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Titolo:
LOCALIZATION AND ACTIVATION OF TYPE-IV COLLAGENASE GELATINASE AT ENDOTHELIAL FOCAL CONTACTS/
Autore:
PARTRIDGE CA; PHILLIPS PG; NIEDBALA MJ; JEFFREY JJ;
Indirizzi:
ALBANY MED COLL,DEPT BIOCHEM & MOL BIOL,A-10,47 NEW SCOTLAND AVE ALBANY NY 12208 STRATTON VET AFFAIRS MED CTR ALBANY NY 12208 BAYER INC W HAVEN CT 06516
Titolo Testata:
American journal of physiology. Lung cellular and molecular physiology
fascicolo: 5, volume: 16, anno: 1997,
pagine: 813 - 822
SICI:
1040-0605(1997)16:5<813:LAAOTC>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATRIX ASSEMBLY SITES; TERMINAL REGION; BINDING-SITE; CELLS; GELATINASE; METALLOPROTEINASE; FIBRONECTIN; FIBROBLASTS; SURFACE; DOMAIN;
Keywords:
METALLOPROTEINASE; EXTRACELLULAR MATRIX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
C.A. Partridge et al., "LOCALIZATION AND ACTIVATION OF TYPE-IV COLLAGENASE GELATINASE AT ENDOTHELIAL FOCAL CONTACTS/", American journal of physiology. Lung cellular and molecular physiology, 16(5), 1997, pp. 813-822

Abstract

The cell-surface localization and site of activation of type IV collagenases/gelatinases (matrix metalloproteinases, MMP) in bovine pulmonary microvascular endothelial (BPMVE) cells was examined. Sucrose density centrifugation of plasma membranes and immunofluorescent staining of whole cells indicated association of 72 kDa (MMP-2) and 96 kDa (MMP-9) type IV collagenase/gelatinases with the plasma membrane. Incubation of the BPMVE cells with rhodaminated MMP-9 demonstrated colocalization with beta(1)-integrin, indicating incorporation into the focal contacts. The focal contacts were extracted with saponin, and associated proteolytic activity was examined by zymography. The focal contacts contained latent MMP-2, and stimulation of the cells with cytochalasin D or with 8-bromoadenosine 3',5'-cyclic monophosphate with 3-isobutyl-1-methylxanthine increased both latent and activated MMP-9 in the focal contacts. Addition of these stimuli in unconditioned culture medium did not produce this effect, indicating that the MMP-9 in focal contact extracts was derived from previously secreted enzyme. The activated metalloproteinase degraded extracellular matrix collagens and was inhibited by 1,10-phenanthroline. These findings indicate that endothelial cells release MMP into the extracellular milieu and then concentrate and activate MMP-9 from medium at the focal contacts.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 13:48:31