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Phosphatidylinositol-specific phospholipase C activity of chromaffin granule-binding proteins

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:6380929
Using (U-/sup 14/C)phosphatidylinositol as substrate, Ca/sup 2 +/-dependent phospholipase C activity was detected in a group of bovine adrenal medullary proteins that bind to chromaffin granule membranes in the presence of Ca/sup 2 +/. The activity was maximal at neutral pH and represented an 80- to 240-fold enrichment of adrenal medullary cytosol phospholipase C activity measured at pH 7.3. The stimulation of activity by Ca/sup 2 +/ was complex; no activity was present in the absence of Ca/sup 2 +/, 25% activation occurred at 1 microM Ca/sup 2 +/, and full activation at 5 mM Ca/sup 2 +/. The enzyme bound to chromaffin granule membranes in the presence of 2 mM Ca/sup 2 +/ but was released at 40 microM Ca/sup 2 +/, suggesting that intrinsic enzyme activity may be regulated by (Ca/sup 2 +/) at 1 microM, but additional activation at higher concentrations of Ca/sup 2 +/ is seen in vitro as a result of Ca/sup 2 +/-dependent binding of the active enzyme to substrate-containing membranes. This enzyme may generate diacylglycerol and phosphorylated inositol to act as intracellular messengers in the vicinity of the chromaffin granule membrane during the process of exocytosis.
OSTI ID:
6380929
Journal Information:
J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 12; ISSN JBCHA
Country of Publication:
United States
Language:
English