Linked Life Data

15134808

Source:http://linkedlifedata.com/resource/pubmed/id/15134808

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2004-5-11
pubmed:abstractText
The cloning of salt-inducible kinase-1 (SIK1) that was specifically expressed in the adrenal glands of high-salt diet-fed rats led to subsequent cloning of adipose-specific SIK2 and rather ubiquitous SIK3. The three enzymes constitute a novel serine/threonine kinase subfamily, a member of AMP-activated protein kinase (PKA) family. Physiological roles of SIK1 and SIK2 have been investigated. The SIK1 transcript was expressed very early in the ACTH-stimulated Y1 cells, even before the expression of transcripts for CYP11A and StAR protein. Forced expression of SIK1 inhibited the ACTH-dependent expression of CYP11A- and StAR protein-genes. Cotransfection assays employing CRE-reporter gene showed that SIK1 could repress the PKA-dependent activation of CRE by acting on the bZIP domain of the CRE-binding protein (CREB), though the target site of SIK1-mediated phosphorylation has yet to be determined. ACTH/PKA-dependent nucleocytoplasmic shuttling of SIK1 took place in Y1 cells, implying that the intracellular movement of SIK1 might be a physiologically important determining factor for regulation of steroidogenic gene expression in the early phase of ACTH-stimulation. The SIK2 gene was expressed in 3T3-L1 cells at a very early stage of adipogenesis. SIK2 could phosphorylate Ser-794 of human insulin-receptor-substrate-1 (IRS-1) in vitro as well as in vivo. In addition, the SIK2 activity in db/db mice adipose tissues was significantly higher than that in wild-type adipose. These results strongly suggest that SIK2 may play important role(s) in modulating the insulin-signaling cascade of adipocytes, and thus, may be involved in the development of insulin resistance. Taken together, these results suggest that the SIK isoforms regulate hormonal signal transduction in both adrenal and adipose tissues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
217
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-12
pubmed:dateRevised
2011-11-1
pubmed:meshHeading
pubmed-meshheading:15134808-Adipose Tissue, pubmed-meshheading:15134808-Adrenal Glands, pubmed-meshheading:15134808-Adrenocorticotropic Hormone, pubmed-meshheading:15134808-Animals, pubmed-meshheading:15134808-Cell Line, pubmed-meshheading:15134808-Cholesterol Side-Chain Cleavage Enzyme, pubmed-meshheading:15134808-Cloning, Molecular, pubmed-meshheading:15134808-Enzyme Activation, pubmed-meshheading:15134808-Gene Expression Regulation, Enzymologic, pubmed-meshheading:15134808-Isoenzymes, pubmed-meshheading:15134808-Mice, pubmed-meshheading:15134808-Organ Specificity, pubmed-meshheading:15134808-Phosphoproteins, pubmed-meshheading:15134808-Phosphorylation, pubmed-meshheading:15134808-Protein-Serine-Threonine Kinases, pubmed-meshheading:15134808-RNA, Messenger, pubmed-meshheading:15134808-Rats, pubmed-meshheading:15134808-Signal Transduction, pubmed-meshheading:15134808-Steroids
pubmed:year
2004
pubmed:articleTitle
Salt-inducible kinase (SIK) isoforms: their involvement in steroidogenesis and adipogenesis.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Graduate School of Medicine H-1, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't