Source:http://linkedlifedata.com/resource/pubmed/id/10611753
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
2000-2-23
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pubmed:abstractText |
The transforming growth factor-betas (TGF-betas) are synthesized as precursor proteins that are modified intracellularly prior to secretion. One of the most relevant intracellular modifications is the cleavage of the C-terminal pro-region from the N-terminal portion of the protein. The C-terminal pro-region is referred to as the latency-associated peptide (LAP) while the N-terminal region is called the mature TGF-beta or active TGF-beta. However, with some exceptions the LAP noncovalently associates with the mature TGF-beta prior to secretion. When the mature TGF-beta is associated with the LAP it is called L-TGF-beta and cannot interact with its receptor and has no biological effect. The TGF-betas and their receptors are very ubiquitously expressed, suggesting that the regulation of TGF-beta activity is likely to be complex and multifactorial. However, one of the most important means of controlling the biological effects of TGF-beta is the regulation of converting L-TGF-beta to active TGF-beta. The current literature supports two major mechanisms of activation of L-TGF-beta and suggests that the mechanism of activation of L-TGF-beta may be varied and context-dependent. For TGF-beta to become biologically active the LAP has to be either released from its associations with L-TGF-beta or undergo conformational change such that the LAP is not released from the L-TGF-beta complex but exposes the TGF-beta receptor binding site. Since TGF-beta has been associated with the pathogenesis of numerous diseases, the various mechanisms of activation of L-TGF-beta in context offer the possibility of controlling TGF-beta activity localized to the organ of involvement and to a more specific disease process.
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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/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta1
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1286-4579
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1255-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10611753-Gene Expression Regulation,
pubmed-meshheading:10611753-Humans,
pubmed-meshheading:10611753-Peptide Fragments,
pubmed-meshheading:10611753-Protein Precursors,
pubmed-meshheading:10611753-Proteins,
pubmed-meshheading:10611753-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:10611753-Transforming Growth Factor beta,
pubmed-meshheading:10611753-Transforming Growth Factor beta1
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pubmed:year |
1999
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pubmed:articleTitle |
TGF-beta: from latent to active.
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pubmed:affiliation |
Department of Medicine and the Manitoba Institute of Cell Biology, University of Manitoba, 100 Olivia Street, Winnipeg R3E 0V9, Manitoba, Canada.
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pubmed:publicationType |
Journal Article,
Review
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