Apoptosis - Condensed matter in cell death

被引：102

作者：

Zamzami, N ^{[1
]}

Kroemer, G ^{[1
]}

机构：

[1] Natl League Canc, CNRS, ERS1984, Apoptosis Canc & Immun Lab, F-94801 Villejuif, France

来源：

NATURE | 1999年 / 401卷 / 6749期

关键词：

D O I：

10.1038/43591

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

During programmed cell death (apoptosis), the doomed cell shrinks and is engulfed by its neighbours. Part of this process involves destruction of the nucleus. A factor involved in nuclear destruction has now been identified. Known as Acinus, it adds an extra level of complexity to what we know about digestion of nuclear DNA, because it seems to act without a DNA-digesting (DNase) activity.

引用

页码：127 / 128

页数：2

共 12 条

[1] CXCR4 and CD4 mediate a rapid CD95-independent cell death in CD4+ T cells [J].

Berndt, C ;

Möpps, B ;

Angermüller, S ;

Gierschik, P ;

Krammer, PH .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (21) :12556-12561

[2] A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD [J].

Enari, M ;

Sakahira, H ;

Yokoyama, H ;

Okawa, K ;

Iwamatsu, A ;

Nagata, S .

NATURE, 1998, 391 (6662) :43-50

[3] Molecular cloning and characterization of human caspase-activated DNase [J].

Mukae, N ;

Enari, M ;

Sakahira, H ;

Fukuda, Y ;

Inazawa, J ;

Toh, H ;

Nagata, S .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (16) :9123-9128

[4] PML induces a novel caspase-independent death process [J].

Quignon, F ;

De Bels, F ;

Koken, M ;

Feunteun, J ;

Ameisen, JC ;

de Thé, H .

NATURE GENETICS, 1998, 20 (03) :259-265

[5] Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation [J].

Sahara, S ;

Aoto, M ;

Eguchi, Y ;

Imamoto, N ;

Yoneda, Y ;

Tsujimoto, Y .

NATURE, 1999, 401 (6749) :168-173

[6] Apoptotic nuclear morphological change without DNA fragmentation [J].

Sakahira, H ;

Enari, M ;

Ohsawa, Y ;

Uchiyama, Y ;

Nagata, S .

CURRENT BIOLOGY, 1999, 9 (10) :543-546

[7] Transition from caspase-dependent to caspase-independent mechanisms at the onset of apoptotic execution [J].

Samejima, K ;

Toné, S ;

Kottke, TJ ;

Enari, M ;

Sakahira, H ;

Cooke, CA ;

Durrieu, F ;

Martins, LM ;

Nagata, S ;

Kaufmann, SH ;

Earnshaw, WC .

JOURNAL OF CELL BIOLOGY, 1998, 143 (01) :225-239

[8] Molecular characterization of mitochondrial apoptosis-inducing factor [J].

Susin, SA ;

Lorenzo, HK ;

Zamzami, N ;

Marzo, I ;

Snow, BE ;

Brothers, GM ;

Mangion, J ;

Jacotot, E ;

Costantini, P ;

Loeffler, M ;

Larochette, N ;

Goodlett, DR ;

Aebersold, R ;

Siderovski, DP ;

Penninger, JM ;

Kroemer, G .

NATURE, 1999, 397 (6718) :441-446

[9] L-DNase II, a molecule that links proteases and endonucleases in apoptosis, derives from the ubiquitous serpin leukocyte elastase inhibitor [J].

Torriglia, A ;

Perani, P ;

Brossas, JY ;

Chaudun, E ;

Treton, J ;

Courtois, Y ;

Counis, MF .

MOLECULAR AND CELLULAR BIOLOGY, 1998, 18 (06) :3612-3619

[10] Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity [J].

Vancompernolle, K ;

Van Herreweghe, F ;

Pynaert, G ;

Van de Craen, M ;

De Vos, K ;

Totty, N ;

Sterling, A ;

Fiers, W ;

Vandenabeele, P ;

Grooten, J .

FEBS LETTERS, 1998, 438 (03) :150-158

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