PubMed Health⌕ Search

Biomedical subjects

Y Chvatchko

Publications and source records attributed to Y Chvatchko.

25 records · Page 2Linked to original sources
PubMed1990

CD8+ T cells respond clonally to Mls-1a-encoded determinants.

T cell responses to the product of the minor lymphocyte stimulatory locus Mls-1a involve the selective use of TCR V beta domains (especially V beta 6 and V beta 8.1) and are generally considered to be restricted to the CD4+ mature subset. We show here that CD8+ (presumably MHC class I-restricted) T cells bearing V beta 6 or V beta 8.1 also respond preferentially to Mls-1a determinants either in vitro (in mixed leukocyte cultures) or in vivo (in an adoptive transfer system). In vitro responses of both CD4+ V beta 6+ and CD8+ V beta 6+ cells to Mls-1a were dependent upon the MHC haplotype of the stimulator cells, with I-E+ (H-2d or H-2k) alleles being much more stimulatory than I-E- (H-2q). These data strengthen the analogy between Mls gene products and other MHC class II-dependent superantigens such as the bacterial enterotoxins.

Animals↗
PubMed1986

Two yeast mutants defective in endocytosis are defective in pheromone response.

We have purified biosynthetically labeled alpha-factor secreted from transformed yeast alpha cells. This alpha-factor binds specifically to a cells and is internalized by a time-, temperature-, and energy-dependent process. alpha-factor is internalized in an intact form and then rapidly degraded. Two yeast mutants defective in the accumulation of an endocytotic marker, lucifer yellow CH, in the vacuole have been isolated. end1 accumulates invaginations of the plasma membrane, and end2, an internal membrane-bound organelle. One of these mutants, end1, is defective for internalization of alpha-factor. Both of these mutants are defective in pheromone response.

Cell Membrane↗
PubMed1984

Internalization and recycling of insulin receptors in hepatoma cells. Absence of regulation by receptor occupancy.

Insulin receptors of Fao hepatoma cells were labelled with a 125I-labelled photoreactive insulin analogue or by surface iodination catalysed by lactoperoxidase. Cells were then incubated at 37 degrees C, and the cellular localization of the labelled receptors was assessed by limited exposure of intact cells to trypsin. The results show that: (1) photolabelled insulin-receptor complexes are internalized and recycled in Fao hepatoma cells; (2) the dynamics of photolabelled insulin receptors (internalization and recycling) is similar before and after down-regulation; (3) the unoccupied receptors labelled by surface iodination are internalized and recycled similarly to covalent insulin-receptor complexes; (4) insulin does not induce internalization of surface-iodinated insulin receptors. We conclude that internalization and recycling of insulin receptors are independent of receptor occupancy by insulin in Fao hepatoma cells.

Affinity Labels↗
PubMed1984

Subunit arrangement of insulin receptors in hepatoma cells.

Insulin receptors from rat hepatoma cells were studied by the three following methods. Firstly, the alpha subunit (Mr 130000) was labelled using a 125I-photoreactive insulin analogue and UV irradiation. Secondly, using phosphorylation of partially purified and immunoprecipitated receptors with [gamma-32P]ATP, the beta subunit (Mr 95000) was labelled. Thirdly, both alpha and beta subunits were labelled by surface iodination catalysed by lactoperoxidase followed by cell solubilization and immunoprecipitation of the receptor with anti-receptor antibodies. The results show that the native insulin receptor exists under different forms: free alpha and beta subunits and the following combinations of disulphide-linked oligomers: alpha beta, alpha 2, alpha 2 beta and alpha 2 beta 2. In addition, it appears that there is at least one insulin binding site per alpha subunit, and that the alpha and beta subunits may be in close physical association in the plasma membrane even when they are not linked by disulphide bonds. In intact cells, only the alpha subunit is sensitive to extracellular proteases that cleave preferentially the region of the alpha subunit bearing the sulphydryl groups responsible for the interchain binding.

Animals↗
PubMed1983

Immunoprecipitation of insulin receptors by antibodies against Class 1 antigens of the murine H-2 major histocompatibility complex.

Insulin receptors from C57BL/6J mouse (H-2b) liver membranes were specifically labeled with 125I-photo-reactive insulin by UV irradiation. Membranes were solubilized and the capacity of various antibodies reacting with the major histocompatibility complex to immunoprecipitate insulin receptors was tested. About 5% of the labeled receptors were immunoprecipitated by a conventional mouse antiserum against H-2b histocompatibility antigens and by a monoclonal antibody against Class 1 antigens of the H-2b haplotype (Kb and Db). No immunoprecipitation was obtained with a monoclonal antibody against Class 2 antigens of I-Ab or against Class 1 antigens of the H-2k haplotype. Insulin receptors can thus be specifically immunoprecipitated by antibodies against class I histocompatibility antigens.

Animals↗
PubMedDate not supplied

The subunit structure of the insulin receptor and molecular interactions with major histocompatibility complex antigens.

Insulin receptors were labeled with 125I-photoreactive insulin (specifically labeling alpha-subunits) and by insulin-stimulated autophosphorylation (specifically labeling beta-subunits). The results show that the insulin receptor exists under different free and disulfide-linked combinations of alpha and beta subunits. Moreover, the insulin receptor is closely associated to class I antigens of the major histocompatibility complex to form a high molecular weight multi-molecular membrane complex.

Adenosine Triphosphate↗