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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1994-12-19
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pubmed:abstractText |
It is well known that osteoporosis is a common complication of patients with glucocorticoid excess. We showed previously that prostaglandin (PG) F2 alpha stimulates the synthesis of PGE2, a potent bone resorbing agent, and that the activation of protein kinase C amplifies the PGF2 alpha-induced PGE2 synthesis through the potentiation of phospholipase A2 activity in osteoblast-like MC3T3-E1 cells. In the present study, we examined the effect of dexamethasone on PGE2 synthesis induced by PGF2 alpha in MC3T3-E1 cells. The pretreatment with dexamethasone significantly inhibited the PGE2 synthesis in a dose-dependent manner in the range between 0.1 and 10 nmol/l in these cells. This effect of dexamethasone was dependent on the time of pretreatment up to 8 h. Dexamethasone also inhibited PGE2 synthesis induced by melittin, known as a phospholipase A2 activator. Furthermore, dexamethasone significantly inhibited the enhancement of PGF2 alpha- or melittin-induced PGE2 synthesis by 12-O-tetradecanoylphorbol-13-acetate, known as a protein kinase C activator. In addition, dexamethasone significantly inhibited PGF2 alpha-induced formation of inositol phosphates in a dose-dependent manner between 0.1 and 10 nmol/l in MC3T3-E1 cells. These results strongly suggest that glucocorticoid inhibits PGF2 alpha-induced PGE2 synthesis through the inhibition of phosphoinositide hydrolysis by phospholipase C as well as phospholipase A2 in osteoblast-like cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dexamethasone,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprost,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Melitten,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0804-4643
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
131
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
510-5
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7952162-Animals,
pubmed-meshheading:7952162-Cells, Cultured,
pubmed-meshheading:7952162-Dexamethasone,
pubmed-meshheading:7952162-Dinoprost,
pubmed-meshheading:7952162-Dinoprostone,
pubmed-meshheading:7952162-Hydrolysis,
pubmed-meshheading:7952162-Melitten,
pubmed-meshheading:7952162-Mice,
pubmed-meshheading:7952162-Osteoblasts,
pubmed-meshheading:7952162-Phosphatidylinositols,
pubmed-meshheading:7952162-Phospholipases A,
pubmed-meshheading:7952162-Phospholipases A2,
pubmed-meshheading:7952162-Tetradecanoylphorbol Acetate,
pubmed-meshheading:7952162-Type C Phospholipases
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pubmed:year |
1994
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pubmed:articleTitle |
Effect of glucocorticoid on prostaglandin F2 alpha-induced prostaglandin E2 synthesis in osteoblast-like cells: inhibition of phosphoinositide hydrolysis by phospholipase C as well as phospholipase A2.
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pubmed:affiliation |
Department of Biochemistry, Aichi Prefectural Colony, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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