Synapsin I from human brain. Phosphorylation by Ca2+, phospholipid-dependent protein kinase.
Synapsin I has been isolated from human brain by a rapid and efficient purification technique, and its phosphorylation by human brain Ca2+, phospholipid-dependent protein kinase (protein kinase C) has been studied. The inhibitory effect of calmodulin on this process has been demonstrated. It is also found that non-esterified fatty acids and acidic phospholipids are inhibitory for synapsin I phosphorylation by Ca2+, calmodulin-dependent protein kinase II.
Severin
S E
SE
M.V. Lomonosov Institute of Fine Chemical Technology, Moscow, USSR.
Moskvitina
E L
EL
Bykova
E V
EV
Lutzenko
S V
SV
Shvets
V I
VI
D001921:Brain / Q000201:enzymology / Q000378:metabolism*; D002147:Calmodulin / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000302:isolation & purification / Q000378:metabolism*; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D013229:Stearic Acids / Q000494:pharmacology; D016704:Synapsins
D002147:Calmodulin; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D013229:Stearic Acids; D016704:Synapsins; C031183:stearic acid; D011493:Protein Kinase C