Source:http://linkedlifedata.com/resource/pubmed/id/15198369
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-6-16
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pubmed:abstractText |
For years an assumption was made that C-peptide, a byproduct of insulin biosynthesis, possessed no appreciable physiologic role. As other contributions in this volume amply testify, the time has come to re-evaluate that notion. C-peptide either directly through interaction with its specific cell-surface receptor or indirectly through an interaction with a related membrane entity, exerts a unique effect on several intracellular processes. We review here results of studies attempting to elucidate such molecular effects of C-peptide in different cell systems and tissues. Lacking a purified C-peptide receptor, we also demonstrate C-peptide effects on distinct elements of the insulin signal transduction pathways.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1543-8600
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25-36
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15198369-Animals,
pubmed-meshheading:15198369-Apoptosis,
pubmed-meshheading:15198369-C-Peptide,
pubmed-meshheading:15198369-Fibroblasts,
pubmed-meshheading:15198369-Humans,
pubmed-meshheading:15198369-Insulin,
pubmed-meshheading:15198369-Loop of Henle,
pubmed-meshheading:15198369-Lung,
pubmed-meshheading:15198369-Muscle, Skeletal,
pubmed-meshheading:15198369-Myoblasts,
pubmed-meshheading:15198369-Neurons,
pubmed-meshheading:15198369-Protein Tyrosine Phosphatases,
pubmed-meshheading:15198369-Signal Transduction
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pubmed:articleTitle |
The C-peptide signaling.
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pubmed:affiliation |
Grunberger Diabetes Institute, Bloomfield Hills, Michigan 48302, USA.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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