Linked Life Data

9837965

Source:http://linkedlifedata.com/resource/pubmed/id/9837965

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
1999-1-14
pubmed:abstractText
Two membrane subfractions, one enriched in GM3 ganglioside and the other containing caveolin, were separated from low density detergent-insoluble membrane fraction prepared by sucrose density gradient centrifugation of postnuclear fraction of mouse melanoma B16 cells. The GM3-enriched subfraction, separated by anti-GM3 monoclonal antibody DH2, contained sphingomyelin, cholesterol, c-Src, and Rho A but not caveolin. In contrast, the caveolin-containing subfraction, separated by anti-caveolin antibody, contained neither GM3, c-Src, nor Rho A but did contain glucosylceramide, Ras, a very small quantity of sphingomyelin, and a very large quantity of cholesterol. The GM3/c-Src-enriched membrane subfraction was characterized by (i) maintenance of GM3-dependent adhesion and (ii) susceptibility to being activated for signal transduction through GM3. 32P-Phosphorylation of c-Src (Mr 60,000) together with two other components (Mr 45,000 and 29,000) was enhanced in the fraction bound to dishes coated with asialo-GM2 (Gg3) or with anti-GM3 monoclonal antibody DH2, detected by incubation with [gamma-32P]ATP at 37 degreesC for 5 min. GM3-dependent adhesion of B16 cells to Gg3-coated dishes and associated signaling were not reduced or abolished in the presence of either filipin or nystatin, which are cholesterol-binding reagents known to abolish caveolae structure and function. B16 melanoma cells incubated with filipin (0.16-0.3 micrograms/ml) or with nystatin (25 micrograms/ml) for 30 min showed depletion of cholesterol in detergent-insoluble membrane fraction but were still capable of binding to Gg3-coated plate and capable of the associated signaling. Thus, the GM3-enriched subfraction, involved in cell adhesion and capable of sending signals through GM3, represents a membrane domain distinguishable from caveolin-containing subfraction or caveolae. This microdomain is hereby termed the "glycosphingolipid signaling domain" or "glycosignaling domain".
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33766-73
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9837965-Animals, pubmed-meshheading:9837965-Caveolin 1, pubmed-meshheading:9837965-Caveolins, pubmed-meshheading:9837965-Cell Adhesion, pubmed-meshheading:9837965-Cell Membrane, pubmed-meshheading:9837965-Dogs, pubmed-meshheading:9837965-Filipin, pubmed-meshheading:9837965-Glycosphingolipids, pubmed-meshheading:9837965-Ligands, pubmed-meshheading:9837965-Melanoma, Experimental, pubmed-meshheading:9837965-Membrane Lipids, pubmed-meshheading:9837965-Membrane Proteins, pubmed-meshheading:9837965-Mice, pubmed-meshheading:9837965-Nystatin, pubmed-meshheading:9837965-Phosphorylation, pubmed-meshheading:9837965-Proto-Oncogene Proteins pp60(c-src), pubmed-meshheading:9837965-Signal Transduction, pubmed-meshheading:9837965-Tumor Cells, Cultured, pubmed-meshheading:9837965-ras Proteins
pubmed:year
1998
pubmed:articleTitle
Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling.
pubmed:affiliation
Pacific Northwest Research Institute, Seattle, Washington 98122 and the Departments of Pathobiology and Microbiology, University of Washington, Seattle, Washington 98195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.