Redistribution of Protein Kinase C Isoforms in Human Neutrophils Stimulated by Formyl Peptides and Phorbol-Myristate Acetate

The redistribution of protein kinase C (PKC) isoforms between the cytosolic and plasma membrane fractions of stimulated human polymorphonuclear leukocytes (PMN) was analysed by means of western blotting with antibodies against PKC βI, βII and ζ. Treatment of PMN with 1 μM formyl-methionyl-leucyl-phe...

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Bibliographic Details
Published in:	Biochemical and biophysical research communications Vol. 212; no. 2; pp. 664 - 672
Main Authors:	Dang, P.M.C., Rais, S., Hakim, J., Perianin, A.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 17-07-1995
Subjects:	Blotting, Western Calcium - pharmacology Cell Membrane - enzymology Cytosol - enzymology Humans Isoenzymes - analysis Isoenzymes - metabolism N-Formylmethionine Leucyl-Phenylalanine - pharmacology Neutrophils - enzymology Neutrophils - ultrastructure Protein Kinase C - analysis Protein Kinase C - metabolism Tetradecanoylphorbol Acetate - pharmacology
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Summary:	The redistribution of protein kinase C (PKC) isoforms between the cytosolic and plasma membrane fractions of stimulated human polymorphonuclear leukocytes (PMN) was analysed by means of western blotting with antibodies against PKC βI, βII and ζ. Treatment of PMN with 1 μM formyl-methionyl-leucyl-phenylalanine (fMLP) induced a rapid (5-10 sec) and sustained (at least 10 min) increase in the membrane association of PKC βI, βII, and the two immunoreactive proteins (76-81 kDa) recognized by the antibody directed against PKC ζ. Optimal translocation of PKC isoforms to the plasma membrane occurred in the presence of 10−6M fMLP and was not associated with a detectable fall in cytosolic PKC. Tn the absence of external calcium, the translocation of all PKC isoforms induced by fMLP was rapid (5 sec) but the membrane association of PKC was lost within one minute. Unlike fMLP, phorbol myristate acetate (PMA) induced a concentration-dependent translocation of the PKC isoforms, which persisted in the membrane in the absence of external calcium. These data provide the first evidence of redistribution of PKC isoforms by a chemoattractant. They further indicate that external calcium plays a crucial role in the persitence of the membrane association of PKC βI, βII and ζ induced by formyl peptides.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1995.2020