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Protein kinase C‐mediated regulation of the expression of CD14 and CD11 /CD18 in U937 cells
Author(s) -
Pedrinaci Susana,
RuizCabello Francisco,
Gomez Ovidio,
Collado Antonia,
Garrido Federico
Publication year - 1990
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910450215
Subject(s) - protein kinase a , u937 cell , protein kinase inhibitor , cd14 , biology , protein kinase c , microbiology and biotechnology , kinase , calcium , chemistry , biochemistry , receptor , apoptosis , organic chemistry
We used the U937 cell line to analyze CD14, CD11/CD18, HLA class‐I and DR antigen expression during PMA‐induced differentiation. Treatment of U937 cells with PMA markedly increased CD14, CDIIa, CDIIb and CDI8 antigen expression, and slightly increased CDIIc expression. Protein kinase C may play a major role in regulating the expression of these antigens. The protein kinase inhibitor H7 abrogated the inductive effect of PMA. Calcium ionophore, when added alone or in the presence of PMA, had no effect. The inhibitory effect of the calcium antagonist verapamil, EGTA, and of chlorpromazine, an antagonist of calcium‐binding proteins, supports a role for calcium‐dependent protein kinase C in the up‐regulation of CDI4 and CDII/CD18 surface expression. The specific calmodulin inhibitors R2457I and W7 had no effect on antigen expression. Our findings suggest that protein kinase C activation is an important step in the PMA‐induced differentiation of U937 cells.