Caspase-2: controversial killer or checkpoint controller?

被引：37

作者：

Kitevska, Tanja ^{[1
]}

Spencer, Damian M. S. ^{[1
]}

Hawkins, Christine J. ^{[1
,2
]}

机构：

[1] La Trobe Univ, Dept Biochem, Bundoora, Vic 3086, Australia

[2] Royal Childrens Hosp, Childrens Canc Ctr, Murdoch Childrens Res Inst, Parkville, Vic 3052, Australia

来源：

APOPTOSIS | 2009年 / 14卷 / 07期

基金：

英国医学研究理事会;

关键词：

Caspase; Protease; Apoptosis; Splicing; PIDDosome; Activation; ENDOPLASMIC-RETICULUM STRESS; PROGRAMMED CELL-DEATH; CYTOCHROME-C RELEASE; ACUTE LYMPHOBLASTIC-LEUKEMIA; INTERACTING PROTEIN RIP; INDUCED APOPTOSIS; DNA-DAMAGE; IN-VITRO; HUNTINGTONS-DISEASE; NUCLEAR-BODIES;

D O I：

10.1007/s10495-009-0365-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The caspases are an evolutionarily conserved family of cysteine proteases, with essential roles in apoptosis or inflammation. Caspase-2 was the second caspase to be cloned and it resembles the prototypical nematode caspase CED-3 more closely than any other mammalian protein. An absence of caspase-2-specific reagents and the subtle phenotype of caspase-2-deficient mice have hampered definition of the physiological role of caspase-2 and identification of factors regulating its activity. Although some data implicate caspase-2 in apoptotic pathways, a link with apoptosis has been less firmly established for caspase-2 than for some other caspases. Emerging evidence suggests that caspase-2 regulates the cell cycle and may act as a tumour suppressor. This article critically reviews the current state of knowledge regarding the biochemistry and biology of this controversial caspase.

引用

页码：829 / 848

页数：20

共 183 条

[1] Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation [J].

Acehan, D ;

Jiang, XJ ;

Morgan, DG ;

Heuser, JE ;

Wang, XD ;

Akey, CW .

MOLECULAR CELL, 2002, 9 (02) :423-432

[2]

Ahmad M, 1997, CANCER RES, V57, P615

[3] Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases [J].

Aho, S .

EXPERIMENTAL DERMATOLOGY, 2004, 13 (11) :700-707

[4] Dissecting processing and apoptotic activity of a cysteine protease by mutant analysis [J].

Allet, B ;

Hochmann, A ;

Martinou, I ;

Berger, A ;

Missotten, M ;

Antonsson, B ;

Sadoul, R ;

Martinou, JC ;

Bernasconi, L .

JOURNAL OF CELL BIOLOGY, 1996, 135 (02) :479-486

[5] Human ICE/CED-3 protease nomenclature [J].

Alnemri, ES ;

Livingston, DJ ;

Nicholson, DW ;

Salvesen, G ;

Thornberry, NA ;

Wong, WW ;

Yuan, JY .

CELL, 1996, 87 (02) :171-171

[6] Protein database searches using compositionally adjusted substitution matrices [J].

Altschul, SF ;

Wootton, JC ;

Gertz, EM ;

Agarwala, R ;

Morgulis, A ;

Schäffer, AA ;

Yu, YK .

FEBS JOURNAL, 2005, 272 (20) :5101-5109

[7] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].

Altschul, SF ;

Madden, TL ;

Schaffer, AA ;

Zhang, JH ;

Zhang, Z ;

Miller, W ;

Lipman, DJ .

NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402

[8] The biochemical mechanism of caspase-2 activation [J].

Baliga, BC ;

Read, SH ;

Kumar, S .

CELL DEATH AND DIFFERENTIATION, 2004, 11 (11) :1234-1241

[9] Role of prodomain in importin-mediated nuclear localization and activation of caspase-2 [J].

Baliga, BC ;

Colussi, PA ;

Read, SH ;

Dias, MM ;

Jans, DA ;

Kumar, S .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (07) :4899-4905

[10] Apoptosome: a platform for the activation of initiator caspases [J].

Bao, Q. ;

Shi, Y. .

CELL DEATH AND DIFFERENTIATION, 2007, 14 (01) :56-65

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