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Protein kinase C β1 overexpression augments phorbol ester-induced increase in endothelial permeability

✍ Scribed by Pablito G. Nagpala; Asrar B. Malik; Phuoc T. Vuong; Hazel Lum

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
438 KB
Volume
166
Category
Article
ISSN
0021-9541

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✦ Synopsis

We studied the postulated involvement of the protein kinase C P1 (PKCP, 1 isoform in the regulation of endothelial permeability using human dermal microvascular endothelial cell line (HMEC-1). We overexpressed the recombinant PKCP, gene via retroviral-mediated transduction in these cells. PKCP, gene transfer was stable, and PKCP, protein production was persistent for at least 1 month posttransduction. Addition of 2 x lo-' M and 2 x M phorbol 12-myristate 13-acetate (PMA) to the control (nontransduced) HMEC-1 cells increased the transendothelial '251albumin clearance rate (an index of endothelial permeability) from 2.5 ? 0.2 x lo-* ll/min to 5.4 ? 1.2 X 1 O-* pl/min and 16.8 t-3.1 X 1 0-* pl/min, respectively. However, addition of 2 X lo-' M PMA to PKCP,-overexpressing HMEC-1 cells produced a maximal increase in the transendothelial 'L51-albumin clearance rate of 15.9 5 2.0 x lo-' pl/min. Challenge of these cells with 2 X M PMA did not further augment the increase in permeability. Activation with PMA was associated with the translocation of the PKCP, from the cytosol to the membrane. These data show that PKCP, overexpression augments the increase in endothelial permeability in response to PKC activation, suggesting an important function for the PKCP, isoform in the regulation of endothelial barrier.

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