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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1995-11-28
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1335744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1379245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1381547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1400436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1429568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1533636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1551458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1555588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1556147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1563484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1634513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1646484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1744087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1847668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-1883201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2142464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2144898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2148568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2505639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2509487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2604692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2643420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2843546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-2971068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-3142885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-3422640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-3470794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-3474655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-3743663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-6448850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-7682010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-7693696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8175735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8276782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8288646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8360168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8419401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8456318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7487873-8479518
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
311 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
393-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7487873-Animals,
pubmed-meshheading:7487873-Aorta, Thoracic,
pubmed-meshheading:7487873-Cells, Cultured,
pubmed-meshheading:7487873-Dose-Response Relationship, Drug,
pubmed-meshheading:7487873-Endocytosis,
pubmed-meshheading:7487873-Extracellular Matrix,
pubmed-meshheading:7487873-Extracellular Matrix Proteins,
pubmed-meshheading:7487873-Fibroblast Growth Factor 2,
pubmed-meshheading:7487873-Heparitin Sulfate,
pubmed-meshheading:7487873-Membrane Proteins,
pubmed-meshheading:7487873-Muscle, Smooth, Vascular,
pubmed-meshheading:7487873-Proteoglycans,
pubmed-meshheading:7487873-Swine,
pubmed-meshheading:7487873-Transforming Growth Factor beta,
pubmed-meshheading:7487873-Up-Regulation
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pubmed:year |
1995
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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.
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pubmed:affiliation |
Laboratoire de Physiopathologie cellulaire et moléculaire des cellules du sang et du vaisseau, INSERM, U 348, Hôpital Lariboisière, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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