Suramin inhibits binding and degradation of platelet-derived growth factor in arterial smooth muscle cells but does not interfere with autocrine stimulation of DNA synthesis
Identifieur interne : 003150 ( Main/Exploration ); précédent : 003149; suivant : 003151Suramin inhibits binding and degradation of platelet-derived growth factor in arterial smooth muscle cells but does not interfere with autocrine stimulation of DNA synthesis
Auteurs : Maria Sjölund [Suède] ; Johan Thyberg [Suède]Source :
- Cell and Tissue Research [ 0302-766X ] ; 1989-04-01.
English descriptors
- KwdEn :
- Teeft :
- Acad, Autocrine, Autocrine stimulation, Betsholtz, Binding buffer, Biol, Cell surface, Cellular, Cellular binding, Cellular proliferation, Continuous presence, Contractile, Control cultures, Degradation, Degraded material, Growth factor, Heldin, Heldin westermark, Inhibitory effect, Intracellular degradation, Large golgi, Lysosomal, Lysosomal enzyme activities, Lysosomal system, Lysosome, Muscle cells, Natl, Nilsson, Pdgf, Phenotype, Phenotypic, Phenotypic modulation, Primary culture, Primary cultures, Proc, Proc natl acad, Receptor, Rinsed, Sarcoma, Secondary cultures, Simian, Simian sarcoma virus, Smooth muscle cells, Specific activities, Standard deviations, Suramin, Synthetic phenotype, Thyberg, Triplicate, Triplicate cultures, Vertical lines, Westermark.
Abstract
Summary: During in vitro culture arterial smooth muscle cells of adult rats are able to produce a platelet-derived growth factor (PDGF)-like protein and to promote their own growth in an autocrine manner. Here, this process has been studied using suramin, a polyanionic drug that has been reported to interfere with the cellular binding of several growth factors. Our results indicate that suramin speeds up the transition of the cells from a contractile to a synthetic phenotype early in primary culture. It inhibits the binding of PDGF to the cells, displaces PDGF bound to the cell surface, and slows down the degradation of PDGF internalized by the cells. It reduces the specific activities of the lysosomal enzymes acid phosphatase, β-N-ace-tylglucosaminidase and β-glucuronidase, and gives rise to an accumulation of lysosomes with myelin-like inlcusions. It blocks PDGF- and serum-induced DNA synthesis and cellular proliferation in secondary cultures, but lacks a distinct inhibitory effect on DNA synthesis in primary cultures under serum-free conditions. The results suggest that the PDGF-like protein produced by the smooth muscle cells under the latter conditions may bind to its receptor and exert its autocrine effect intracellularly, without prior release into the pericellular space.
Url:
DOI: 10.1007/BF00224716
Affiliations:
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cultures</term><term>Degradation</term><term>Degraded material</term><term>Growth factor</term><term>Heldin</term><term>Heldin westermark</term><term>Inhibitory effect</term><term>Intracellular degradation</term><term>Large golgi</term><term>Lysosomal</term><term>Lysosomal enzyme activities</term><term>Lysosomal system</term><term>Lysosome</term><term>Muscle cells</term><term>Natl</term><term>Nilsson</term><term>Pdgf</term><term>Phenotype</term><term>Phenotypic</term><term>Phenotypic modulation</term><term>Primary culture</term><term>Primary cultures</term><term>Proc</term><term>Proc natl acad</term><term>Receptor</term><term>Rinsed</term><term>Sarcoma</term><term>Secondary cultures</term><term>Simian</term><term>Simian sarcoma virus</term><term>Smooth muscle cells</term><term>Specific activities</term><term>Standard deviations</term><term>Suramin</term><term>Synthetic phenotype</term><term>Thyberg</term><term>Triplicate</term><term>Triplicate cultures</term><term>Vertical lines</term><term>Westermark</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: During in vitro culture arterial smooth muscle cells of adult rats are able to produce a platelet-derived growth factor (PDGF)-like protein and to promote their own growth in an autocrine manner. Here, this process has been studied using suramin, a polyanionic drug that has been reported to interfere with the cellular binding of several growth factors. Our results indicate that suramin speeds up the transition of the cells from a contractile to a synthetic phenotype early in primary culture. It inhibits the binding of PDGF to the cells, displaces PDGF bound to the cell surface, and slows down the degradation of PDGF internalized by the cells. It reduces the specific activities of the lysosomal enzymes acid phosphatase, β-N-ace-tylglucosaminidase and β-glucuronidase, and gives rise to an accumulation of lysosomes with myelin-like inlcusions. It blocks PDGF- and serum-induced DNA synthesis and cellular proliferation in secondary cultures, but lacks a distinct inhibitory effect on DNA synthesis in primary cultures under serum-free conditions. The results suggest that the PDGF-like protein produced by the smooth muscle cells under the latter conditions may bind to its receptor and exert its autocrine effect intracellularly, without prior release into the pericellular space.</div></front></TEI><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><country name="Suède"><region name="Svealand"><name sortKey="Sjolund, Maria" sort="Sjolund, Maria" uniqKey="Sjolund M" first="Maria" last="Sjölund">Maria Sjölund</name></region><name sortKey="Thyberg, Johan" sort="Thyberg, Johan" uniqKey="Thyberg J" first="Johan" last="Thyberg">Johan Thyberg</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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