Linked Life Data

16595703

Source:http://linkedlifedata.com/resource/pubmed/id/16595703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-4-5
pubmed:abstractText
Interleukin-1alpha (IL-1alpha) plays an important role in the regulation of immune responses as well as in non-inflammatory events in different types of cells. Here we have investigated the involvement of the extracellular signal-regulated kinase (ERK) cascade in IL-1alpha-induced steroidogenesis by primary cultures of immature rat Leydig cells. Our findings indicate that protein kinase C functions as an upstream component of signal transduction from the IL-1 receptor type I (IL-1RI) to the ERK cascade. It was observed that IL-1alpha upregulated both steroidogenic acute regulatory (StAR) protein expression and its phosphorylation when compared with controls. Selective inhibition of these mitogen-activated protein kinases (MAPKs) by UO126 enhanced both the expression and phosphorylation of the StAR protein, but suppressed androgen production by the immature Leydig cells as well as dissipating the mitochondrial electrochemical potential (Psim) in these cells. The evidence that water-soluble cholesterol but not 22R-hydroxycholesterol-stimulated steroidogenesis was inhibited by UO126 suggested that an intact Psim across the inner mitochondrial membrane is required for cholesterol translocation and is positively regulated by the ERK cascade. We propose that activation of ERKs by IL-1alpha plays a dual role in the regulation of steroidogenesis in immature Leydig cells: these MAPKs downregulate StAR expression and phosphorylation, while at the same time they support an intact Psim across the inner mitochondrial membrane, thereby promoting translocation of cholesterol into the mitochondria of the Leydig cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0952-5041
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-36
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16595703-Animals, pubmed-meshheading:16595703-Biological Transport, pubmed-meshheading:16595703-Butadienes, pubmed-meshheading:16595703-Cell Differentiation, pubmed-meshheading:16595703-Cells, Cultured, pubmed-meshheading:16595703-Cholesterol, pubmed-meshheading:16595703-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:16595703-Enzyme Activation, pubmed-meshheading:16595703-Interleukin-1, pubmed-meshheading:16595703-Leydig Cells, pubmed-meshheading:16595703-Male, pubmed-meshheading:16595703-Mitochondrial Membranes, pubmed-meshheading:16595703-Mitogen-Activated Protein Kinase 1, pubmed-meshheading:16595703-Mitogen-Activated Protein Kinase 3, pubmed-meshheading:16595703-Nitriles, pubmed-meshheading:16595703-Phosphorylation, pubmed-meshheading:16595703-Protein Kinase C, pubmed-meshheading:16595703-Protein Kinase Inhibitors, pubmed-meshheading:16595703-Rats, pubmed-meshheading:16595703-Rats, Sprague-Dawley, pubmed-meshheading:16595703-Steroids, pubmed-meshheading:16595703-Time Factors
pubmed:year
2006
pubmed:articleTitle
Induction of steroidogenesis in immature rat Leydig cells by interleukin-1alpha is dependent on extracellular signal-regulated kinases.
pubmed:affiliation
Department of Woman and Child Health, Pediatric Endocrinology Unit Q2:08, Karolinska Institute & University Hospital, Astrid Lindgren Children's Hospital, SE-17176 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural