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Identification, Characterization, Immunocytochemical Localization, and Developmental Changes in the Activity of Calcium/Calmodulin‐Dependent Protein Kinase II in the CNS of Bombyx mori During Postembryonic Development
Author(s) -
Shanavas A.,
DuttaGupta Aparna,
Murthy Ch. R. K.
Publication year - 1998
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1998.70041644.x
Subject(s) - autophosphorylation , bombyx mori , biology , calmodulin , protein kinase a , biochemistry , bombyx , kinase , microbiology and biotechnology , phosphorylation , map2k7 , cyclin dependent kinase 2 , enzyme , gene
In the present investigation, in vitro phosphorylation of CNS proteins of the silkworm Bombyx mori during the postembryonic development have been studied. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and autoradiography of phosphorylated proteins revealed the presence of major phosphoproteins of 59/60 kDa. Based on molecular mass, calcium/calmodulin‐dependent autophosphorylation, substrate specificity, KN‐62 inhibition, apparent K m for ATP and syntide‐2, these proteins were identified as calcium/calmodulin‐dependent protein kinase II (CaM kinase II). Anti‐rat CaM kinase II monoclonal antibody showed immunoreactivity with Bombyx CaM kinase II isoforms. This kinase showed a high degree of autophosphorylation in neural tissue. During postembryonic development of Bombyx , two distinct peaks of enzyme activity could be noticed, one at the late‐larval and another at the late‐pupal stage, which were associated with an increase in amount of the enzyme. These results suggested that the expression of CaM kinase II in the CNS of Bombyx was developmentally regulated.