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J Biol Chem, Vol. 273, Issue 42, 27654-27661, October 16, 1998
Differential Downstream Functions of Protein Kinase C and
- in EL4 Mouse Thymoma Cells
Moira S.
Resnick ,
Beom-Sik
Kang¶,
Dien
Luu¶,
Jeffery T.
Wickham¶,
Julianne J.
Sando , and
Chang S.
Hahn¶
From the Department of Pharmacology,
¶ Microbiology, and Beirne B. Carter Center for Immunology
Research, University of Virginia Health Sciences Center,
Charlottesville, Virginia 22908
Sensitive EL4 mouse thymoma cells (s-EL4) respond
to phorbol esters with growth inhibition, adherence to substrate, and
production of cytokines including interleukin 2. Since these cells
express several of the phorbol ester-sensitive protein kinase C (PKC) isozymes, the function of each isozyme remains unclear. Previous studies demonstrated that s-EL4 cells expressed substantially more
PKC and PKC than did EL4 cells resistant to phorbol esters (r-EL4). To examine potential roles for PKC and PKC in EL4 cells, wild type and constitutively active versions of the isozymes were transiently expressed using a Sindbis virus system. Expression of
constitutively active PKC , but not PKC , in s- and r-EL4 cells altered cell morphology and cytoskeletal structure in a manner similar
to that of phorbol ester treatment, suggesting a role for PKC in
cytoskeletal organization. Prolonged treatment of s-EL4 cells with
phorbol esters results in inhibition of cell cycling along with a
decreased expression of most of the PKC isozymes, including PKC .
Introduction of virally expressed PKC , but not PKC , overcame the
inhibitory effects of the prolonged phorbol ester treatment on cell
cycle progression, suggesting a possible involvement of PKC in cell
cycle regulation. These results support differential functions for
PKC and PKC in T cell activation.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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