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Scientific article
English

Does protein kinase C control receptor-mediated phagocytosis in human neutrophils?

Contributors

Andersson, T.; Fallman, M.; Lew, Daniel Pablo; Stendahl, O.

Published in

FEBS letters, vol. 239, no. 2, p. 371-375

Publication date

1988

Abstract

It was previously demonstrated that C3bi- but not IgG-mediated phagocytosis in human neutrophils is a Ca2+-independent process [(1985) Nature 315, 509-511]. The objective of this study was to elucidate the nature of an additional messenger signal(s) that may be involved in receptor-mediated phagocytosis in these cells. The C3bi- and IgG-mediated phagocytic ability of neutrophils was inhibited by forskolin, a potent activator of adenylate cyclase. It was found that forskolin induced a 3-fold increase in cAMP levels and simultaneously reduced the uptake of both C3bi- and IgG-opsonized particles by 65%. This inhibition was reversed by exposure to either phorbol myristate acetate (PMA) or diacylglycerol (OAG), which are both activators of protein kinase C, but not by the inactive analog 4 alpha-PMA. PMA could also restore the phagocytic ability of neutrophils with an experimentally impaired calcium response. These results suggest that activation of protein kinase C might be an important transducing signal controlling receptor-mediated phagocytosis in human neutrophils.

Keywords

  • Cyclic AMP/blood
  • Diglycerides/pharmacology
  • Humans
  • Neutrophils/drug effects/immunology/ physiology
  • Phagocytosis
  • Protein Kinase C/ blood/physiology
  • Receptors, Immunologic/ physiology
  • Tetradecanoylphorbol Acetate/pharmacology

UNIGE affiliation entities

Citation (ISO format)

ANDERSSON, T. et al. Does protein kinase C control receptor-mediated phagocytosis in human neutrophils? In: FEBS letters, 1988, vol. 239, n° 2, p. 371–375.

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Journal ISSN

0014-5793
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