂修复
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Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis.Bcl-xL作为DNA损伤诱导凋亡中胞质细胞色素C积累抑制剂的作用。
Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6939-42. doi: 10.1073/pnas.94.13.6939.
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Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2.半胱天冬酶介导的PAK2激活调控凋亡细胞中的膜及形态变化。
Science. 1997 Jun 6;276(5318):1571-4. doi: 10.1126/science.276.5318.1571.
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Tumor promotion by depleting cells of protein kinase C delta.通过消耗蛋白激酶Cδ细胞进行肿瘤促进
Mol Cell Biol. 1997 Jun;17(6):3418-28. doi: 10.1128/MCB.17.6.3418.
10
Protein kinase C delta inhibits the proliferation of vascular smooth muscle cells by suppressing G1 cyclin expression.蛋白激酶Cδ通过抑制G1期细胞周期蛋白的表达来抑制血管平滑肌细胞的增殖。
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蛋白激酶Cδ使DNA依赖性蛋白激酶失活：对细胞凋亡的影响。

Inactivation of DNA-dependent protein kinase by protein kinase Cdelta: implications for apoptosis.

作者信息

Bharti A, Kraeft S K, Gounder M, Pandey P, Jin S, Yuan Z M, Lees-Miller S P, Weichselbaum R, Weaver D, Chen L B, Kufe D, Kharbanda S

机构信息

Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.

出版信息

Mol Cell Biol. 1998 Nov;18(11):6719-28. doi: 10.1128/MCB.18.11.6719.

DOI:10.1128/MCB.18.11.6719
PMID:9774685
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC109255/
Abstract

Protein kinase Cdelta (PKCdelta) is proteolytically cleaved and activated at the onset of apoptosis induced by DNA-damaging agents, tumor necrosis factor, and anti-Fas antibody. A role for PKCdelta in apoptosis is supported by the finding that overexpression of the catalytic fragment of PKCdelta (PKCdelta CF) in cells is associated with the appearance of certain characteristics of apoptosis. However, the functional relationship between PKCdelta cleavage and induction of apoptosis is unknown. The present studies demonstrate that PKCdelta associates constitutively with the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). The results show that PKCdelta CF phosphorylates DNA-PKcs in vitro. Interaction of DNA-PKcs with PKCdelta CF inhibits the function of DNA-PKcs to form complexes with DNA and to phosphorylate its downstream target, p53. The results also demonstrate that cells deficient in DNA-PK are resistant to apoptosis induced by overexpressing PKCdelta CF. These findings support the hypothesis that functional interactions between PKCdelta and DNA-PK contribute to DNA damage-induced apoptosis.

摘要

蛋白激酶Cδ（PKCδ）在DNA损伤剂、肿瘤坏死因子和抗Fas抗体诱导的细胞凋亡开始时被蛋白水解切割并激活。PKCδ在细胞凋亡中的作用得到了以下发现的支持：在细胞中过表达PKCδ的催化片段（PKCδ CF）与细胞凋亡某些特征的出现有关。然而，PKCδ切割与细胞凋亡诱导之间的功能关系尚不清楚。目前的研究表明，PKCδ与DNA依赖性蛋白激酶催化亚基（DNA-PKcs）组成性结合。结果表明，PKCδ CF在体外可使DNA-PKcs磷酸化。DNA-PKcs与PKCδ CF的相互作用抑制了DNA-PKcs与DNA形成复合物并使其下游靶点p53磷酸化的功能。结果还表明，缺乏DNA-PK的细胞对过表达PKCδ CF诱导的细胞凋亡具有抗性。这些发现支持了以下假设：PKCδ与DNA-PK之间的功能相互作用有助于DNA损伤诱导的细胞凋亡。