Source:http://linkedlifedata.com/resource/pubmed/id/10941932
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
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| pubmed:dateCreated |
2000-12-11
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| pubmed:abstractText |
HIV-1 enters cells through interacting with cell surface molecules such as CD4 and chemokine receptors. We generated recombinant soluble gp120s derived from T-cell line-tropic (T-tropic) and macrophage-tropic (M-tropic) HIV-1 strains using a baculovirus expression system and investigated the association of CD4-gp120 complex with the chemokine receptor and/or other surface molecule(s). For monitoring the co-down-modulations of the CD4-gp120 complex, a cytoplasmic domain deletion mutant (tailless CD4), which is not capable of undergoing down-modulation by itself in response to phorbol ester PMA, was used. Our studies revealed both cell-type and HIV-1 strain-specific differences. We found that T-tropic gp120s were capable of priming co-down-modulation with tailless CD4 by interacting with CXCR4, whereas M-tropic SF162 gp120 could not after PMA treatment even in the presence of CCR5. Among the T-tropic HIV-1 envelopes, IIIB gp120 was the most potent. Furthermore, the ability of gp120 to prime the PMA induced co-down-modulation of tailless CD4 appeared to be dependent on the concentration of the principal coreceptor CXCR4. Nevertheless, the observation that IIIB gp120 strongly primed tailless CD4 co-down-modulation on human osteosarcoma HOS cells that express undetectable levels of surface CXCR4 raised the possibility that membrane component(s) other than those recently identified can be involved in down-modulation of the CD4/gp120 complexes.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogens,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CXCR4,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
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| pubmed:status |
MEDLINE
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| pubmed:issn |
0385-5600
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
44
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
489-98
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10941932-3T3 Cells,
pubmed-meshheading:10941932-Animals,
pubmed-meshheading:10941932-Antigens, CD4,
pubmed-meshheading:10941932-Baculoviridae,
pubmed-meshheading:10941932-COS Cells,
pubmed-meshheading:10941932-Cell Membrane,
pubmed-meshheading:10941932-Down-Regulation,
pubmed-meshheading:10941932-Genetic Vectors,
pubmed-meshheading:10941932-HIV Envelope Protein gp120,
pubmed-meshheading:10941932-HIV-1,
pubmed-meshheading:10941932-HeLa Cells,
pubmed-meshheading:10941932-Humans,
pubmed-meshheading:10941932-L Cells (Cell Line),
pubmed-meshheading:10941932-Mice,
pubmed-meshheading:10941932-Mitogens,
pubmed-meshheading:10941932-Protein Binding,
pubmed-meshheading:10941932-Receptors, CXCR4,
pubmed-meshheading:10941932-Recombinant Fusion Proteins,
pubmed-meshheading:10941932-Tetradecanoylphorbol Acetate
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| pubmed:year |
2000
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| pubmed:articleTitle |
Differential level in co-down-modulation of CD4 and CXCR4 primed by HIV-1 gp120 in response to phorbol ester, PMA, among HIV-1 isolates.
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| pubmed:affiliation |
Department of Immunology, Institute of Basic Medical Sciences, University of Tsukuba, Ibaraki, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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