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2
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本文引用的文献

1
A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform.分辨率为12.8埃的人类凋亡小体结构为这个细胞死亡平台提供了深入见解。
Structure. 2005 Nov;13(11):1725-35. doi: 10.1016/j.str.2005.09.006.
2
Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation.构建二聚体半胱天冬酶-9：对半胱天冬酶激活的诱导邻近模型的重新评估。
PLoS Biol. 2005 Jun;3(6):e183. doi: 10.1371/journal.pbio.0030183. Epub 2005 May 10.
3
Molecular mechanisms of caspase regulation during apoptosis.细胞凋亡过程中半胱天冬酶调节的分子机制。
Nat Rev Mol Cell Biol. 2004 Nov;5(11):897-907. doi: 10.1038/nrm1496.
4
Caspase activation: revisiting the induced proximity model.半胱天冬酶激活：重新审视诱导邻近模型。
Cell. 2004 Jun 25;117(7):855-8. doi: 10.1016/j.cell.2004.06.007.
5
Cell death: critical control points.细胞死亡：关键控制点。
Cell. 2004 Jan 23;116(2):205-19. doi: 10.1016/s0092-8674(04)00046-7.
6
The CD95(APO-1/Fas) DISC and beyond.CD95（APO-1/Fas）死亡诱导信号复合物及其他相关内容。
Cell Death Differ. 2003 Jan;10(1):26-35. doi: 10.1038/sj.cdd.4401186.
7
Insights into the regulatory mechanism for caspase-8 activation.对半胱天冬酶-8激活调控机制的见解。
Mol Cell. 2003 Feb;11(2):543-9. doi: 10.1016/s1097-2765(03)00059-5.
8
A unified model for apical caspase activation.顶端半胱天冬酶激活的统一模型。
Mol Cell. 2003 Feb;11(2):529-41. doi: 10.1016/s1097-2765(03)00051-0.
9
Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP.半胱天冬酶-3和X连锁凋亡抑制蛋白对凋亡蛋白酶激活因子-1/半胱天冬酶-9凋亡小体的调控
J Biol Chem. 2003 Mar 7;278(10):8091-8. doi: 10.1074/jbc.M204783200. Epub 2002 Dec 27.
10
Caspases and apoptosis.半胱天冬酶与细胞凋亡
Essays Biochem. 2002;38:9-19. doi: 10.1042/bse0380009.

半胱天冬酶-9全酶是一种特异性且最佳的半胱天冬酶-3加工机器。

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

作者信息

Yin Qian, Park Hyun Ho, Chung Jee Y, Lin Su-Chang, Lo Yu-Chih, da Graca Li S, Jiang Xuejun, Wu Hao

机构信息

Department of Biochemistry, Weill Medical College of Cornell University, New York, New York 10021, USA.

出版信息

Mol Cell. 2006 Apr 21;22(2):259-68. doi: 10.1016/j.molcel.2006.03.030.

DOI:10.1016/j.molcel.2006.03.030
PMID:16630893
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2904439/
Abstract

Caspase-9 activation is critical for intrinsic cell death. The activity of caspase-9 is increased dramatically upon association with the apoptosome, and the apoptosome bound caspase-9 is the caspase-9 holoenzyme (C9Holo). In this study, we use quantitative enzymatic assays to fully characterize C9Holo and a leucine-zipper-linked dimeric caspase-9 (LZ-C9). We surprisingly show that LZ-C9 is more active than C9Holo for the optimal caspase-9 peptide substrate LEHD-AFC but is much less active than C9Holo for the physiological substrate procaspase-3. The measured Km values of C9Holo and LZ-C9 for LEHD-AFC are similar, demonstrating that dimerization is sufficient for catalytic activation of caspase-9. The lower activity of C9Holo against LEHD-AFC may be attributed to incomplete C9Holo assembly. However, the measured Km of C9Holo for procaspase-3 is much lower than that of LZ-C9. Therefore, in addition to dimerization, the apoptosome activates caspase-9 by enhancing its affinity for procaspase-3, which is important for procaspase-3 activation at the physiological concentration.

摘要

半胱天冬酶-9的激活对于细胞内源性死亡至关重要。半胱天冬酶-9与凋亡小体结合后活性会显著增加，与凋亡小体结合的半胱天冬酶-9即为半胱天冬酶-9全酶（C9Holo）。在本研究中，我们使用定量酶促测定法全面表征了C9Holo和一种亮氨酸拉链连接的二聚体半胱天冬酶-9（LZ-C9）。我们惊人地发现，对于最佳的半胱天冬酶-9肽底物LEHD-AFC，LZ-C9比C9Holo更具活性，但对于生理底物procaspase-3，LZ-C9的活性远低于C9Holo。C9Holo和LZ-C9对LEHD-AFC的测得Km值相似，表明二聚化足以实现半胱天冬酶-9的催化激活。C9Holo对LEHD-AFC活性较低可能归因于C9Holo组装不完全。然而，C9Holo对procaspase-3的测得Km远低于LZ-C9。因此，除了二聚化之外，凋亡小体通过增强半胱天冬酶-9对procaspase-3的亲和力来激活半胱天冬酶-9，这对于在生理浓度下激活procaspase-3很重要。