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Titolo:
DISMANTLING CELL-CELL CONTACTS DURING APOPTOSIS IS COUPLED TO A CASPASE-DEPENDENT PROTEOLYTIC CLEAVAGE OF BETA-CATENIN
Autore:
BRANCOLINI C; LAZAREVIC D; RODRIGUEZ J; SCHNEIDER C;
Indirizzi:
CONSORZIO INTERUNIV BIOTECHNOL,LAB NAZL,AREA SCI PK,PADRICIANO 99 I-34142 TRIESTE ITALY CONSORZIO INTERUNIV BIOTECHNOL,LAB NAZL I-34142 TRIESTE ITALY COLD SPRING HARBOR LAB COLD SPRING HARBOR NY 11724 UNIV UDINE,SEZ BIOL,DIPARTIMENTO SCI & TECNOL BIOMED I-33100 UDINE ITALY
Titolo Testata:
The Journal of cell biology
fascicolo: 3, volume: 139, anno: 1997,
pagine: 759 - 771
SICI:
0021-9525(1997)139:3<759:DCCDAI>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEATH GENE CED-3; INTERLEUKIN 1-BETA-CONVERTING ENZYME; BACULOVIRUS P35 PROTEIN; ICE-LIKE PROTEASES; E-CADHERIN; CYSTEINE PROTEASE; ALPHA-CATENIN; IL-1-BETA-CONVERTING ENZYME; ICE/CED-3 PROTEASE; CYTOPLASMIC DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
81
Recensione:
Indirizzi per estratti:
Citazione:
C. Brancolini et al., "DISMANTLING CELL-CELL CONTACTS DURING APOPTOSIS IS COUPLED TO A CASPASE-DEPENDENT PROTEOLYTIC CLEAVAGE OF BETA-CATENIN", The Journal of cell biology, 139(3), 1997, pp. 759-771

Abstract

Cell death by apoptosis is a tightly regulated process that requires coordinated modification in cellular architecture. The caspase protease family has been shown to play a key role in apoptosis. Here we report that specific and ordered changes in the actin cytoskeleton take place during apoptosis. In this context, we have dissected one of the first hallmarks in cell death, represented by the severing of contacts among neighboring cells. More specifically, we provide demonstration forthe mechanism that could contribute to the disassembly of cytoskeletal organization at cell-cell adhesion. In fact, beta-catenin, a known regulator of cell-cell adhesion, is proteolytically processed in different cell types after induction of apoptosis. Caspase-3 (cpp32/apopain/yama) cleaves in vitro translated beta-catenin into a form which is similar in size to that observed in cells undergoing apoptosis. beta-Catenin cleavage, during apoptosis in vivo and after caspase-3 treatment in vitro, removes the amino- and carboxy-terminal regions of the protein. The resulting beta-catenin product is unable to bind alpha-cateninthat is responsible for actin filament binding and organization. Thisevidence indicates that connection with actin filaments organized at cell-cell contacts could be dismantled during apoptosis. Our observations suggest that caspases orchestrate the specific and sequential changes in the actin cytoskeleton occurring during cell death via cleavageof different regulators of the microfilament system.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 12:14:24