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

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

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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@article{101df052bee44168a8415216424642b1,

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 \textasciitilde{} 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",

year = "1985",

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doi = "10.1016/0008-8749(85)90378-8",

language = "English",

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journal = "Cellular Immunology",

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TY - JOUR

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.

UR - https://www.scopus.com/pages/publications/0022337680

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

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

M3 - Article

C2 - 3879809

AN - SCOPUS:0022337680

SN - 0008-8749

VL - 96

SP - 462

EP - 471

JO - Cellular Immunology

JF - Cellular Immunology

IS - 2

ER -

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

Abstract

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