Calcium-activated, phospholipid-dependent protein kinase and protein substrates in primary cultures of astrocytes.
Phosphoinositide-linked transmembrane signaling in the brain involves calcium-activated, phospholipid-dependent protein kinase (protein kinase C), but little is known about the glial contribution to this system. We observed that phosphorylation of several proteins in a cytosol fraction of rat astrocytes in primary culture was increased by the addition of calcium and phosphatidylserine. These agents also stimulated phosphate incorporation into lysine-rich histone, a substrate for protein kinase C. Addition of diacylglycerol, an activator of protein kinase C, further increased histone phosphorylation, whereas polymyxin B, an inhibitor of protein kinase C, blocked the stimulatory effect of calcium and phosphatidylserine. Based on enzyme units per mg protein, the activity of protein kinase C in astrocytes appears similar to that in whole brain cytosol. These results indicate that astrocytes display protein kinase C activity and suggest that the glial enzyme may be an important component of the receptor-linked phosphoinositide response system in the brain.
D000818:Animals; D000831:Animals, Newborn; D001253:Astrocytes / Q000201:enzymology*; D002478:Cells, Cultured; D003600:Cytosol / Q000201:enzymology; D006657:Histones / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010716:Phosphatidylinositols / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D006657:Histones; D009419:Nerve Tissue Proteins; D010716:Phosphatidylinositols; D011493:Protein Kinase C