Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1990-11-21
pubmed:abstractText
We have examined the expression of TCR genes in 4-hydroxy-3-nitrophenyl-acetyl (NP)-specific Ts cell hybridomas. Each of three independently isolated hybridomas expressed in-frame TCR alpha-chain rearrangements derived from the original suppressor Ts cell. Different V alpha and J alpha gene segments were rearranged and expressed in each Ts cell line. The only TCR beta-chain expressed in these cells was derived from the BW5147 fusion partner. Expression of the BW5147 beta-chain was found to correlate with cell surface Ag binding, inasmuch as subclones derived from one of the original Ts lines expressed greatly reduced levels of beta-chain mRNA and no longer bound to NP-coupled RBC. Subclones that continued to express beta-chain mRNA did bind to NP-coupled RBC. This suggests that the Ag receptor on Ts hybridomas is a TCR-alpha beta dimer composed of a unique alpha-chain and the BW5147 beta-chain. Ag binding could be modulated by preincubation of Ts hybridoma cells with anti-TCR-alpha beta antibody, thereby supporting this conclusion. Suppressor factor activity was measured in the conditioned media of Ts subclones that differed by 250-fold in levels of beta-chain mRNA expression. No difference in suppressor factor activity was found; conditioned media from these subclones suppressed both plaque-forming cell responses and delayed-type hypersensitivity responses at approximately equivalent dilutions. Suppressor factor activity in the conditioned media of both a beta-chain negative subclone and a beta-chain positive subclone could be absorbed with an antibody that recognizes the TCR alpha-chain, but not with an antibody that recognizes the TCR beta-chain. We conclude that suppressor factor activity in the conditioned media of these Ts hybridomas is not derived from surface TCR-alpha beta receptors, although it does share TCR alpha-chain determinants.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
145
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2809-19
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2170525-Amino Acid Sequence, pubmed-meshheading:2170525-Animals, pubmed-meshheading:2170525-Base Sequence, pubmed-meshheading:2170525-Blotting, Northern, pubmed-meshheading:2170525-Blotting, Southern, pubmed-meshheading:2170525-Chromatography, Affinity, pubmed-meshheading:2170525-Cloning, Molecular, pubmed-meshheading:2170525-DNA, pubmed-meshheading:2170525-Gene Rearrangement, alpha-Chain T-Cell Antigen Receptor, pubmed-meshheading:2170525-Gene Rearrangement, beta-Chain T-Cell Antigen Receptor, pubmed-meshheading:2170525-Gene Rearrangement, gamma-Chain T-Cell Antigen Receptor, pubmed-meshheading:2170525-Hybridomas, pubmed-meshheading:2170525-Immune Tolerance, pubmed-meshheading:2170525-Mice, pubmed-meshheading:2170525-Molecular Sequence Data, pubmed-meshheading:2170525-Oligonucleotides, pubmed-meshheading:2170525-Polymerase Chain Reaction, pubmed-meshheading:2170525-RNA, Messenger, pubmed-meshheading:2170525-Receptors, Antigen, T-Cell, pubmed-meshheading:2170525-Suppressor Factors, Immunologic, pubmed-meshheading:2170525-T-Lymphocytes, Regulatory
pubmed:year
1990
pubmed:articleTitle
Expression of functional alpha beta T cell receptor gene rearrangements in suppressor T cell hybridomas correlates with antigen binding, but not with suppressor cell function.
pubmed:affiliation
Genetics Institute, Cambridge, MA 02140.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't