Investigations on myelinogenesis in vitro: I. The occurrence of endogenous protein kinase and its role in the phosphorylation of myelin basic proteins in "myelin-like membranes" isolated from cerebral cell cultures.
The presence of a protein kinase capable of phosphorylating endogenous as well as exogenously added myelin basic proteins has been demonstrated in a myelin-like membrane fraction isolated from reaggregating and surface adhering, primary cultures of cells dissociated from embryonic mouse brain. Only the large and small components of myelin basic proteins were found to be phosphorylated when myelin-like membrane fraction was incubated with [gamma-32P]ATP. The protein kinase endogenous to the myelin-like membrane fraction was mainly of the cyclic AMP independent type. There was very little cyclic AMP dependent or cyclic GMP dependent protein kinase activities in this myelin-like fraction. Although the myelin basic proteins were the only endogenous proteins phosphorylated, protein kinase of the myelin-like membrane was capable of catalyzing the phosphorylation of exogenous substrates, such as histones.
D000818:Animals; D001921:Brain / Q000166:cytology / Q000196:embryology; D002478:Cells, Cultured; D003995:Dibutyryl Cyclic GMP / Q000494:pharmacology; D066298:In Vitro Techniques; D008566:Membranes / Q000378:metabolism; D051379:Mice; D008970:Molecular Weight; D004676:Myelin Basic Protein / Q000378:metabolism*; D009186:Myelin Sheath / Q000502:physiology*; D009712:Nucleotides, Cyclic / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
D004676:Myelin Basic Protein; D009712:Nucleotides, Cyclic; D010750:Phosphoproteins; D003995:Dibutyryl Cyclic GMP; D011494:Protein Kinases