Source:http://linkedlifedata.com/resource/pubmed/id/21558470
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2011-6-13
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| pubmed:abstractText |
High doses of insulin and the insulin analog AspB10 have been reported to increase mammary tumor incidence in female rats likely via receptor-mediated mechanisms, possibly involving enhanced IGF-1 receptor activation. However, insulin and IGF-1 receptor functionality and intracellular signaling in the rat mammary gland in vivo is essentially unexplored. The authors investigated the effect of a single subcutaneous dose of 600 nmol/kg human insulin or IGF-1 on Akt and ERK1/2 phosphorylation in rat liver, colon, and mammary gland. Rat tissues were examined by Western blotting and immunohistochemistry by phosphorylation-specific antibodies. Insulin as well as IGF-1 caused Akt phosphorylation in mammary epithelial cells, with myoepithelial and basal epithelial cells being most sensitive. IGF-1 caused stronger Akt phosphorylation than insulin in mammary gland epithelial cells. Phosphorylation of ERK1/2 was not influenced by insulin or IGF-1. Rather, in liver and mammary gland P-ERK1/2 appeared to correlate with estrous cycling, supporting that ERK1/2 has important physiological roles in these two organs. In short, these findings supported that the rat mammary gland epithelium expresses functional insulin and IGF-1 receptors and that phosphorylation of Akt as well as ERK1/2 may be of value in understanding the effects of exogenous insulin in the rat mammary gland and colon.
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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/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 1
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
1533-1601
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
39
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
623-40
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| pubmed:dateRevised |
2011-11-17
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| pubmed:meshHeading |
pubmed-meshheading:21558470-Animals,
pubmed-meshheading:21558470-Blotting, Western,
pubmed-meshheading:21558470-Breast,
pubmed-meshheading:21558470-Colon,
pubmed-meshheading:21558470-Epithelial Cells,
pubmed-meshheading:21558470-Female,
pubmed-meshheading:21558470-Humans,
pubmed-meshheading:21558470-Immunohistochemistry,
pubmed-meshheading:21558470-Insulin,
pubmed-meshheading:21558470-Insulin-Like Growth Factor I,
pubmed-meshheading:21558470-Liver,
pubmed-meshheading:21558470-Mammary Glands, Animal,
pubmed-meshheading:21558470-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:21558470-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:21558470-Phosphorylation,
pubmed-meshheading:21558470-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:21558470-Rats,
pubmed-meshheading:21558470-Rats, Sprague-Dawley,
pubmed-meshheading:21558470-Receptor, IGF Type 1,
pubmed-meshheading:21558470-Signal Transduction
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| pubmed:year |
2011
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| pubmed:articleTitle |
In situ phosphorylation of Akt and ERK1/2 in rat mammary gland, colon, and liver following treatment with human insulin and IGF-1.
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| pubmed:affiliation |
Department of Veterinary Disease Biology, Faculty of Life Sciences, University of Copenhagen, Denmark. hhvd@novonordisk.com
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| pubmed:publicationType |
Journal Article,
Comparative Study
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