| pubmed-article:10816596 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10816596 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:10816596 | lifeskim:mentions | umls-concept:C0302600 | lld:lifeskim |
| pubmed-article:10816596 | lifeskim:mentions | umls-concept:C0019134 | lld:lifeskim |
| pubmed-article:10816596 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:10816596 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:10816596 | pubmed:dateCreated | 2000-9-14 | lld:pubmed |
| pubmed-article:10816596 | pubmed:abstractText | Fibroblast growth factors (FGFs) are known to induce formation of new blood vessels, angiogenesis. We show that FGF-induced angiogenesis can be modulated using selectively desulfated heparin. Chinese hamster ovary cells (CHO677) deficient in heparan sulfate biosynthesis were employed to assess the function of heparin/heparan sulfate in FGF receptor-1 (FGFR-1) signal transduction and biological responses. In the presence of FGF-2, FGFR-1 kinase and subsequent mitogen-activated protein kinase Erk2 activities were augmented in a dose-dependent manner, whereas high concentrations of heparin resulted in decreased activity. The length of the heparin oligomer, minimally an 8/10-mer, was critical for the ability to enhance FGFR-1 kinase activity. The N- and 2-O-sulfate groups of heparin were essential for binding to FGF-2, whereas stimulation of FGFR-1 and Erk2 kinases by FGF-2 also required the presence of 6-O-sulfate groups. Sulfation at 2-O- and 6-O-positions was moreover a prerequisite for binding of heparin to a lysine-rich peptide corresponding to amino acids 160-177 in the extracellular domain of FGFR-1. Selectively 6-O-desulfated heparin, which binds to FGF-2 but fails to bind the receptor, decreased FGF-2-induced proliferation of CHO677 cells, presumably by displacing intact heparin. Furthermore, FGF-2-induced angiogenesis in chick embryos was inhibited by 6-O-desulfated heparin. Thus, formation of a ternary complex of FGF-2, heparin, and FGFR-1 appears critical for the activation of FGFR-1 kinase and downstream signal transduction. Preventing complex formation by modified heparin preparations may allow regulation of FGF-2 functions, such as induction of angiogenesis. | lld:pubmed |
| pubmed-article:10816596 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10816596 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10816596 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10816596 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10816596 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10816596 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:LarssonHH | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:LindahlUU | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:LundinLL | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:KandaSS | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:KreugerJJ | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:SalmivirtaMM | lld:pubmed |
| pubmed-article:10816596 | pubmed:author | pubmed-author:Claesson-Wels... | lld:pubmed |
| pubmed-article:10816596 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10816596 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:10816596 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10816596 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10816596 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10816596 | pubmed:pagination | 24653-60 | lld:pubmed |
| pubmed-article:10816596 | pubmed:dateRevised | 2010-5-26 | lld:pubmed |
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| pubmed-article:10816596 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10816596 | pubmed:articleTitle | Selectively desulfated heparin inhibits fibroblast growth factor-induced mitogenicity and angiogenesis. | lld:pubmed |
| pubmed-article:10816596 | pubmed:affiliation | Department of Genetics and Pathology, Rudbeck Laboratory, S-751 85 Uppsala, Sweden. | lld:pubmed |
| pubmed-article:10816596 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10816596 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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