Linked Life Data

9405489

Source:http://linkedlifedata.com/resource/pubmed/id/9405489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
1998-1-22
pubmed:databankReference
pubmed:abstractText
We earlier confirmed that there are isoforms of Ca2+/calmodulin (CaM)-dependent protein kinase I (CaM kinase I) (CaM kinase Ibeta1 and Igamma) beside CaM kinase Ialpha by cDNA cloning (Yokokura, H., Terada, O., Naito, Y., and Hidaka, H. (1997) Biochim. Biophys. Acta 1338, 8-12). Here, we demonstrate the existence of an isoform-specific activation mechanism of CaM kinase I and alternative splicing specifically regulating CaM kinase I (CaM kinase Ibeta2) in the central nervous system. To cast light on isoform structure-enzyme activity relationships, CaM kinase Ibeta1, Ibeta2, and Ialpha were expressed separately using a baculovirus/Sf9 cell expression system. The novel CaM kinase Ibeta2 isoform demonstrated similar catalytic activity to those of CaM kinase Ibeta1 and Ialpha. Interestingly, CaM kinase Ibeta1 and Ibeta2 both can activate CaM kinase Ialpha activity via phosphorylation at Thr177. Reverse transcribed-polymerase chain reaction analysis showed that CaM kinase Ibeta2 is dominant in the cerebrum and cerebellum, whereas CaM kinase Ibeta1 is present in peripheral tissues such as liver, heart, lung, kidney, spleen, and testis. CaM kinase Ibeta2 was also detected with an anti-CaM kinase Ibeta2 antibody in PC12 cells. The results indicate that alternative splicing is a means for tissue-specific expression of CaM kinase Ibeta. Thus the Thr177 residue of CaM kinase Ialpha is phosphorylated by not only CaM kinase kinase but also CaM kinase Ibeta for activation of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32704-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Isoform-specific activation and structural diversity of calmodulin kinase I.
pubmed:affiliation
Department of Pharmacology, Nagoya University School of Medicine, Showa-ku, Nagoya 466, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't