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Titolo:
ARG-GLY-ASP PEPTIDE INCREASES ENDOTHELIAL HYDRAULIC CONDUCTIVITY - COMPARISON WITH THROMBIN RESPONSE
Autore:
QIAO RL; YAN WH; LUM H; MALIK AB;
Indirizzi:
RUSH PRESBYTERIAN ST LUKES MED CTR,RUSH MED COLL,DEPT PHARMACOL,2242 W HARRISON ST,SUITE 260 CHICAGO IL 60612 RUSH PRESBYTERIAN ST LUKES MED CTR,RUSH MED COLL,DEPT PHARMACOL CHICAGO IL 60612
Titolo Testata:
American journal of physiology. Cell physiology
fascicolo: 1, volume: 38, anno: 1995,
pagine: 110 - 117
SICI:
0363-6143(1995)38:1<110:APIEHC>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXTRACELLULAR-MATRIX; CELL-ADHESION; BARRIER PROPERTIES; PERMEABILITY; ALBUMIN; VITRONECTIN; MODULATION; INTEGRINS; FLUID; ORGANIZATION;
Keywords:
GRGDSP; GRGESP; EXTRACELLULAR MATRIX; DIBUTYRYL ADENOSINE 3',5'-CYCLIC MONOPHOSPHATE; ALPHA-THROMBIN; INTEGRIN RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
R.L. Qiao et al., "ARG-GLY-ASP PEPTIDE INCREASES ENDOTHELIAL HYDRAULIC CONDUCTIVITY - COMPARISON WITH THROMBIN RESPONSE", American journal of physiology. Cell physiology, 38(1), 1995, pp. 110-117

Abstract

The contribution of integrin receptors to the regulation of endothelial permeability was studied using cultured bovine pulmonary microvascular endothelial cell (BPMVEC) monolayers by the measurement of hydraulic conductivity (L(p)). Treatment of monolayers with a peptide containing the sequence Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP) (0.85 mM) to competefor the RGD sequence of extracellular matrix (ECM) proteins increasedendothelial L(p) threefold, whereas the control peptide Gly-Arg-Gly-Glu-Ser-Pro had no effect on L(p). This action of GRGDSP on L(p) was not significantly altered by dibutyryl adenosine 3',5'-cyclic monophosphate (DBcAMP; 0.5 mM). Endothelial L(p) increased twofold when the monolayers were challenged with a-thrombin (5 x 10(-8) M for 10 min), and this response was completely reversed by DBcAMP. The strength of adhesion of endothelial cells was estimated by evaluating the ability of endothelial cells to remain attached to ECM after treating the monolayers with 0.05% trypsin plus 0.5 mM EDTA. Exposure of the monolayers to either GRGDSP or alpha-thrombin significantly reduced the strength of adhesion to the ECM. DBcAMP prevented the antiadhesive effect of alpha-thrombin but not that of GRGDSP. Treatment of the monolayers with either alpha-thrombin or GRGDSP caused formation of intercellular gaps, but only the thrombin-induced intercellular gaps were accompanied by reorganization of actin filaments. These results indicate that integrin binding to ECM proteins regulates an important determinant of endothelial permeability and that alpha-thrombin and GRGDSP increase endothelial cell monolayer permeability by different mechanisms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:39:59