| pubmed-article:7487873 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C1704256 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C0033692 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C0380603 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:7487873 | lifeskim:mentions | umls-concept:C1515406 | lld:lifeskim |
| pubmed-article:7487873 | pubmed:dateCreated | 1995-11-28 | lld:pubmed |
| pubmed-article:7487873 | pubmed:abstractText | Basic fibroblast growth factor (bFGF) was internalized by smooth muscle cells (SMC) from pig aorta. Correlation between heparin inhibition of binding and late internalization (8 h) implicated low-affinity sites in bFGF internalization. Transforming growth factor-beta 1 (TGF-beta 1) induced a 38% increase in bFGF internalized between 4 and 8 h. While bFGF and/or TGF-beta 1 enhanced cell-surface proteoglycan synthesis, 35S-labelled proteoglycans of the extracellular matrix (ECM) were not affected. This might be explained by the different turnover rates displayed by the two populations of proteoglycans. Although bFGF and/or TGF-beta 1 induced a similar stimulation in cell-surface chondroitin sulphate/dermatan sulphate and heparan sulphate (HS) proteoglycan synthesis, only the turnover of HS proteoglycans was increased. Twice as much HS proteoglycan was internalized in the presence of TGF-beta 1 or bFGF. Furthermore, TGF-beta 1 induced a 43 +/- 12% increase in HS proteoglycan internalized in the presence of bFGF with a parallel 38% increase in bFGF internalization. Overall, the results indicated that bFGF bound to two HS proteoglycan populations. bFGF storage (70% of bFGF bound to SMC) was not affected by TGF-beta 1 under our conditions and involved ECM proteoglycans characterized by a low turnover. bFGF internalization up-regulated by TGF-beta 1 involved cell-surface HS proteoglycan characterized by a high turnover. | lld:pubmed |
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| pubmed-article:7487873 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7487873 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7487873 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7487873 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7487873 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7487873 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7487873 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7487873 | pubmed:author | pubmed-author:TobelemGG | lld:pubmed |
| pubmed-article:7487873 | pubmed:author | pubmed-author:BerrouEE | lld:pubmed |
| pubmed-article:7487873 | pubmed:author | pubmed-author:Lévy-Toledano... | lld:pubmed |
| pubmed-article:7487873 | pubmed:author | pubmed-author:QuarchUU | lld:pubmed |
| pubmed-article:7487873 | pubmed:author | pubmed-author:BryckaertMM | lld:pubmed |
| pubmed-article:7487873 | pubmed:author | pubmed-author:Fontenay-Roup... | lld:pubmed |
| pubmed-article:7487873 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7487873 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7487873 | pubmed:volume | 311 ( Pt 2) | lld:pubmed |
| pubmed-article:7487873 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7487873 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7487873 | pubmed:pagination | 393-9 | lld:pubmed |
| pubmed-article:7487873 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
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| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
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| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
| pubmed-article:7487873 | pubmed:meshHeading | pubmed-meshheading:7487873-... | lld:pubmed |
| pubmed-article:7487873 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7487873 | pubmed:articleTitle | Transforming growth factor-beta 1 increases internalization of basic fibroblast growth factor by smooth muscle cells: implication of cell-surface heparan sulphate proteoglycan endocytosis. | lld:pubmed |
| pubmed-article:7487873 | pubmed:affiliation | Laboratoire de Physiopathologie cellulaire et moléculaire des cellules du sang et du vaisseau, INSERM, U 348, Hôpital Lariboisière, Paris, France. | lld:pubmed |
| pubmed-article:7487873 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7487873 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
