Linked Life Data

2625433

Source:http://linkedlifedata.com/resource/pubmed/id/2625433

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-4-3
pubmed:abstractText
We have characterized the interaction of homodimeric porcine transforming growth factor-beta 1 (TGF-beta 1) with affinity-purified human plasma fibronectin. Using a solid-phase binding assay, we have demonstrated that TGF-beta 1 binds to fibronectin immobilized on Immunlon ITM microtiter plates. TGF-beta 1 binding increased with time, reaching a plateau after 4-6 h, and was dependent upon the concentration of both labeled TGF-beta 1 and immobilized fibronectin present. The binding of radiolabeled TGF-beta 1 to fibronectin was saturable and was reduced 75% in the presence of a 100-fold excess of unlabeled TGF-beta 1. TGF-beta 1 bound to fibronectin with an association rate constant (Ka) of 2.96 x 10(3) M-1 s-1 and did not readily dissociate under various conditions. The binding of TGF-beta 1 to fibronectin was insensitive to variations in ionic strength over a range of 0.1-1.0 M NaCl and was relatively insensitive to divalent cation concentration in the range of 0.1-10.0 mM as well. These data suggest that the binding of TGF-beta 1 to fibronectin may not be dependent upon the interaction of charged amino acids within these two molecules. However, the binding of TGF-beta 1 to fibronectin was strongly pH-dependent and binding decreased dramatically below pH 4.0 and above pH 10.0, suggesting that charged amino acids may influence TGF-beta 1/fibronectin interactions. The association of TGF-beta 1 with immobilized fibronectin or other extracellular matrix components and subsequent dissociation under acidic conditions or by an as-yet-unidentified mechanism may play a role in the distribution and/or activity of this potent growth regulator at sites of tissue injury and inflammation in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0730-2312
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-200
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Transforming growth factor-beta 1 binds to immobilized fibronectin.
pubmed:affiliation
Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis 55455.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't