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Protein kinase activities associated with ribosomes of developing rat brain. Identification of eukaryotic initiation factor 2 kinases
Author(s) -
Alcazar Alberto,
Fando Juan L.,
Azuara Carmen,
Galea Elena,
Salinas Matilde
Publication year - 1986
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/0736-5748(86)90005-5
Subject(s) - kinase , microbiology and biotechnology , ribosome , identification (biology) , initiation factor , biology , biochemistry , gene , rna , botany
Protein kinases associated with ribosomes in the brains of suckling (4–10 days) and adult (2 months) rats were extracted from ribosomal fraction with 0.5 M KCl. The different protein kinase activities were characterized by their ability to phosphorylate three exogenous substrates: casein, histone IIs and histone IIIs in the presence of different modulators. Ribosomal salt wash fractions contain a high casein kinase activity which was partially inhibited by heparin and stimulated by calmodulin in the presence of Ca 2+ , indicating the presence of casein kinase I and II and calcium/calmodulindependent kinases. Cyclic AMP and cyclic GMP‐dependent kinases and protein kinase C (calcium/phospholipids‐dependent kinase) were also present. No differences were found in the casein kinase activities of suckling and adult animals, but histone kinase activities were higher in adult than in suckling animals. To identify initiation factor 2 kinases, purified factor from adult brains was used as a protein marker. In addition to the phosphorylation of both factor subunits α and β by casein kinase I or II, an increased phosphorylation was detected of a subunit in the presence of cyclic AMP, and β subunit, in the presence of Ca 2+ /calmodulin or Ca 2+ /phospholipids. Present results reinforce our hypothesis that, as occurs in other eukaryotic cells, the decreased rate of protein synthesis during brain development may be regulated by phosphorylation of initiation factor 2.