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Titolo:
DISSECTION OF PATHWAYS LEADING TO ANTIGEN RECEPTOR-INDUCED AND FAS CD95-INDUCED APOPTOSIS IN HUMAN B-CELLS/
Autore:
LENS SMA; DENDRIJVER BFA; POTGENS AJG; TESSELAAR K; VANOERS MHJ; VANLIER RAW;
Indirizzi:
NETHERLANDS RED CROSS,BLOOD TRANSFUS SERV,CENT LAB,DEPT CLIN VIROIMMUNOL,PLESMANLAAN 125 NL-1066 CX AMSTERDAM NETHERLANDS NETHERLANDS RED CROSS,BLOOD TRANSFUS SERV,CENT LAB,DEPT EXPT IMMUNOHAEMATOL NL-1066 CX AMSTERDAM NETHERLANDS UNIV AMSTERDAM,ACAD MED CTR,EXPT & CLIN IMMUNOL LAB NL-1105 AZ AMSTERDAM NETHERLANDS UNIV AMSTERDAM,ACAD MED CTR,DEPT HEMATOL NL-1105 AZ AMSTERDAM NETHERLANDS
Titolo Testata:
The Journal of immunology
fascicolo: 12, volume: 160, anno: 1998,
pagine: 6083 - 6092
SICI:
0022-1767(1998)160:12<6083:DOPLTA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
FAS-MEDIATED APOPTOSIS; CRMA-INHIBITABLE PROTEASE; ENZYME-LIKE PROTEASE; T-CELL; DEATH DOMAIN; LYMPHOPROLIFERATIVE SYNDROME; ICE/CED-3 PROTEASE; SIGNALING COMPLEX; COMMON MEDIATOR; CD95 FAS/APO-1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
S.M.A. Lens et al., "DISSECTION OF PATHWAYS LEADING TO ANTIGEN RECEPTOR-INDUCED AND FAS CD95-INDUCED APOPTOSIS IN HUMAN B-CELLS/", The Journal of immunology, 160(12), 1998, pp. 6083-6092

Abstract

To dissect intracellular pathways involved in B cell Ag receptor (BCR)-mediated and Fas-induced human B cell death, we isolated clones of the Burkitt lymphoma cell line Ramos with different apoptosis sensitivities, Selection for sensitivity to Fas-induced apoptosis also selectedfor clones with enhanced BCR death sensitivity and vice versa. In contrast, clones resistant to Fas-mediated apoptosis could still undergo BCR-induced cell death. Based on the functional phenotypes of these clones, we hypothesized that both receptor-induced apoptosis pathways are initially distinct but may eventually converge. Indeed, ligation of both Fas and BCR resulted in cleavage of the IL-1 beta-converting enzyme/Ced-3-like protease caspase 3 and its substrates Ac-Asp-Glu-Val-Asp-aldehyde and poly(ADP-ribose) polymerase, Markedly, qualitative differences in the caspase 3 cleavage pattern induced by Fas or BCR ligation were observed; whereas Fas ligation generated caspase 3 cleavage products of 19/20 and 17 kDa, only the latter cleavage product was found upon BCR cross-linking. The caspase inhibitor Val-Ala-Asp-fluoromethylketone blocked both Fas-and BCR-mediated apoptosis, but differentiallyaffected caspase 3 cleavage induced by either stimulus. Finally, overexpression of a Fas-associated death domain (FADD) dominant-negative mutant protein was found to inhibit Fas-induced apoptosis but not BCR-induced apoptosis, Together our findings imply that Fas and BCR couple,via FADD-dependent and FADD-independent mechanisms, respectively, to distinct proteases upstream of caspase 3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 19:14:14