Protein phosphorylation systems in postmortem human brain

Protein phosphorylation systems regulated by cyclic adenosine 3',5'-monophosphate (cyclic AMP), or calcium in conjunction with calmodulin or phospholipid/diacylglycerol, have been studied by phosphorylation in vitro of particulate and soluble fractions from human postmortem brain samples....

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Bibliographic Details
Published in:Journal of molecular neuroscience 1989-01, Vol.1 (2), p.105-116
Main Authors: Walaas, S I, Perdahl-Wallace, E, Winblad, B, Greengard, P
Format: Article
Language:English
Subjects:
550101 - Behavioral Biology- Tracer Techniques
550201 - Biochemistry- Tracer Techniques
550501 - Metabolism- Tracer Techniques
Adenosine Triphosphate - metabolism
ALKALINE EARTH METALS
ANIMALS
AUTOPSY
AUTORADIOGRAPHY
BASIC BIOLOGICAL SCIENCES
BODY
BRAIN
Brain - metabolism
CALCIUM
CALMODULIN
CENTRAL NERVOUS SYSTEM
CHEMICAL REACTIONS
CYCLASES
DIAGNOSTIC TECHNIQUES
ELECTROPHORESIS
Electrophoresis, Polyacrylamide Gel
ELEMENTS
ENZYME ACTIVITY
ENZYMES
Humans
LYASES
MAMMALS
MAN
METALS
MOLECULAR WEIGHT
Nerve Tissue Proteins - isolation & purification
Nerve Tissue Proteins - metabolism
NERVOUS SYSTEM
Organ Specificity
ORGANIC COMPOUNDS
ORGANS
Phosphorus Radioisotopes
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
Postmortem Changes
PRIMATES
PROTEINS
Rats
TRANSFERASES
VERTEBRATES
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Summary:Protein phosphorylation systems regulated by cyclic adenosine 3',5'-monophosphate (cyclic AMP), or calcium in conjunction with calmodulin or phospholipid/diacylglycerol, have been studied by phosphorylation in vitro of particulate and soluble fractions from human postmortem brain samples. One-dimensional or two-dimensional gel electrophoretic protein separations were used for analysis. Protein phosphorylation catalyzed by cyclic AMP-dependent protein kinase was found to be highly active in both particulate and soluble preparations throughout the human CNS, with groups of both widely distributed and region-specific substrates being observed in different brain nuclei. Dopamine-innervated parts of the basal ganglia and cerebral cortex contained the phosphoproteins previously observed in rodent basal ganglia. In contrast, calcium/phospholipid-dependent and calcium/calmodulin-dependent protein phosphorylation systems were less prominent in human postmortem brain than in rodent brain, and only a few widely distributed substrates for these protein kinases were found. Protein staining indicated that postmortem proteolysis, particularly of high-molecular-mass proteins, was prominent in deeply located, subcortical regions in the human brain. Our results indicate that it is feasible to use human postmortem brain samples, when obtained under carefully controlled conditions, for qualitative studies on brain protein phosphorylation. Such studies should be of value in studies on human neurological and/or psychiatric disorders.
ISSN:0895-8696
1559-1166
DOI:10.1007/BF02918896