Calcium · calmodulin-dependent protein kinase II and calcium · phospholipid-dependent protein kinase activities in rat tissues assayed with a synthetic peptide

Yoshiaki Hashimoto, Thomas R. Soderling

    Research output: Contribution to journalArticle

    148 Scopus citations

    Abstract

    Rat tissue levels of Ca2+ · calmodulin-dependent protein kinase II (protein kinase II) and Ca2+ · phospholipid-dependent protein kinase (protein kinase C) were selectively assayed using the synthetic peptide syntide-2 as substrate. The sequence of syntide-2 (proleualaargthrleuservalalaglyleuprogly lyslys) is homologous to phosphorylation site 2 in glycogen synthase. The relative Vmax Km ratios of the known Ca2+-dependent protein kinases for syntide-2 were determined to be as follows: protein kinase II, 100; protein kinase C, 22; phosphorylase kinase, 2; myosin light chain kinase, 0.005. Levels of protein kinase II were highest in cerebrum (3.36 units/g tissue) and spleen (0.85 units/g) and lowest in testis (0.05 units/g) and kidney (0.04 units/g). Protein kinase II activity was localized predominantly in the 100,000g particulate fraction of cerebrum and testis, in the supernatant fraction of heart, liver, adrenal, and kidney, and about equally distributed between particulate and supernatant in spleen and lung. Likewise, protein kinase C activity was highest in cerebrum (0.56 units/g) and spleen (0.47 units/ g), and the majority of activity was present in the cytosolic fraction for all tissues measured except for cerebrum and testis in which the kinase activity was equal in both fractions. Finally, the ratios of protein kinase II to protein kinase C were different in various rat tissues and between particulate and supernatant fractions. These results suggest somewhat different functions for these two Ca2+-regulated, multifunctional protein kinases.

    Original languageEnglish (US)
    Pages (from-to)418-425
    Number of pages8
    JournalArchives of Biochemistry and Biophysics
    Volume252
    Issue number2
    DOIs
    StatePublished - Feb 1 1987

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology

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