Disease relevance of Thy1

• Anti-Thy1 nephritis was induced in Wistar rats by injecting mouse anti-rat Thy1 antibodies intravenously [1].
• RESULTS: RGCs comprise 67.5% +/- 6.5% (mean +/- SD) of cells in the ganglion cell layer (GCL) of control mice based on nuclear morphology and the presence of mRNA for the ganglion cell marker Thy1 [2].
• Expression of Thy1, TL and LYT antigens on spontaneous leukemias of BALB/MO strain of mice [3].
• After subcloning into a plasmid vector containing the bacterial Eco-gpt gene as a selectable marker, the Thy-1 gene was introduced into the Thy-1-deficient mouse lymphoma AKR1 (Thy-1-d), and the rat neuronal cell line, B50 [4].
• The Thy-1.2, Lyt-2, and T-30 differentiation antigens were not detected on any B lymphoma or plasmacytoma [5].

Psychiatry related information on Thy1

• Independent and cooperative behavior of Thy1 and CD3:TcR T cell signalling pathways [6].
• RESULTS: We show here that Thy-1 null mice are unable to make the appropriate dietary choice in the test for social transmission of food preference, despite showing a normal level of social interaction with the demonstrator mouse, normal neophobia, and normal learning in a T-maze using scented food as cues [7].
• Analogous to a successful strategy for the production of transgenic animal models for Alzheimer's disease we generated mice expressing wildtype and the A53T mutant of human alphaSN in the nervous system under control of mouse Thy1 regulatory sequences [8].
• Rabbit antisera specific for idiotypic determinants (Id) of monoclonal Thy-1 autoantibodies were tested for their capacity to elicit Id-bearing thymus autoantibodies in mice [9].

High impact information on Thy1

• The phenotype associated with inappropriate developmental regulation of the Thy-1 gene suggests that the Thy-1 antigen may play a role in inducing activation or differentiation events on early lymphocyte progenitor cells [10].
• The Thy-1 antigen is a cell-surface glycoprotein of unknown function expressed on mouse T lymphocytes, neurons, and hematopoietic stem cells [10].
• The results indicate the presence of multiple cis-acting regulators of Thy-1 gene expression that have changed in both their character and arrangement over the course of Thy-1 gene evolution [11].
• A hybrid Thy-1 gene composed of the human coding region with the 5' and 3' flanking regions of the mouse gene was expressed abnormally in a different part of the kidney (the tubular epithelia), which resulted in a proliferative kidney disorder [12].
• The glycosylation defect of Thy-1-mutant lymphomas of the class E complementation group has been identified as a block in the synthesis of the lipid-linked oligosaccharide precursor of the asparagine-linked oligosaccharides of glycoproteins [13].

Chemical compound and disease context of Thy1

• Recombinant bacteriophage and cosmid clones containing the gene for the mouse Thy-1.2 glycoprotein were isolated and characterized [14].
• To demonstrate the kinetics of in vivo activation of murine LCs and DETCs in the elicitation phase of contact hypersensitivity, we measured the cell area positively stained for I-A and gammadeltaT-cell receptor (or Thy-1.2), respectively, under a fluorescence microscope at various time intervals after topical application of dinitrofluorobenzene [15].
• The effect of indomethacin (INDO), a specific inhibitor of prostaglandin (PG) synthesis, on the expression of markers during thymocyte differentiation such as Thy-1, H-2K, and peanut agglutinin (PNA) receptor was examined by immunofluorescence, using poorly differentiated thymoma, EL-4, as the indicator cells [16].
• The surface proteins of Thy-1 positive mouse lymphomas and Thy-1 negative variants were labeled by lactoperoxidase-catalyzed iodination and characterized by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate and by immunological studies [17].
• Essentially all eukaryotic cells, including murine lymphomas, express surface proteins, such as Thy-1, which are anchored by a phosphoinositol mannolipid [18].

Biological context of Thy1

• These antigens include histocompatibility antigens of the H-2 complex (H-2.8 of the K-end and H-2dx(D) of the H-2dx haplotype) and two thymic markers, TL1.2 and Thy1 [19].
• The genes for two other cell surface molecules believed to be involved in cell-cell interactions, Thy-1 and the delta chain of the T3-T cell receptor complex, have recently been localized to the same region of chromosome 11 in man [20].
• The complete exon/intron structure and the nucleotide sequence of the Thy-1.2 gene was determined [21].
• The entire coding sequence of Thy-1 is distributed among three exons, encoding amino acid residues -19 to 8, -7 to 106, and 107 to 143, respectively [22].
• These L-cell lines contain between two and four copies of the cloned Thy-1 gene stably integrated in the host genome [4].

