Source:http://linkedlifedata.com/resource/pubmed/id/10673367
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2000-3-9
|
pubmed:abstractText |
The growth of the malignant human mammary MDA-MB-231 cells is stimulated by fibroblast growth factor-1 (FGF-1) but not by FGF-2. When these cells are cultured in the presence of chlorate, an inhibitor of heparan sulfate (HS) sulfation, their proliferation is stimulated by both FGF-1 and FGF-2. We analyzed the interactions of FGF-1 and FGF-2 with HS purified from the cell layer and the culture medium of control and chlorate-treated MDA-MB-231 cells. The HS from the cell layer bound FGF-1 with faster association kinetics than the HS from the culture medium, and so had a higher affinity for FGF-1. Chlorate treatment had no significant effect on the FGF-1 binding kinetics of the HS. In contrast to FGF-1, chlorate treatment of the cells significantly altered the FGF-2 binding kinetics. The HS from untreated cells possessed two binding sites for FGF-2, one with fast association kinetics (k(ass) 470,000 to 610,000 M(-1) s(-1)) and a high affinity (K(d) 46 to 70 nM) and one with slower association kinetics (k(ass) 74,000 to 100,000 M(-1) s(-1)) and a lower affinity (K(d) 290 to 400 nM). HS from chlorate-treated cells possessed just a single binding site for FGF-2 with fast association kinetics (k(ass) 270,000 to 290,000 M(-1) s(-1)) and a high affinity (K(d) 41 to 57 nM). These results show that there is a relationship between the binding kinetics of FGFs and their ability to stimulate cell growth.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chlorates,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
|
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
267
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
770-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10673367-Artifacts,
pubmed-meshheading:10673367-Breast Neoplasms,
pubmed-meshheading:10673367-Cell Division,
pubmed-meshheading:10673367-Cell Survival,
pubmed-meshheading:10673367-Chlorates,
pubmed-meshheading:10673367-Female,
pubmed-meshheading:10673367-Fibroblast Growth Factor 1,
pubmed-meshheading:10673367-Fibroblast Growth Factor 2,
pubmed-meshheading:10673367-Heparitin Sulfate,
pubmed-meshheading:10673367-Humans,
pubmed-meshheading:10673367-Kinetics,
pubmed-meshheading:10673367-Recombinant Proteins,
pubmed-meshheading:10673367-Tumor Cells, Cultured
|
pubmed:year |
2000
|
pubmed:articleTitle |
Differential regulation of FGF-1 and -2 mitogenic activity is related to their kinetics of binding to heparan sulfate in MDA-MB-231 human breast cancer cells.
|
pubmed:affiliation |
School of Biological Sciences, Life Sciences Building, University of Liverpool, Crown Street, Liverpool, L69 7ZB, United Kingdom.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|