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Titolo:
PECAM-1 shedding during apoptosis generates a membrane-anchored truncated molecule with unique signaling characteristics
Autore:
Ilan, N; Mohsenin, A; Cheung, L; Madri, JA;
Indirizzi:
Yale Univ, Sch Med, Dept Pathol, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 ed, Dept Pathol, New Haven, CT 06520 USA
Titolo Testata:
FASEB JOURNAL
fascicolo: 2, volume: 15, anno: 2001,
pagine: 362 - 372
SICI:
0892-6638(200102)15:2<362:PSDAGA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION MOLECULE-1; ENDOTHELIAL GROWTH-FACTOR; RECEPTOR TYROSINE KINASE; MIGRATION IN-VITRO; BETA-CATENIN; TRANSENDOTHELIAL MIGRATION; EXTRACELLULAR-MATRIX; ECTODOMAIN CLEAVAGE; SURVIVAL FACTOR; CYCLIN D1;
Keywords:
platelet-endothelial cell adhesion molecule (CD31); endothelium; apoptosis; shedding; cleavage;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Madri, JA Yale Univ, Sch Med, Dept Pathol, 310 Cedar St,POB 208023, New Haven, CT 06520 USA Yale Univ 310 Cedar St,POB 208023 New Haven CT USA 06520 520 USA
Citazione:
N. Ilan et al., "PECAM-1 shedding during apoptosis generates a membrane-anchored truncated molecule with unique signaling characteristics", FASEB J, 15(2), 2001, pp. 362-372

Abstract

Shedding of cell surface molecules, including growth factor receptors, provides a mechanism by which cells regulate signal transduction events. Here we show that platelet-endothelial cell adhesion molecule (PECAM)-1 is shed from the endothelial cell surface during apoptosis and accumulates in the culture medium as a similar to 100 kDa soluble protein. The cleavage mediating the shedding is matrix metalloproteinase (MMP) dependent, as GM6001, a broad-spectrum MMP inhibitor, inhibits PECAM-1 accumulation in the culture medium in a dose-responsive manner. In addition to the 100 kDa soluble fragment, PECAM-1 cleavage generates the formation of a truncated (Tr.) similar to 28 kDa molecule, composed of the transmembrane and the cytoplasmic PECAM-1 domains. Transfections of the full-length (F1) and the Tr. PECAM-1 gene constructs into endothelial and nonendothelial cells were performed. We found 1) significantly more gamma -catenin and SHP-2 bound to the truncated than to the full-length PECAM-1; 2) stable expression of the truncated PECAM-1 in SW480 colon carcinoma cells resulted in a dramatic decrease in cell proliferation, whereas expression of comparable levels of the full-length PECAM-1 had no effect; 3) the decrease observed in cell proliferation is due, in part, to an increase in programmed cell death (apoptosis) and correlatedwith continuous caspase 8 cleavage and p38/JNK phosphorylation. These results support the intimate involvement of PECAM-1 in signal transduction cascades and also suggest that caspase substrates (e.g., PECAM-1) may possess distinct and unique functions on cleavage.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:40:08