Linked Life Data

2843356

Source:http://linkedlifedata.com/resource/pubmed/id/2843356

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-10-27
pubmed:abstractText
The possibility that FSH modulates the Ca++-, phospholipid-dependent pathway was studied in cultured rat Sertoli cells. Cells were metabolically labeled with [3H]myoinositol, and accumulation of [3H]inositol phosphates [( 3H]inositol mono-, di-, and trisphosphates) was measured by extraction and fractionation on ion exchange chromatography. Fetal bovine serum increased Sertoli cell phosphoinositide (PI) turnover in a time and concentration-dependent manner (ED50 = 2-3% vol/vol). FSH by itself had no significant effect on the accumulation of inositol phosphates. On the other hand, FSH inhibited, in a concentration-dependent manner, the serum-stimulated accumulation of inositol phosphates by more than 50%. HPLC ion exchange chromatography of the inositol phosphates showed that all isomers present in serum-stimulated extracts were reduced to the same extent after treatment with FSH. The treatment of the cells with either forskolin, the beta-adrenergic agonist isoproterenol, or (Bu)2cAMP also inhibited the PI turnover stimulated by fetal bovine serum. FSH inhibition was not detected in mature Sertoli cells, in which FSH no longer stimulates cAMP accumulation. These results demonstrate that FSH, via formation of cAMP, exerts inhibitory effects on the PI turnover of the Sertoli cell. Thus, while stimulating the cAMP-dependent pathway, at the same time FSH inhibits the Ca++-, phospholipid-dependent pathway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
123
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2032-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Follicle-stimulating hormone modulation of phosphoinositide turnover in the immature rat Sertoli cell in culture.
pubmed:affiliation
Institute of Histology and General Embryology, University of Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't