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Translocation of Protein Kinase C to Subcellular Fractions of Human Neutrophils
Author(s) -
CHRISTIANSEN N. O.,
BORREGAARD N.
Publication year - 1989
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1989.tb01140.x
Subject(s) - chromosomal translocation , subcellular localization , kinase , microbiology and biotechnology , protein kinase a , chemistry , biology , biochemistry , cytoplasm , gene
The subcellular localization of protein kinase C in unstimulated human neutrophils and neutrophils stimulated by phorbol‐myristate‐acetate (PMA), 1‐oleoyl‐2‐acetyl‐rac‐glycerol (OAG), and ionomycin was investigated in subcellular tractions obtained by nitrogen cavitation and Percoll density gradient centrifugation. Protein kinase C was found to he localized mainly in the cytosol in unstimulated cells, whereas significant translocation to fractions containing the plasma membrane was observed after stimulation by PMA, OAG, and ionomycin. At the same time, phospholipid‐insensitive protein kinase activity appeared in the cytosol and the plasma membrane fractions. To determine whether binding of protein kinase C occurred to the plasma membrane or to intracellular membranes that had translocated to the plasma membrane, we investigated the ability of isolated azurophil, specific and secretory granules, and plasma membrane vesicles to bind protein kinase C in response to addition of PMA and OAG. Only fractions containing plasma membranes and secretory granules were able to bind protein kinase C. The observation explains the selective activation of plasma membrane structures by protein kinase C.