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Titolo:
METALLOPROTEINASE-MEDIATED REGULATION OF L-SELECTIN LEVELS ON LEUKOCYTES
Autore:
PREECE G; MURPHY G; AGER A;
Indirizzi:
NATL INST MED RES,DIV CELLULAR IMMUNOL,RIDGEWAY,MILL HILL LONDON NW7 1AA ENGLAND NATL INST MED RES,DIV CELLULAR IMMUNOL LONDON NW7 1AA ENGLAND STRANGEWAYS RES LAB,DEPT CELL & MOLEC BIOL CAMBRIDGE CB1 4RN ENGLAND
Titolo Testata:
The Journal of biological chemistry
fascicolo: 20, volume: 271, anno: 1996,
pagine: 11634 - 11640
SICI:
0021-9258(1996)271:20<11634:MROLLO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-TERMINAL DOMAIN; PROTEIN-KINASE-C; CELL-SURFACE; CHEMOTACTIC FACTORS; HOMING RECEPTOR; ADHESION; ACTIVATION; LYMPHOCYTES; INHIBITORS; INVIVO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
G. Preece et al., "METALLOPROTEINASE-MEDIATED REGULATION OF L-SELECTIN LEVELS ON LEUKOCYTES", The Journal of biological chemistry, 271(20), 1996, pp. 11634-11640

Abstract

Leucocyte (L)-selectin can be proteolytically cleaved in the membraneproximal extracellular region to yield a soluble fragment that contains the functional lectin and epidermal growth factor domains. A variety of stimuli are known to stimulate L-selectin shedding including chemoattractants, phorbol esters, and L-selectin cross-linking; however, the enzymes that regulate L-selectin expression are not characterized, In this study we have used phorbol ester to stimulate endoproteolytic release of L-selectin and identified a major role for a cell surface metalloproteinase (L-selectin sheddase) in this process. The hydroxamicacid based inhibitor of zinc-dependent matrix metalloproteinases Ro 31-9790 completely prevented shedding of cell surface L-selectin from leucocytes in mouse, rat, and man, L-selectin was susceptible to cleavage by known matrix metalloproteinases. Recombinant human fibroblast collagenase (MMP1) reduced the number of L-selectin-positive lymphocytesto a similar extent as phorbol ester activation, and stromelysin (MMP3) had a partial effect on L-selectin expression, Gelatinases A (MMP2)and B (MMP9) were without effect, Lymphocytes did not express fibroblast collagenase or stromelysin at the cell surface, and tissue inhibitor of metalloproteinases (TIMP) did not affect L-selectin levels, L-selectin sheddase was not detected in media harvested from phorbol esterstimulated lymphocytes and was only able to cleave L selectin in the cis but not the trans configuration. These results suggest that endoproteolytic release of L-selectin from the leucocyte surface is mediatedby a metalloproteinase (L-selectin sheddase), which is distinguishable from known matrix metalloproteinases. Understanding the regulation of L-selectin sheddase will be critical for controlling leucocyte migration from the blood.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:17:27