Literature DB >> 10545436

Downregulation of protein kinase cdelta activity enhances endothelial cell adaptation to hypoxia.

Y Shizukuda1, A Helisch, R Yokota, J A Ware.   

Abstract

BACKGROUND: Although protein kinase C (PKC) has been implicated in ischemic cell death, the role of individual PKC isoenzymes in the response of endothelial cells (ECs) to hypoxia is unknown. METHODS AND
RESULTS: To test the effect of hypoxia on the activity of individual PKC isoenzymes, human ECs were exposed to 95% N(2) with 5% CO(2) for 24 hours. This severe hypoxia reduced PKCdelta specific activity in both human umbilical vein ECs (HUVECs) and a HUVEC-derived EC line (ECVs) significantly (80.5+/-5.7% and 55.5+/-8. 6% of normoxia controls, respectively); the activities of PKCalpha and PKCepsilon were unchanged. The protein levels of PKCalpha, PKCdelta, and PKCepsilon were unchanged by hypoxia. To determine whether PKCdelta downregulation by hypoxia was linked to EC function, ECVs in which PKCdelta was stably overexpressed (PKCdelta-ECs) were exposed to hypoxia. A significant increase in cell death was observed in PKCdelta-ECs compared with controls (5.8+/-0.6% versus 2. 3+/-0.4% at 24 hours, 13.2+/-1.2% versus 4.1+/-0.4% at 48 hours, P<0. 05) during hypoxia. Neither the DNA laddering assay nor TUNEL staining revealed an increase in apoptosis of PKCdelta-ECs exposed to hypoxia, suggesting a hypoxia-induced increase in nonapoptotic cell death of PKCdelta-ECs. Inhibition of NO synthase with N(G)-monomethyl-L-arginine (L-NMMA) affected neither the decline in PKCdelta activity nor the EC death induced by hypoxia.
CONCLUSIONS: PKCdelta activity is decreased by hypoxia by a mechanism that does not involve NO synthase; this downregulation appears to enhance EC survival during hypoxia by decreasing nonapoptotic cell death.

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Year:  1999        PMID: 10545436     DOI: 10.1161/01.cir.100.18.1909

Source DB:  PubMed          Journal:  Circulation        ISSN: 0009-7322            Impact factor:   29.690


  9 in total

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2.  Antecedent ethanol ingestion prevents postischemic leukocyte adhesion and P-selectin expression by a protein kinase C-dependent mechanism.

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Authors:  T Klink; C Bela; S Stoelting; S O Peters; R Broll; T Wagner
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6.  PKC (Protein Kinase C)-δ Modulates AT (Antithrombin) Signaling in Vascular Endothelial Cells.

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8.  Phosphoproteomic Analysis of Rat Neutrophils Shows the Effect of Intestinal Ischemia/Reperfusion and Preconditioning on Kinases and Phosphatases.

Authors:  Muhammad Tahir; Samina Arshid; Belchor Fontes; Mariana S Castro; Simone Sidoli; Veit Schwämmle; Isabelle S Luz; Peter Roepstorff; Wagner Fontes
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9.  PKCδ regulates force signaling during VEGF/CXCL4 induced dissociation of endothelial tubes.

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Journal:  PLoS One       Date:  2014-04-03       Impact factor: 3.240

  9 in total

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