Abstract
The ontogeny of two endogenous substrates for cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase; EC 2.7.1.37) has been studied in rat and guinea pig cerebrum. These endogenous substrates, referred to as proteins Ia and Ib, have been shown in other studies to be specific to nervous tissue and to be enriched in the synaptic membrane and synaptic vesicle fractions of adult brain. In the present study, proteins Ia and Ib were shown to increase markedly during the time of major synaptogenesis in rat cerebrum and guinea pig cerebrum, in which the morphological development of synapses is predominantly postnatal and prenatal, respectively. Similar results were obtained either by measuring endogenous phosphorylation of proteins Ia and Ib in the synaptic membrane fraction or by measuring phosphorylation of extracted proteins Ia and Ib with added protein kinase.
MeSH Terms
Animals
Brain/embryology,metabolism,ultrastructure
Cyclic AMP/metabolism
Gestational Age
Guinea Pigs
Nerve Tissue Proteins/metabolism
Phosphoproteins/metabolism
Phosphorylation
Protein Kinases/metabolism
Rats
Synapses/ultrastructure
Chemicals
Nerve Tissue Proteins
Phosphoproteins
Cyclic AMP
Protein Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lohmann S M
Ueda T
Greengard P
References (14)
14 references, click to expand
-
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75
PMID: 14907713
-
The relationship between mammalian foetal weight and conception age.
J Physiol. 1951 Jul;114(3):306-17
PMID: 14861815
-
Adenosine 3':5'-monophosphate-regulated phosphoprotein system of neuronal membranes. II. Solubilization, purification, and some properties of an endogenous adenosine 3':5'-monophosphate-dependent protein kinase.
J Biol Chem. 1977 Jul 25;252(14):5164-74
PMID: 17614
-
Adenosine 3':5'-monophosphate-regulated phosphoprotein system of neuronal membranes. I. Solubilization, purification, and some properties of an endogenous phosphoprotein.
J Biol Chem. 1977 Jul 25;252(14):5155-63
PMID: 194903
-
Purification of phosphoprotein phosphatase from bovine cardiac muscle that catalyzes dephosphorylation of cyclic AMP-binding protein component of protein kinase.
J Biol Chem. 1977 May 10;252(9):2855-9
PMID: 192723
-
Synaptogenesis in the corpus striatum of infant rat.
Exp Neurol. 1973 Jan;38(1):70-9
PMID: 4120090
-
Synaptogenesis in guinea-pig cerebral cortex: a glutaral-dehyde-PTA study.
Brain Res. 1974 Apr 19;70(2):245-59
PMID: 4133062
-
The formation of synaptic junctions in developing rat brain: a quantitative electron microscopic study.
Brain Res. 1967 Dec;6(4):716-27
PMID: 4169903
-
Regulation of endogenous phosphorylation of specific proteins in synaptic membrane fractions from rat brain by adenosine 3':5'-monophosphate.
J Biol Chem. 1973 Dec 10;248(23):8295-305
PMID: 4356625
-
Widespread occurrence of a specific protein in vertebrate tissues and regulation by cyclic AMP of its endogenous phosphorylation and dephosphorylation.
Metabolism. 1975 Mar;24(3):331-41
PMID: 165355
-
Solubilization of a phosphoprotein and its associated cyclic AMP-dependent protein kinase and phosphoprotein phosphatase from synaptic membrane fractions, and some kinetic evidence for their existence as a complex.
Arch Biochem Biophys. 1975 Oct;170(2):492-503
PMID: 172014
-
Possible role for cyclic nucleotides and phosphorylated membrane proteins in postsynaptic actions of neurotransmitters.
Nature. 1976 Mar 11;260(5547):101-8
PMID: 176592
-
A quantitative electron microscopic study of synaptogenesis in the dentate gyrus of the rat.
Brain Res. 1973 Dec 7;63:195-204
PMID: 4764297
-
Quantitative studies of postnatal changes in synapses in rat superficial motor cerebral cortex. An electron microscopical study.
Z Zellforsch Mikrosk Anat. 1970;110(4):559-68
PMID: 5515538