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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-9-30
|
| pubmed:abstractText |
Previous studies have indicated that in HepG2 cells HDL3-signalling involves glycosylphosphatidylinositol (GPI) anchored proteins. HDL3-binding to HepG2 cells was found to be enhanced by cellular preincubation with PI-PLC inhibitors and sensitive to a cellular preincubation with exogenous PI-PLC, suggesting that HDL3 binds directly on GPI-anchored proteins to initiate signaling. Moreover HDL3-binding was found to be partly inhibited by antibodies against the HDL-binding protein (AbHBP). HDL3, when binding to HepG2 cells, promoted the release in the culture medium of a 110 kDa protein that binds AbHBP, while a cellular preincubation with antibodies against the inositol-phosphoglycan (IPG) moiety of GPI-anchor (AbIPG), used to block lipolytic cleavage of the GPI-anchor, inhibits HDL3-induced release of the 110 kDa protein in the culture medium. In [3H]-PC prelabeled HepG2 cells, AbHBP were found to stimulate PC-hydrolysis and DAG generation within 5 min as did HDL3 stimulation. Cellular preincubation with AbIPG was found to inhibit only the HDL3-signal and not the AbHBP-signal, while a prior cellular pretreatment with PI-PLC from Bacillus cereus was found to inhibit the HDL3-and AbHBP-signal. Moreover cellular preincubation with AbHBP for 1 h at 37 degrees C was found to inhibit HDL3-signalling pathways. Our results suggest that in HepG2 cells a 110 kDa protein, which could be HBP, can be anchored to the membrane via GPI, and can function in HDL3-signalling pathways as binding sites.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lipoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/high density lipoprotein binding...,
http://linkedlifedata.com/resource/pubmed/chemical/high density lipoprotein receptors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
21
|
| pubmed:volume |
1358
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
103-12
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9296527-Antibodies,
pubmed-meshheading:9296527-Binding Sites,
pubmed-meshheading:9296527-Carrier Proteins,
pubmed-meshheading:9296527-Glycosylphosphatidylinositols,
pubmed-meshheading:9296527-Humans,
pubmed-meshheading:9296527-Lipoproteins, HDL,
pubmed-meshheading:9296527-Membrane Proteins,
pubmed-meshheading:9296527-Phosphatidylcholines,
pubmed-meshheading:9296527-Phospholipases,
pubmed-meshheading:9296527-RNA-Binding Proteins,
pubmed-meshheading:9296527-Receptors, Lipoprotein,
pubmed-meshheading:9296527-Signal Transduction,
pubmed-meshheading:9296527-Tumor Cells, Cultured
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
HDL3 binds to glycosylphosphatidylinositol-anchored proteins to activate signalling pathways.
|
| pubmed:affiliation |
Unité INSERM 325, Institut Pasteur, Lille, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|