Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PROTEIN-KINASE-C DEPENDENT EFFECTS OF 12(S)-HETE ON ENDOTHELIAL-CELL VITRONECTIN RECEPTOR AND FIBRONECTIN RECEPTOR
Autore:
TANG DG; CHEN YQ; DIGLIO CA; HONN KV;
Indirizzi:
WAYNE STATE UNIV,DEPT RADIAT ONCOL DETROIT MI 48202 WAYNE STATE UNIV,DEPT PATHOL DETROIT MI 48202 WAYNE STATE UNIV,DEPT CHEM DETROIT MI 48202 HARPER GRACE HOSP,GERSHENSON RADIAT ONCOL CTR DETROIT MI 48201
Titolo Testata:
The Journal of cell biology
fascicolo: 3, volume: 121, anno: 1993,
pagine: 689 - 704
SICI:
0021-9525(1993)121:3<689:PDEO1O>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARG-GLY-ASP; PLATELET GLYCOPROTEIN-IIB; EXTRACELLULAR-MATRIX; ADHESION RECEPTORS; INTEGRIN RECEPTOR; ATTACHMENT; MEMBRANE; IIIA; STAUROSPORINE; CYTOSKELETON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
D.G. Tang et al., "PROTEIN-KINASE-C DEPENDENT EFFECTS OF 12(S)-HETE ON ENDOTHELIAL-CELL VITRONECTIN RECEPTOR AND FIBRONECTIN RECEPTOR", The Journal of cell biology, 121(3), 1993, pp. 689-704

Abstract

12(S)-HETE, a lipoxygenase metabolite of arachidonic acid induced a nondestructive and reversible endothelial cell (EC) retraction. 12(S)-HETE induced EC retraction was inhibited by protein kinase C inhibitorscalphostin C and staurosporine but not by the protein kinase A inhibitor H8. The role of EC integrins alphavbeta3 and alpha5beta1 in 12(S)-HETE induced EC retraction was investigated. In confluent EC cultures,alphavbeta3 is localized to focal adhesions at both the cell body andcell-cell borders and is colocalized with vinculin-containing focal adhesions. In contrast, alpha5beta1 is primarily enriched at the cell-cell borders, demonstrating codistribution with cell cortical microfilaments and extracellular fibronectin. Both receptors were functional inmediating cell-cell or cell-matrix interactions based on the observations that specific antibodies inhibited EC adhesion to intact subendothelial matrix and disrupted the monolayer integrity. 12(S)-HETE induced a multistep, temporally defined redistribution of the alphavbeta3-containing focal adhesions, leading to an eventual decrease in alphavbeta3 plaques in the retracted ECs. This effect of 12(S)-HETE was inhibited by calphostin C but not by H8. The alterations of alphavbeta3-containing focal adhesions preceded the development of EC retraction. 12(S)-HETE also enhanced EC alphavbeta3 surface expression as revealed by immunofluorescence, flow cytometry, and digitized image analysis. 12(S)-HETE-induced alphavbeta3 rearrangement (i.e., decreased focal adhesion localization and enhanced surface expression) did not result from altered mRNA transcription (as revealed by semi-quantitative RT-PCR analysis) or protein translation (as revealed by Western blotting). In contrast to its effect on alphavbeta3, 12(S)-HETE did not demonstrate a temporally related, well-defined effect on the distribution pattern andthe surface expression of alpha5beta1, although the cell-cell border staining pattern of alpha5beta1 was disrupted due to EC retraction. Itis concluded that 12(S)-HETE-induced decrease of alphavbeta3 localization to focal adhesions may contribute to the development of EC retraction and that 12(S)-HETE induced increase in alphavbeta3 surface expression may promote adhesion of inflammatory leukocytes as well as tumorcells to endothelium.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 20:02:27