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

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

doi:10.1016/0006-291X(92)91522-R

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 journal › Article › peer-review

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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 language	English (US)
Pages (from-to)	40-46
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	189
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(92)91522-R
State	Published - Nov 30 1992
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(92)91522-R

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title = "Immunocytochemical expression and localization of protein kinase C in bovine aortic endothelial cells",

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.",

author = "Rosales, {Oscar R.} and Carlos Isales and Michael Nathanson and Sumpio, {Bauer E.}",

note = "Funding Information: 1Supported by grants to B.E.S. from the NIH (HL40305, Administration. O.R.R. was an AHA Research Fellow,",

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T1 - Immunocytochemical expression and localization of protein kinase C in bovine aortic endothelial cells

AU - Rosales, Oscar R.

AU - Isales, Carlos

AU - Nathanson, Michael

AU - Sumpio, Bauer E.

N1 - Funding Information: 1Supported by grants to B.E.S. from the NIH (HL40305, Administration. O.R.R. was an AHA Research Fellow,

PY - 1992/11/30

Y1 - 1992/11/30

N2 - 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.

AB - 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.

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

Abstract

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