Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.17 (CaMKII)
 4,029 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

CaM kinase-Gr is a Ca2+/calmodulin-dependent protein kinase that is enriched in brain and thymus. The enzyme was isolated from rat cerebellum, which contained alpha (M(r) 65,000) and beta (M(r) 67,000) polypeptides, and rat forebrain, which contained only the alpha polypeptide. Both enzyme preparations readily underwent autophosphorylation with dramatic up-regulation of their Ca2+/calmodulin-dependent, as well as-independent, activity. Autophosphorylation also caused a characteristic retardation in the electrophoretic gel mobility of the alpha and beta polypeptides. Treatment of autophosphorylated CaM kinase-Gr with acid phosphatase fully dephosphorylated the enzyme and reversed the changes in electrophoretic migration of both polypeptides. Phosphopeptide mapping indicated that the alpha and beta polypeptides were phosphorylated on identical or homologous sites, which probably induces similar structural and catalytic modifications in the two polypeptides. The actual site(s) of autophosphorylation was determined by the purification and amino acid sequencing of tryptic peptides from 32P-labeled CaM kinase-Gr. The major site of autophosphorylation was localized to a novel N-terminal domain, which is rich in Ser/Thr/Pro residues. The functional and structural studies on CaM kinase-Gr autophosphorylation imply that the enzyme is comprised of two regulatory domains, one on either side of a catalytic domain, followed by a C-terminal, putative association domain. The properties of such a structural model are discussed.
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PMID:Site and consequences of the autophosphorylation of Ca2+/calmodulin-dependent protein kinase type "Gr". 838 11

The localization of Ca2+/calmodulin-dependent protein kinase IV (CaM kinase IV) in the mature and developing rat retina was examined by immunohistochemistry and in situ hybridization histochemistry. In immunoblotting analysis, a single band of 63 kDa was detected in the crude homogenate of the adult rat retina, indicating the presence of the alpha polypeptide of CaM kinase IV. In the adult rat retina, most of the bipolar cells and some ganglion cells exhibited CaM kinase IV-immunoreactivity. By immunoelectron microscopy, the immunoreactive product was predominantly localized to the nucleus of immunoreactive cells. In the developing rat retina, immunoreactive bipolar cells were first detected on postnatal day 10 (P10), and they were abundant on P14. All these findings suggest that CaM kinase IV may participate in some yet unknown nuclear Ca(2+)-relating visual signal-processing of the retina.
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PMID:Immunohistochemical localization of Ca2+/calmodulin-dependent protein kinase type IV in the mature and developing rat retina. 878 75