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Titolo:
CASPASES - THE EXECUTIONERS OF APOPTOSIS
Autore:
COHEN GM;
Indirizzi:
UNIV LEICESTER,MRC,TOXICOL UNIT,POB 138,HODGKIN BLDG LEICESTER LE1 9HN LEICS ENGLAND
Titolo Testata:
Biochemical journal
, volume: 326, anno: 1997,
parte:, 1
pagine: 1 - 16
SICI:
0264-6021(1997)326:<1:C-TEOA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERLEUKIN-1-BETA CONVERTING-ENZYME; PROGRAMMED CELL-DEATH; BACULOVIRUS P35 PROTEIN; FAS-MEDIATED APOPTOSIS; ICE-LIKE PROTEASES; IL-1-BETA-CONVERTING ENZYME; POLY(ADP-RIBOSE) POLYMERASE; EPITHELIAL-CELLS; GENE CED-3; IN-VITRO;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
158
Recensione:
Indirizzi per estratti:
Citazione:
G.M. Cohen, "CASPASES - THE EXECUTIONERS OF APOPTOSIS", Biochemical journal, 326, 1997, pp. 1-16

Abstract

Apoptosis is a major form of cell death, characterized initially by aseries of stereotypic morphological changes. In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the recognition that CED-3 has sequence identity with the mammalian cysteine protease interleukin-Ip-converting enzyme (ICE), a family of at least 10 related cysteine proteases has been identified. These proteins are characterized by almost absolute specificity for aspartic acid in the P-1 position. All the caspases (ICE-like proteases) contain a conserved QACXG (where X is R, Q or G) pentapeptide active-site motif. Caspases are synthesized as inactive proenzymes comprising an N-terminal peptide (prodomain) together with one largeand one small subunit. The crystal structures of both caspase-1 and caspase-3 show that the active enzyme is a heterotetramer, containing two small and two large subunits, Activation of caspases during apoptosis results in the cleavage of critical cellular substrates, including poly(ADP-ribose) polymerase and lamins, so precipitating the dramatic morphological changes of apoptosis. Apoptosis induced by CD95 (Fas/APO-1) and tumour necrosis factor activates caspase-8 (MACH/FLICE/Mch5), which contains an N-terminus with FADD (Fas-associating protein with death domain)-like death effector domains, so providing a direct link between cell death receptors and the caspases. The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of caspase-2 and recruits it to the signalling complex. Cells undergoing apoptosis following triggering of death receptors execute the death programme by activating a hierarchy of caspases,with caspase-8 and possibly caspase-10 being at or near the apex of this apoptotic cascade.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 16:31:26