Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1994-7-29
|
| pubmed:abstractText |
Treatment of HC11 mouse mammary epithelial cells with the lactogenic hormones dexamethasone, insulin, and prolactin (DIP) leads to cellular differentiation and production of the milk protein beta-casein. The following experimental evidence suggests the involvement of protein kinase C (PKC) in DIP induced signal transduction. Down-regulation of PKC by 12-O-tetradecanoylphorbol-13-acetate or addition of CGP 41251, a selective inhibitor of PKC, inhibited beta-casein protein expression induced by DIP in HC11 cells. This inhibition occurs at the level of transcription, since the DIP mediated activation of a beta-casein promoter-luciferase reporter construct or of mammary gland specific factor (MGF), an essential transcription factor for beta-casein promoter activity, was also inhibited by CGP 41251. Inhibition or down-regulation of PKC reduced the activation of MGF by prolactin as well. PKC-alpha, the only conventional PKC isoform expressed in HC11 cells, is most likely involved in the DIP induced beta-casein expression. (a) Only PKC-alpha and PKC-epsilon are down-regulated by 12-O-tetradecanoylphorbol-13-acetate whereas PKC-delta and PKC-zeta are not. (b) Of the PKC isoforms expressed in HC11 cells, CGP 41251 inhibits PKC-alpha more potently than PKC-delta, PKC-epsilon, and PKC-zeta. The IC50 for the inhibition of beta-casein synthesis, MGF activation, and beta-casein promoter activity by CGP 41251 correlated well with the IC50 of PKC-alpha inhibition. (c) Finally, only PKC-alpha translocated to membrane fractions after DIP or prolactin treatment. Taken together, these data indicate that PKC-alpha plays an important role in the signaling pathway activated by prolactin during beta-casein induction.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4'-N-benzoylstaurosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Dexamethasone,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Prolactin,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
1044-9523
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
239-47
|
| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:8018556-Alkaloids,
pubmed-meshheading:8018556-Amino Acid Sequence,
pubmed-meshheading:8018556-Animals,
pubmed-meshheading:8018556-Base Sequence,
pubmed-meshheading:8018556-Caseins,
pubmed-meshheading:8018556-Cell Differentiation,
pubmed-meshheading:8018556-Cell Line,
pubmed-meshheading:8018556-Dexamethasone,
pubmed-meshheading:8018556-Epithelial Cells,
pubmed-meshheading:8018556-Epithelium,
pubmed-meshheading:8018556-Female,
pubmed-meshheading:8018556-Gene Expression Regulation,
pubmed-meshheading:8018556-Insulin,
pubmed-meshheading:8018556-Isoenzymes,
pubmed-meshheading:8018556-Mammary Glands, Animal,
pubmed-meshheading:8018556-Mice,
pubmed-meshheading:8018556-Mice, Inbred BALB C,
pubmed-meshheading:8018556-Molecular Sequence Data,
pubmed-meshheading:8018556-Pregnancy,
pubmed-meshheading:8018556-Prolactin,
pubmed-meshheading:8018556-Protein Kinase C,
pubmed-meshheading:8018556-Protein Kinase C-alpha,
pubmed-meshheading:8018556-Staurosporine,
pubmed-meshheading:8018556-Tetradecanoylphorbol Acetate
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Protein kinase C and mammary cell differentiation: involvement of protein kinase C alpha in the induction of beta-casein expression.
|
| pubmed:affiliation |
Friedrich Miescher Institute, Basel, Switzerland.
|
| pubmed:publicationType |
Journal Article
|