Abstract:
:The interaction of basic FGF (bFGF) with heparin, heparan sulfate and related sugars can potentiate or antagonize bFGF activity, depending on the size of the saccharide used. Oligosaccharides based on heparin structures, as small as six sugar residues, have been demonstrated to bind to bFGF and block its activity, while larger structures (> 10 sugar residues) tend to potentiate bFGF. In this study we have synthesized a series of compounds designed to test the requirements of size and sulfation for binding of oligosaccharides to bFGF. These oligosaccharides are not derived from heparin, but rather, are linear chains of glucose linked alpha 1-4 (malto-oligosaccharides) that have been chemically sulfated. In addition to bFGF binding, these compounds were tested for their ability to block basic functions of endothelial cells that are known to be mediated, at least in part, by bFGF. We report that the ability of sulfated malto-oligosaccharides to block binding of bFGF to heparan sulfate was dependent on the size (at least a tetrasaccharide is required), and the degree of sulfation. The activity profile in the bFGF ELISA closely correlated with the ability of these compounds to block REEC or HMVEC tube formation on Matrigel. There was a similar relationship of size and sulfation to the ability of the sulfated malto-oligosaccharides to inhibit endothelial cell growth for most human and rat EC types tested. The single exception was REEC cell growth. One isolate of these cells was stimulated by sulfated malto-oligosaccharides rather than inhibited by them, while a second isolate was neither stimulated nor inhibited. This stimulation showed no correlation with inhibition of bFGF binding in the ELISA assay, suggesting that growth of this cell type was probably not dependent on bFGF. Compounds derived from this series of sulfated, malto-oligosaccharides have the potential to function as bFGF antagonists, are relatively easy to produce, and possess relatively low anticoagulant properties.
journal_name
J Cell Physioljournal_title
Journal of cellular physiologyauthors
Foxall C,Wei Z,Schaefer ME,Casabonne M,Fugedi P,Peto C,Castellot JJ Jr,Brandley BKdoi
10.1002/(SICI)1097-4652(199609)168:3<657::AID-JCP1subject
Has Abstractpub_date
1996-09-01 00:00:00pages
657-67issue
3eissn
0021-9541issn
1097-4652pii
10.1002/(SICI)1097-4652(199609)168:3<657::AID-JCP1journal_volume
168pub_type
杂志文章abstract::The possibility that one or both of the synthetic triamines, 1,3,6-triaminohexane and 1,4,7-triaminoheptane, could substitute for the naturally occurring polyamines in the growth of SV-3T3 cells was investigated. It was found that these triamines did lead to a restoration of growth in cells in which spermidine content...
journal_title:Journal of cellular physiology
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journal_title:Journal of cellular physiology
pub_type: 杂志文章
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更新日期:1978-02-01 00:00:00
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更新日期:1990-10-01 00:00:00
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journal_title:Journal of cellular physiology
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更新日期:1991-09-01 00:00:00
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pub_type: 杂志文章
doi:10.1002/jcp.1041200215
更新日期:1984-08-01 00:00:00
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doi:10.1002/jcp.22865
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journal_title:Journal of cellular physiology
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journal_title:Journal of cellular physiology
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更新日期:2005-06-01 00:00:00
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journal_title:Journal of cellular physiology
pub_type: 杂志文章
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journal_title:Journal of cellular physiology
pub_type: 杂志文章
doi:10.1002/jcp.1041280222
更新日期:1986-08-01 00:00:00
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更新日期:2017-12-01 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of cellular physiology
pub_type: 杂志文章
doi:10.1002/jcp.1041180109
更新日期:1984-01-01 00:00:00
abstract::Insulin and type I insulin-like growth factor (IGF-I) suppressed growth hormone (GH) expression followed by the induction of prolactin (PRL) biosynthesis in MtT/S cells cultured with normal sera. Insulin also increased the peptidylarginine deiminase activity in a dose-dependent manner. The increase was detectable at 1...
journal_title:Journal of cellular physiology
pub_type: 杂志文章
doi:10.1002/jcp.1041500227
更新日期:1992-02-01 00:00:00