pubmed-article:8884181 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C0026844 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C0016895 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C1160185 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
pubmed-article:8884181 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:8884181 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8884181 | pubmed:dateCreated | 1997-2-21 | lld:pubmed |
pubmed-article:8884181 | pubmed:abstractText | Gangliosides appear to regulate proliferation of different cell types. In the present study, we investigated the effects of gangliosides GM1, GM2 and GM3 on platelet-derived growth factor (PDGF)-induced vascular smooth muscle cell (VSMC) growth. In addition, we examined the effects of gangliosides on the PDGF-BB-dependent signalling transduction pathway in rat aortic VSMC. GM2 and GM1 inhibit the PDGF-BB-dependent receptor tyrosine autophosphorylation, stimulation of the PLC-gamma 1, increase of inositol-1,4,5-trisphosphate (InsP3), elevation in cytosolic free Ca2+ ([Ca2+]i), expression of the immediate early growth response gene c-fos and cell proliferation with the following rank order of potency GM2 > GM1. Although GM3 did not influence the PDGF-BB-dependent receptor autophosphorylation and PLC-gamma 1 activation, it effectively inhibited the PDGF-BB-dependent InsP3 formation, [Ca2+]i and cell growth. Binding studies with 125I-PDGF-BB on VSMC in the presence and absence of 10 to 50 microM of each ganglioside revealed that GM1 and GM2 effectively inhibited the specific binding of PDGF-BB with an IC50 value of 20 microM for GM2 and 30 microM for GM1. GM3 had no significant effect on the specific 125I-PDGF-BB binding. These observations suggest that GM1 and GM2 may interact with PDGF-BB or its receptor resulting in a prevention of its binding. GM3 was able to suppress the PDGF-BB-dependent increase of InsP3 and [Ca2+]i downstream of the PDGF-BB-dependent receptor autophosphorylation and PLC-gamma 1 activity. | lld:pubmed |
pubmed-article:8884181 | pubmed:language | eng | lld:pubmed |
pubmed-article:8884181 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8884181 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8884181 | pubmed:month | Sep | lld:pubmed |
pubmed-article:8884181 | pubmed:issn | 0171-9335 | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:VetterHH | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:KrausRR | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:HoppeJJ | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:DASG DGD | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:SchulteKK | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:SachinidisAA | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:SeulCC | lld:pubmed |
pubmed-article:8884181 | pubmed:author | pubmed-author:Meyer zu... | lld:pubmed |
pubmed-article:8884181 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8884181 | pubmed:volume | 71 | lld:pubmed |
pubmed-article:8884181 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8884181 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8884181 | pubmed:pagination | 79-88 | lld:pubmed |
pubmed-article:8884181 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8884181 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8884181 | pubmed:articleTitle | Gangliosides GM1, GM2 and GM3 inhibit the platelet-derived growth factor-induced signalling transduction pathway in vascular smooth muscle cells by different mechanisms. | lld:pubmed |
pubmed-article:8884181 | pubmed:affiliation | Medizinische Universitäts-Poliklinik, Bonn, Germany. | lld:pubmed |
pubmed-article:8884181 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8884181 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:8884181 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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