Selective effects of TPA and IL-1 on protein phosphorylation in murine thymocytes

Sofia Avissar; Kurt H. Stenzel; Abraham Novogrodsky

doi:10.1016/0008-8749(85)90378-8

Selective effects of TPA and IL-1 on protein phosphorylation in murine thymocytes

Sofia Avissar, Kurt H. Stenzel, Abraham Novogrodsky

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Abstract

Protein kinase C activity was demonstrated in murine thymocytes and the effects of TPA and IL-1 on this enzyme were studied. TPA, but not IL-1, could substitute for diacylglycerol in protein kinase C activation. Although TPA and IL-1 are both potent comitogens for murine thymocytes they markedly differ in their effects on protein phosphorylation and protein kinase C activation. Treatment of intact thymocytes with TPA resulted in a marked increase in the phosphorylation of an endogenous protein with M_r ~ 44,000. Enhanced phosphorylation of this protein was also observed when protein kinase C was activated in thymocyte extracts. In contrast to TPA, IL-1 neither induced phosphorylation of the 44,000-Da protein nor activated protein kinase C. The data suggests that protein kinase C does not mediate the comitogenic effect of IL-1 in murine thymocytes.

Original language	English
Pages (from-to)	462-471
Number of pages	10
Journal	Cellular Immunology
Volume	96
Issue number	2
DOIs	https://doi.org/10.1016/0008-8749(85)90378-8
State	Published - 1 Jan 1985
Externally published	Yes

ASJC Scopus subject areas

Immunology

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title = "Selective effects of TPA and IL-1 on protein phosphorylation in murine thymocytes",

abstract = "Protein kinase C activity was demonstrated in murine thymocytes and the effects of TPA and IL-1 on this enzyme were studied. TPA, but not IL-1, could substitute for diacylglycerol in protein kinase C activation. Although TPA and IL-1 are both potent comitogens for murine thymocytes they markedly differ in their effects on protein phosphorylation and protein kinase C activation. Treatment of intact thymocytes with TPA resulted in a marked increase in the phosphorylation of an endogenous protein with Mr ~ 44,000. Enhanced phosphorylation of this protein was also observed when protein kinase C was activated in thymocyte extracts. In contrast to TPA, IL-1 neither induced phosphorylation of the 44,000-Da protein nor activated protein kinase C. The data suggests that protein kinase C does not mediate the comitogenic effect of IL-1 in murine thymocytes.",

author = "Sofia Avissar and Stenzel, {Kurt H.} and Abraham Novogrodsky",

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T1 - Selective effects of TPA and IL-1 on protein phosphorylation in murine thymocytes

AU - Avissar, Sofia

AU - Stenzel, Kurt H.

AU - Novogrodsky, Abraham

PY - 1985/1/1

Y1 - 1985/1/1

N2 - Protein kinase C activity was demonstrated in murine thymocytes and the effects of TPA and IL-1 on this enzyme were studied. TPA, but not IL-1, could substitute for diacylglycerol in protein kinase C activation. Although TPA and IL-1 are both potent comitogens for murine thymocytes they markedly differ in their effects on protein phosphorylation and protein kinase C activation. Treatment of intact thymocytes with TPA resulted in a marked increase in the phosphorylation of an endogenous protein with Mr ~ 44,000. Enhanced phosphorylation of this protein was also observed when protein kinase C was activated in thymocyte extracts. In contrast to TPA, IL-1 neither induced phosphorylation of the 44,000-Da protein nor activated protein kinase C. The data suggests that protein kinase C does not mediate the comitogenic effect of IL-1 in murine thymocytes.

AB - Protein kinase C activity was demonstrated in murine thymocytes and the effects of TPA and IL-1 on this enzyme were studied. TPA, but not IL-1, could substitute for diacylglycerol in protein kinase C activation. Although TPA and IL-1 are both potent comitogens for murine thymocytes they markedly differ in their effects on protein phosphorylation and protein kinase C activation. Treatment of intact thymocytes with TPA resulted in a marked increase in the phosphorylation of an endogenous protein with Mr ~ 44,000. Enhanced phosphorylation of this protein was also observed when protein kinase C was activated in thymocyte extracts. In contrast to TPA, IL-1 neither induced phosphorylation of the 44,000-Da protein nor activated protein kinase C. The data suggests that protein kinase C does not mediate the comitogenic effect of IL-1 in murine thymocytes.

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U2 - 10.1016/0008-8749(85)90378-8

DO - 10.1016/0008-8749(85)90378-8

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ER -

Selective effects of TPA and IL-1 on protein phosphorylation in murine thymocytes

Abstract

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