Source:http://linkedlifedata.com/resource/pubmed/id/10395686
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1999-7-29
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| pubmed:abstractText |
CD4+ T cells transfected with the C-terminal 130 aa of human IL-16 are rendered resistant to HIV infection. Whether the constitutively expressed IL-16 acts intracellularly, extracellularly, or both is not clear. To address this question and to further study the processing of IL-16, new constructs containing either the C-terminal 130 aa or the C-terminal 100 aa (PDZ-like motif) were constructed with and without a signal peptide. Pulse-chase experiments and treatment of cells with brefeldin A and/or tunicamycin showed that IL-16 is secreted despite the absence of a signal peptide, but with a signal peptide IL-16 is processed through the endoplasmic reticulum-golgi pathway and is glycosylated. Cells expressing IL-16 linked to a signal peptide secrete considerably more IL-16 into the supernatant than cells expressing IL-16 without a signal peptide and are considerably more resistant to HIV replication. Resistance extends to almost 25 days for cells expressing IL-16 with signal peptide as compared with only 15 days for cells without signal peptide. Cells expressing the C-terminal 100 aa not linked to a signal peptide are poor secretors of IL-16 and show little if any resistance to HIV. In contrast, cells expressing the C-terminal 100 aa linked to a signal peptide secrete IL-16 and are resistant to HIV replication. It is concluded that the secretion of IL-16 is required for HIV inhibition.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-16,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
163
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
906-12
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10395686-Amino Acid Sequence,
pubmed-meshheading:10395686-Amino Acids,
pubmed-meshheading:10395686-Antiviral Agents,
pubmed-meshheading:10395686-CD4-Positive T-Lymphocytes,
pubmed-meshheading:10395686-Extracellular Space,
pubmed-meshheading:10395686-Genetic Vectors,
pubmed-meshheading:10395686-Glycosylation,
pubmed-meshheading:10395686-HIV-1,
pubmed-meshheading:10395686-Humans,
pubmed-meshheading:10395686-Interleukin-16,
pubmed-meshheading:10395686-Intracellular Fluid,
pubmed-meshheading:10395686-Jurkat Cells,
pubmed-meshheading:10395686-Molecular Sequence Data,
pubmed-meshheading:10395686-Peptide Fragments,
pubmed-meshheading:10395686-Protein Processing, Post-Translational,
pubmed-meshheading:10395686-Protein Sorting Signals,
pubmed-meshheading:10395686-Recombinant Fusion Proteins,
pubmed-meshheading:10395686-Transfection,
pubmed-meshheading:10395686-Virus Replication
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| pubmed:year |
1999
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| pubmed:articleTitle |
Processing, secretion, and anti-HIV-1 activity of IL-16 with or without a signal peptide in CD4+ T cells.
|
| pubmed:affiliation |
Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental Research, Bethesda, MD 20892, USA.
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| pubmed:publicationType |
Journal Article,
Comparative Study
|