GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

TableEdit

Jump to: navigation, search

PMID:17951978

You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki

See Help for Help on this wiki. See the documentation for how to use the table editor

Citation

Ge, X, Low, B, Liang, M and Fu, J (2007) Angiotensin II directly triggers endothelial exocytosis via protein kinase C-dependent protein kinase D2 activation. J. Pharmacol. Sci. 105:168-76

Abstract

Angiotensin II (AII) has been reported to induce leukocyte adhesion to endothelium through up-regulation of P-selectin surface expression. However, the underlying molecular and cellular mechanisms remain unknown. P-selectin is stored in Weibel-Palade bodies (WPBs), large secretory granules, in endothelial cells. In this study, we examined the role of protein kinase D (PKD), a newly identified regulator of protein transport, in AII-induced WPB exocytosis and the resultant P-selectin surface expression. We demonstrated that PKD2 was rapidly activated by AII in endothelial cells through phosphorylation of the activation loop at Ser744/748. AII-induced PKD2 activation correlated with increased P-selectin surface expression. Furthermore, AII-regulated PKD2 activation is protein kinase C (PKC) alpha-dependent. Importantly, knock-down of either PKD2 or PKCalpha expression inhibited AII-mediated P-selectin surface expression and monocyte adhesion. Our findings provide the first evidence that stimulation of P-selectin surface expression via PKCalpha-dependent PKD2 activation could be an important mechanism in the early onset of AII-initiated endothelial adhesiveness.

Links

PubMed

Keywords

Angiotensin II/pharmacology; Animals; Cell Adhesion; Cells, Cultured; Endothelium, Vascular/metabolism; Exocytosis/physiology; Gene Expression; Goats; Humans; Immunoblotting; Mice; P-Selectin/metabolism; Phosphorylation; Protein Kinase C-alpha/metabolism; Protein Kinases/metabolism; Rabbits; Weibel-Palade Bodies/metabolism

public



Cancel