Immunocytochemical expression and localization of protein kinase C in bovine aortic endothelial cells

Oscar R. Rosales, Carlos Isales, Michael Nathanson, Bauer E. Sumpio

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Total PKC activity in BAEC incubated for 24 hrs in either 10% serum (FBS) or serum-deprived media (SDM) was similar. However, most of the activity (69%) in the FBS group was detected in the particulate fraction, while it was mainly in the cystosolic fraction (66%) in the SDM group. By confocal microscopy, there was diffuse cytoplasmic localization of the antibodies to the α and β PKC isoforms. γ PKC was not detected. Treatment of FBS or SDM cells with a phorbol ester resulted in an increase in PKC activity with translocation to the particulate fraction. PKC α immunofluorescence redistributed to the perinuclear region whereas PKC β staining remained mostly cytosolic. Calphostin C, a PKC inhibitor, prevented the phorbol ester-induced increase in PKC activity and translocation.

Original languageEnglish (US)
Pages (from-to)40-46
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume189
Issue number1
DOIs
StatePublished - Nov 30 1992

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Endothelial cells
Phorbol Esters
Protein Kinase C
Endothelial Cells
Confocal microscopy
Serum
Protein Isoforms
Antibodies
Confocal Microscopy
Fluorescent Antibody Technique
Staining and Labeling
calphostin C
Therapeutics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Immunocytochemical expression and localization of protein kinase C in bovine aortic endothelial cells. / Rosales, Oscar R.; Isales, Carlos; Nathanson, Michael; Sumpio, Bauer E.

In: Biochemical and Biophysical Research Communications, Vol. 189, No. 1, 30.11.1992, p. 40-46.

Research output: Contribution to journalArticle

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