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New alternatively spliced variants of calmodulin-dependent protein kinase II from rabbit liver
1Department of Biochemistry, Asahikawa Medical College, Hokkaido, Japan.
Abstract:
Polymerase chain reaction analysis revealed four alternatively spliced variants of each of the gamma and delta isoforms of calmodulin-dependent protein kinase II (CaM-kinase II) in rabbit liver. Among the four variants of the gamma isoform, two were novel ones, designated as CaM-kinase II gamma-H and gamma-I. The gamma-I variant possessed both of the two deletable exons; D2a and D2b, which had never been found together in any variant. Sequence analysis of the gamma-I indicated that the D2a was upstream of the D2b and that they were contiguous with each other in the gamma-I. Among the four variants of the delta isoform, two were also novel ones, designated as CaM-kinase II delta-11 and delta-12, and the other two were the already-reported ones, delta-2 and delta-6. The delta-11 and delta-12 were identical to the delta-2 and delta-6, respectively, except that three bases (CAG) located at a splicing junction was deleted in the delta-11 and delta-12, suggesting two splicing sites of a single intron. Thus, the diverse splicing patterns may produce many more variants than those so far considered.