Anatomical context of Thy1

• (a) NK cells do not express Thy1, Ly2, or Ig surface markers [23].
• In addition, while thymic expression of Thy1 is relatively normal, peripheral T cells isolated from Ets-1 mutant mice display a striking loss of Thy1 expression [24].
• Additionally, Thy1 was found to be induced only on those B cell subsets capable of producing IgE [25].
• The combination of saponin and digitonin treatment was also compatible with the staining of sCD3 and other lymphocyte surface antigens such as Thy1, CD4, CD8, B220, and IgM [26].
• 1. In addition, some rapidly renewed bone marrow lymphocytes express low intensities of Thy1 (Thy1lo) [27].

Associations of Thy1 with chemical compounds

• Further studies tested for LPS and IL-4-induced expression of Fc epsilon RII and Thy1 on the various B cell populations [25].
• In each case, the number of null lymphocytes, as defined by a lack of radioautographic labeling of either B220 glycoprotein or Thy1, increased markedly in both the bone marrow and spleen [27].
• Moreover, sulfate glycans could modulate the binding of rat mAb directed at spatially distinct Thy-1 epitopes [28].
• It was shown that 125I-labeled Thy-1 directly bound to immobilized heparin [28].
• By cross-hybridization with a mouse Thy-1 probe, we isolated cDNA clones from a pcD-expression library prepared from mRNA of C5 cells [29].

Physical interactions of Thy1

• Resting murine T cell activation induced by either CD3 complexes or Thy1 molecules was investigated in vitro, using surface-bound anti-CD3 mAb as the stimulus [30].
• Although both of these pathways are initiated by an increased activity of Lyn kinase, the exact mechanism by which Lyn kinase interacts with aggregated FcepsilonRI and Thy-1 is not completely understood [31].
• Differential expression of class II major histocompatibility complex and Thy 1.2 antigens on mouse decidua [32].

Regulatory relationships of Thy1

• The brain T cell cross-reactive, mitogenic determinant is not expressed on Thy-1- mutants of the BW5147 T cell lymphoma that fail to express the Thy-1 molecule but do express other T cell surface proteins such as T-200 and gp 69, 71 [33].
• The majority of cells demonstrating TGF-beta activation and myofibroblast differentiation in bleomycin-induced lesions were Thy-1-negative [34].
• Since the Thy1 triggering pathway has different accessory cell and cytokine requirements than does the CD3: TCR lymphocyte activation pathway, it is possible that immunization was more effective in changing the cellular interactions of the T-lymphocyte than in altering its intrinsic capabilities [35].
• However, the Thy1 pathway is also regulated independently since IL2 production is larger when stimulated by anti-Thy1 than anti-CD3 mAbs [6].
• First, a profound inhibition of primary PFC responses occurs when foreign H-2 antigens are expressed on Thy-1 incompatible donor cells [36].

Other interactions of Thy1

• After serial passage, one Thy 1- tumor altered its cell surface phenotype to Thy 1low B220- [37].
• Analyses of Mus domesticus/M. spretus interspecific backcross mice showed that Cbl-1 maps between the immunoglobulin kappa light chain and T-cell receptor beta chain loci and that Cbl-2 is tightly linked to Thy-1 [38].
• Both fractions were highly enriched in other glycosylphosphatidylinositol-anchored proteins such as NCAM 120 and Thy-1 [39].
• Migration of Thy-1+ dendritic epidermal cells (Thy-1+DEC): Ly48 and TNF-alpha are responsible for the migration of Thy-1+DEC to the epidermis [40].
• In the thymus, BST-1 was expressed on CD4-CD8-CD3- [triple negative (TN)] CD90 (Thy-1)+ cells [41].

Analytical, diagnostic and therapeutic context of Thy1

• Thy1 expression was examined using in situ hybridization [2].
• The predicted amino acid sequence indicates that the mouse Thy-1 molecule contains a 19 amino acid leader peptide and the 112 amino acids reported previously from protein sequence analysis, plus 31 extra amino acids at the carboxyl terminus [22].
• Expression of the neuronal cell surface glycoprotein Thy-1 has been studied during the development of the olfactory bulb in mice and rats, using in situ hybridisation and immunohistochemistry to follow the appearance of Thy-1 mRNA and protein, respectively [42].
• Tumor transplantation experiments demonstrated that the Thy 1.2- tumor cells could reestablish in the thymus and spleen of irradiated hosts, and low level expression of the Thy 1 molecule was observed in the thymus but not the spleen on the first passage [37].
• Flow cytometry of the tumor cells indicated that approximately 50% were positive for Thy 1 [37].

References