Structural evidence that the small subunit found associated with the TL antigen is β 2-microglobulinYokoyama, Kazushige; Stockert, Elisabeth; Old, Lloyd; Nathenson, Stanley
doi: 10.1007/BF00347048pmid: 6179864
Comparative tryptic peptide mapping and partial amino-terminal primary sequence analysis of the light chain component associated with the TL antigens showed that the small subunit of TL was identical to the β
2m light chain associated with the H-2K or D product of the same strain. Peptide comparison of the β
2m from the Tla products of an A strain X-ray induced leukemia RADA1 (Tla
a) and of a C57BL/6 strain X-ray induced leukemia ERLD (Tla
b) showed differences to the extent of 25–35% in their peptides. This is consistent with previous results showing β
2m allelic variations between these mouse strains. The data prove the structural identity of the β
2m molecules from TL and H-2K, D antigens as well as reveal the strain specific polymorphism of the β
2m associated with these products.
A human Thy-1-like antigen expressed on cultured leukemic T-cellsSaji, Fumitaka; Tanigaki, Nobuyuki
doi: 10.1007/BF00347049pmid: 6125472
A human cell membrane antigen that is highly T-cell specific among a number of leukocyte cell lines was isolated from cells of a human T-cell leukemia cell line, SKW-3. In addition to the high specificity to T-cell-type cell lines, the isolated antigen showed the following characteristics: (1) It is an acidic glycoprotein of approximately 30 000 daltons that has a charge heterogeneity and probably a disulfide bond(s); (2) Its antigenicity is stable when treated with heat, acid, and various protein denaturants; (3) It is widely distributed in lymphoid and nonlymphoid tissues but is most predominant in brain. These features are similar, if not identical, to those reported for the Thy-1 antigen of mouse or rat and have raised the possibility that this cell membrane antigen may correspond to human “lymphocyte” Thy-1 antigen, the counterpart of human “brain” Thy-I antigen.
Functional similarities of AeEα Ia molecules as determined by analysis with T-cell clonesBeck, Barbara; Infante, Anthony; Fathman, C.
doi: 10.1007/BF00347050pmid: 6179865
Recognition of AeEα Ia antigens at the functional level was investigated using T-cell clones. The reactivities of an alloreactive and an antigen-reactive clone, both of which recognized AeEα Ia molecules, were compared on a panel of stimulator/antigen-presenting cells of various genotypes. The two clones recognized all tested A
e
b
E
α
x
Ia molecules, where x is a haplotype capable of expressing an Ia.7-bearing Eα polypeptide. Ia antigen recognition by either clone could be inhibited by the monoclonal antibody Y-17, which recognizes a combinatorial serologic determinant on certain AeEα molecules. There were no differences in the recognition of Ia by the alloreactive versus the antigen-reactive clone, suggesting that Ia antigens are recognized by the two clones in a fundamentally similar way. The recognition of these various Ia molecules by the two cloned T-cell lines provides evidence that the Eα polypeptides from H-2 haplotypes k, d, r, and u are functionally indistinguishable.
Further polymorphism of the Tla locus defined by monoclonal TL antibodiesShen, Fung-Win; Chorney, Michael; Boyse, Edward
doi: 10.1007/BF00347051pmid: 7106865
Six new monoclonal TL antibodies are described. At least one new TL antigen is defined (TL.7), and at least one more Tla allele, bringing the total number of known Tla alleles to six. Five of the monoclonal antibodies, and probably all six, identify distinct TL antigenic specificities. Four of these antigens conform in strain distribution and expression on leukemia cells to antigens defined by conventional antisera. The data contain a hint that monoclonal TL antibodies like TL.m6 may serve to identify a region of the Tla gene, which determines whether or not prothymocytes will respond to physiological induction by expressing TL, and thus may provide a means to study the regulatory mechanism that determines whether mouse strains are phenotypically TL+ or TL−
Absence of HLA association or linkage for variations in sensitivity to the odor of androstenonePollack, Marilyn; Wysocki, Charles; Beauchamp, Gary; Braun, David; Callaway, Cynthia; Dupont, Bo
doi: 10.1007/BF00347052pmid: 7201974
Sensitivity to the odor of 5-androst-16-en-3-one (androstenone), a testosterone metabolite, shows wide variations among unrelated individuals. Analysis of correlations in sensitivity between monozygotic twin pairs, dizygotic twin pairs, and nontwin sib pairs now shows that at least a portion of this variation is genetically determined. However, although data from some mouse studies have suggested a relationship between olfaction and the murine histocompatibility system (H-2), we were unable to demonstrate any role of the human HLA system in explaining the wide individual variations in human sensitivity to androstenone. An additional analysis of HLA antigens among 61 human mating pairs also provided no evidence that HLA phenotypes play a role in human mating preference. These data fail to support a role for the human HLA system in the recognition of an odorant of potential biological significance.
Molecular weight determination of two genetically linked cell surface murine antigens: ThB and Ly-6Matossian-Rogers, Arpi; Rogers, P.; Ledbetter, J.; Herzenberg, L.
doi: 10.1007/BF00347053pmid: 7106866
Various murine tumor lines were screened by FACS analysis for the surface antigens ThB and Ly-6.2. Positive cell lines were used for immunoprecipitation studies. A monoclonal ThB-specific antibody immunoprecipitated a unique acidic protein of approximately 16 000 daltons from several positive tumors and from concanavalin A (Con-A) and LPS activated splenic lymphocytes. Monoclonal Ly-6.2-specific antibody was used to immunoprecipitate a 33 500 dalton protein that was shown to exist in four similarly sized forms with different basic charges. In the course of these studies, the apparent molecular weight of the surface antigen T 30, immunoprecipitated with a monoclonal T 30-specific antibody from the cell line EL4, was found to be approximately 25 000 daltons.