Characterization of calcium-activated, phospholipid-dependent protein kinase from rat serosal mast cells and RBL-1 cells |
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| Authors: | M Kurosawa C W Parker |
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| Affiliation: | 1. Department of Biological Sciences, School of Crystallography, Birkbeck College, London, United Kingdom;2. Institut Pasteur, Unité de Recherche et d’Expertise Bactéries Anaérobies et Toxines, Institut Pasteur, Paris, France;3. College of Life and Environmental Sciences, University of Exeter, Exeter, United Kingdom |
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| Abstract: | Evidence is presented that rat serosal mast cells and cells of the rat basophilic leukemia line, RBL-1, each contain a calcium-activated, phospholipid-dependent protein kinase. The enzymes are very similar in their activation requirements to the calcium-dependent enzymes termed protein kinase Cs in brain. The enzyme is selectively stimulated by diolein and phosphatidylserine and is inhibited by several local anesthetics. The Ka for Ca2+ is 1.0 X 10(-3) M and 1.5 X 10(-4) M in mast cells and RBL-1 cells, respectively. The enzyme in mast cells is rapidly activated and apparently changed in its intracellular distribution when intact mast cells are stimulated with 48/80, A-23187, and anti-IgE and 12-O-tetradecanoyl-13-acetate in combination. |
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