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...

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Bibliographic Details
Published in:FEBS letters 1989-12, Vol.258 (2), p.223-226
Main Authors: SEVERIN, S. E. JR, MOSKVITINA, E. L, BYKOVA, E. V, LUTZENKO, S. V, SHVETS, V. I
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Brain - enzymology
Brain - metabolism
Calmodulin - pharmacology
Fundamental and applied biological sciences. Psychology
Humans
Kinetics
Miscellaneous
Models, Biological
Nerve Tissue Proteins - isolation & purification
Nerve Tissue Proteins - metabolism
Phosphoproteins - isolation & purification
Phosphoproteins - metabolism
Phosphorylation
Protein Kinase C - metabolism
Proteins
Stearic Acids - pharmacology
Synapsins
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Summary: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.
ISSN:0014-5793
1873-3468