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A truncated isoform of Ca 2+ /calmodulin‐dependent protein kinase II expressed in human islets of Langerhans may result from trans‐splicing
Author(s) -
Breen Maria A.,
Ashcroft Stephen J.H.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00555-3
Subject(s) - microbiology and biotechnology , complementary dna , alternative splicing , biology , protein kinase a , gene , cyclin dependent kinase 4 , cyclin dependent kinase 2 , map3k7 , cyclin dependent kinase 9 , rna splicing , gene isoform , map2k7 , kinase , rna , biochemistry
Calcium/calmodulin‐dependent protein kinase II (CaM kinase II) has been proposed to play a key role in glucose stimulated insulin secretion. Using the rapid amplification of cDNA ends technique we amplified the 3′ end of the CaM kinase II γ gene from human islet RNA. A novel cDNA was detected composed of 5′ sequence from the human CaM kinase II γ gene joined to the 3′ end of the human signal recognition particle 72 (SRP72) gene. We predict that this mRNA species will code for a truncated form of CaM kinase II, designated γ SRP , comprising the entire catalytic and regulatory domains of the protein and with a predicted molecular weight of 37 kDa. We mapped the human SRP72 gene to chromosome 18 and, as the CaM kinase II γ gene was previously mapped to human chromosome 10q22, we suggest this novel cDNA may have resulted from trans‐splicing.