Isozymic forms of rat brain Ca2+-activated and phospholipid-dependent protein kinase.
AUTOR(ES)
Huang, K P
RESUMO
Three forms of rat brain Ca2+-activated and phospholipid-dependent protein kinase (EC 2.7.1.37) were separated by hydroxylapatite column chromatography. These enzymes, designated type I, II, and III protein kinase C, all have a molecular weight of 82,000, undergo autophosphorylation in the presence of Ca2+, phosphatidylserine, and diolein, and bind [3H]phorbol 12,13-dibutyrate. Autophosphorylation of these kinases resulted in an incorporation of 1-1.5 mol of 32P per mol of enzyme. Two-dimensional peptide mapping analysis revealed that these kinases had different sites of autophosphorylation. Phosphoamino acid analysis showed that type I and type III protein kinase C primarily autophosphorylated at a serine residue, whereas type II kinase autophosphorylated at both serine and threonine residues. In addition, polyclonal antibodies raised against a mixture of three types of the kinase preferentially inhibited type I and type II enzymes. Monoclonal antibodies against type I and type II kinase only recognized their respective enzymes but not the type III enzyme. These results demonstrate the presence of isozymic forms of protein kinase C in rat brain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=386965Documentos Relacionados
- Purified rat brain calcium- and phospholipid-dependent protein kinase phosphorylates ribosomal protein S6.
- Diacylglycerol stimulates DNA synthesis and cell division in mouse 3T3 cells: role of Ca2+-sensitive phospholipid-dependent protein kinase.
- Characterization of pituitary calcium-activated, phospholipid-dependent protein kinase: redistribution by gonadotropin-releasing hormone.
- Polyclonal antibodies to phospholipid/Ca2+-dependent protein kinase and immunocytochemical localization of the enzyme in rat brain.
- Activation of membrane protein-tyrosine phosphatase involving cAMP- and Ca2+/phospholipid-dependent protein kinases.