RGD Reference Report - New isoforms of Ca2+/calmodulin-dependent protein kinase II in smooth muscle. - Rat Genome Database

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New isoforms of Ca2+/calmodulin-dependent protein kinase II in smooth muscle.

Authors: Zhou, ZL  Ikebe, M 
Citation: Zhou ZL and Ikebe M, Biochem J 1994 Apr 15;299 ( Pt 2):489-95.
RGD ID: 728273
Pubmed: PMID:8172610   (View Abstract at PubMed)
PMCID: PMC1138298   (View Article at PubMed Central)

Four novel isoforms of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) were found in rat aorta smooth muscle. Two of them were related to gamma-isoform of brain CaM kinase II (gamma-a). Differences in the primary structure of these isoforms were located in the variable region. One of them (gamma-b) contained 23 unique amino acid residues, whereas the other (gamma-c) did not contain this sequence. Both isoforms lacked the two segments (Val-316 to Gln-337 and Lys-353 to Leu-362) present in gamma-a. The DNA sequence of these gamma-isoforms except the variable region was exactly the same, suggesting that they are produced by alternative splicing. Another two isoforms were related to the delta-isoform of brain CaM kinase II (delta-a). delta-b contained a unique 11-residue sequence in the variable region whereas delta-c did not. As found for gamma-isoforms, the sequence analysis suggested that the three delta-isoforms are also produced by alternative splicing. Analysis of RNA by reverse transcription PCR confirmed the existence of specific messages for gamma-b, delta-a and delta-b. The variety of isoforms of CaM kinase II suggest that each isoform may play a specialized role in cell regulation.

Objects referenced in this article
Gene Camk2g calcium/calmodulin-dependent protein kinase II gamma Rattus norvegicus

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