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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
33
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pubmed:dateCreated |
1991-12-26
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pubmed:abstractText |
It has been widely assumed that the interaction of transforming growth factor-beta 1 (TGF-beta 1) with its serum-binding protein, alpha 2-macroglobulin (alpha 2M), mediates the rapid clearance of TGF-beta 1 from the circulation. To test this, we have analyzed the effect of TGF-beta 1 binding on the conformational state of alpha 2M. Our results demonstrate that the binding of TGF-beta 1 to alpha 2M does not lead to the conformational change in the alpha 2M molecule that is required for the clearance of the alpha 2M.TGF-beta 1 complex via the alpha 2M receptor. Furthermore, endogenous TGF-beta 1 is associated with the conformationally unaltered slow clearance form of alpha 2M. Clearance studies in mice show that the half-life of 125I-TGF-beta 1 in the circulation (1.6 +/- 0.71 min) is not affected by blocking the alpha 2M receptor with excess conformationally altered alpha 2M. These results suggest that TGF-beta 1 is rapidly cleared from the circulation after injection by a pathway not involving alpha 2M.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22290-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1718991-Animals,
pubmed-meshheading:1718991-Autoradiography,
pubmed-meshheading:1718991-Blotting, Western,
pubmed-meshheading:1718991-Chromatography, Ion Exchange,
pubmed-meshheading:1718991-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1718991-Female,
pubmed-meshheading:1718991-Humans,
pubmed-meshheading:1718991-Iodine Radioisotopes,
pubmed-meshheading:1718991-Metabolic Clearance Rate,
pubmed-meshheading:1718991-Methylamines,
pubmed-meshheading:1718991-Mice,
pubmed-meshheading:1718991-Mice, Inbred Strains,
pubmed-meshheading:1718991-Protein Conformation,
pubmed-meshheading:1718991-Swine,
pubmed-meshheading:1718991-Tissue Distribution,
pubmed-meshheading:1718991-Transforming Growth Factor beta,
pubmed-meshheading:1718991-Trypsin,
pubmed-meshheading:1718991-alpha-Macroglobulins
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pubmed:year |
1991
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pubmed:articleTitle |
Interaction of transforming growth factor-beta 1 with alpha 2-macroglobulin. Role in transforming growth factor-beta 1 clearance.
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pubmed:affiliation |
Section of Protein Engineering, National Research Council of Canada, Montreal, Quebec.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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