rdf:type |
|
lifeskim:mentions |
umls-concept:C0011065,
umls-concept:C0017262,
umls-concept:C0023690,
umls-concept:C0039194,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0253023,
umls-concept:C0441889,
umls-concept:C0699040,
umls-concept:C1332714,
umls-concept:C2911684
|
pubmed:issue |
11
|
pubmed:dateCreated |
1998-4-20
|
pubmed:abstractText |
Cross-linking of cell surface CD4 molecules by anti-CD4 mAb or HIV-1 gp120/anti-gp120 Ab primes resting T lymphocytes for activation-induced cell death (AICD) triggered via the CD3/TCR complex. In striking contrast, we demonstrate here that preincubation of activated human CD4+ T cells with anti-CD4 mAb consistently inhibited AICD triggered via anti-CD3 mAb or Staphylococcus aureus enterotoxin A superantigen. Inhibition of AICD of CD4+ T cell clones was also observed with F(ab')2, but not with Fab, of anti-CD4 mAb. Moreover, soluble HIV-1 gp120, but not rIL-16, inhibited AICD stimulated by S. aureus enterotoxin A. In susceptible clones, CD4 ligation prevented the up-regulation of Fas ligand mRNA and cell surface expression in response to anti-CD3 mAb or superantigen stimulation. CD3/TCR-dependent protein tyrosine phosphorylation and cytokine production were also prevented by preceding CD4 ligation. The inhibition of AICD due to the prevention of Fas ligand upregulation reveals a novel immunoregulatory consequence of CD4 ligation that might play a role in HIV infection and in the therapeutic application of anti-CD4 mAb.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/FASLG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fas Ligand Protein,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-16,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin A, Staphylococcal
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0022-1767
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
159
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5742-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9548519-Antibodies,
pubmed-meshheading:9548519-Antigens, CD4,
pubmed-meshheading:9548519-CD4-Positive T-Lymphocytes,
pubmed-meshheading:9548519-Cell Death,
pubmed-meshheading:9548519-Cytokines,
pubmed-meshheading:9548519-Enterotoxins,
pubmed-meshheading:9548519-Fas Ligand Protein,
pubmed-meshheading:9548519-HIV Envelope Protein gp120,
pubmed-meshheading:9548519-Humans,
pubmed-meshheading:9548519-Interleukin-16,
pubmed-meshheading:9548519-Lymphocyte Activation,
pubmed-meshheading:9548519-Membrane Glycoproteins,
pubmed-meshheading:9548519-Phosphorylation,
pubmed-meshheading:9548519-Receptors, Antigen, T-Cell,
pubmed-meshheading:9548519-Staphylococcus aureus
|
pubmed:year |
1997
|
pubmed:articleTitle |
Ligation of cell surface CD4 inhibits activation-induced death of human T lymphocytes at the level of Fas ligand expression.
|
pubmed:affiliation |
Department of Immunology, Paul Ehrlich Institute, Langen, Germany.
|
pubmed:publicationType |
Journal Article
|