Work

Fas activation opposes PMA-stimulated changes in the localization of PKCδ: a mechanism for reducing neutrophil adhesion to endothelial cells

Year: 2002

Type: article

Abstract: We have shown previously that Fas activation results in a partial reduction of phorbol 12-myristate 13-acetate (PMA)-stimulated neutrophil adhesion to endothelial cells. The reduction in adhesion precedes early membrane markers of apoptosis and is not associated with any loss of membrane integrity. Rather, Fas activation reduces the PMA-stimulated expression and aggregation of beta2 integrins responsible for endothelial adhesion. A possible signaling mechanism for Fas effects on adhesion is the localization of protein kinase C delta (PKCdelta). Western blot and immunofluorescence studies indicated that 1 h of Fas activation is required to reduce PMA-stimulated translocation of PKCdelta to the membrane and adhesion. Rottlerin, a PKCdelta inhibitor, also reduced PMA-induced PKCdelta translocation and adhesion. In contrast, Gö6976, an inhibitor of conventional PKC isotypes, did not affect PMA-stimulated PKCdelta translocation or reduce adhesion. There was no additive effect of Fas activation and rottlerin on reducing adhesion, suggesting that both agents were using a common pathway.

Source: Journal of Leukocyte Biology

DOI: 10.1189/jlb.71.5.863

Authors: Bill Hendey, Chun Liu Zhu, Stephanie Greenstein

Institution: Rush University

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,800