Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PROLIDASE ACTIVITY IN FIBROBLASTS IS REGULATED BY INTERACTION OF EXTRACELLULAR-MATRIX WITH CELL-SURFACE INTEGRIN RECEPTORS
Autore:
PALKA JA; PHANG JM;
Indirizzi:
NCI,FREDERICK CANC RES & DEV CTR,LNMR,DIV BASIC SCI,BLDG 560,ROOM 12-91 FREDERICK MD 21702 NCI,FREDERICK CANC RES & DEV CTR,LNMR,DIV BASIC SCI FREDERICK MD 21702
Titolo Testata:
Journal of cellular biochemistry
fascicolo: 2, volume: 67, anno: 1997,
pagine: 166 - 175
SICI:
0730-2312(1997)67:2<166:PAIFIR>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
L-PROLINE; DEFICIENCY; COLLAGEN; PROTEINS; IMINODIPEPTIDURIA; LOCALIZATION; HYDROLYSIS; EXPRESSION; CLEAVAGE; PH;
Keywords:
PROLIDASE; FIBROBLASTS; COLLAGEN; INTEGRINS; EXTRACELLULAR MATRIX-CELL INTERACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Palka e J.M. Phang, "PROLIDASE ACTIVITY IN FIBROBLASTS IS REGULATED BY INTERACTION OF EXTRACELLULAR-MATRIX WITH CELL-SURFACE INTEGRIN RECEPTORS", Journal of cellular biochemistry, 67(2), 1997, pp. 166-175

Abstract

Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides. The enzyme plays an important role in the recycling of proline for collagen synthesis and cell growth. An increase in enzyme activity is correlated with increased rates of collagen turnover indicative of extracellular matrix (ECM) remodeling, but the mechanism linking prolidase activity and ECM is poorly understood. Thus, the effect of ECM-cell interaction on intracellular prolidase activity is of special interest. In cultured human skin fibroblasts, the interaction with ECM and, more specifically, type I collagen mediated by thebeta(1) integrin receptor regulates cellular prolidase activity. Supporting evidence comes from the following observations: 1) in sparse cells with a low amount of ECM collagen or in confluent cells in which ECM collagen was removed by collagenase (but not by trypsin or elastase) treatment, prolidase activity was decreased; 2) this effect was reversed by the addition of type I collagen or beta(1) integrin antibody (agonist for beta(1) integrin receptor); 3) sparse cells (with typically low prolidase activity) showed increased prolidase activity when grown on plates coated with type I collagen or on type IV collagen and laminin, constituents of basement membrane; 4) the relative differences in prolidase activity due to collagenase treatment and subsequent recovery of the activity by beta(1) integrin antibody or type I collagen treatment were accompanied by parallel differences in the amount of theenzyme protein recovered from these cells, as shown by Western immunoblot analysis. Thus, we conclude that prolidase activity responded to ECM metabolism (tissue remodeling) through signals mediated by the integrin receptor. (C) 1997 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 11:56:34