The Experts below are selected from a list of 48 Experts worldwide ranked by ideXlab platform
Michael Reth - One of the best experts on this subject based on the ideXlab platform.
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the products of pre b cell specific genes lambda 5 and vpreb and the ImMunoglobulin Mu Chain form a complex that is transported onto the cell surface
Journal of Experimental Medicine, 1990Co-Authors: Takeshi Tsubata, Michael RethAbstract:We constructed expression vectors coding for the two pre-B-specific genes, VpreB and lambda 5, and transfected them together with a Mu vector (Mu tm) into Ig- myeloma cells. In a transfectant expressing all three introduced genes, the Mu tm Chain is transported on the cell surface. A biochemical analysis demonstrated that, in these cells, the Mu tm Chain is associated noncovalently with an 18-kD protein and covalently with a 22-kD protein, which are most likely the products of VpreB and lambda 5, respectively. Our results, thus, strongly suggest that the products of lambda 5 and VpreB bind to Mu Chains and have the same capacity as conventional Ig L Chains to allow surface expression of Mu Chains.
Tasuku Honjo - One of the best experts on this subject based on the ideXlab platform.
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the human s Mu bp 2 a dna binding protein specific to the single stranded guanine rich sequence related to the ImMunoglobulin Mu Chain switch region
Journal of Biological Chemistry, 1993Co-Authors: Yosho Fukita, T R Mizuta, M Shirozu, Kazuo Ozawa, Akira Shimizu, Tasuku HonjoAbstract:Abstract We have cloned the cDNA encoding the human homologue of S Mu bp-2, which binds to single-stranded DNA with 5'-phosphorylated guanine-rich sequences related to the ImMunoglobulin Mu Chain switch (S Mu) region. The deduced amino acid sequences of the mouse and human S Mu bp-2 are 76.5% homologous and contain motifs conserved among helicases. We have identified a domain essential for DNA binding at residues 638-786. The binding domain is less conserved (63% homologous) than the putative catalytic domain of N-terminal half containing most of the helicase motifs (85% homologous). The human and mouse S Mu bp-2 have similar, although slightly different, binding specificities. Although the mouse S Mu bp-2 preferentially binds to the mouse S Mu motif (GGGGT), the human S Mu bp-2 binds equally well to the human (GGGCT) and mouse S Mu motifs. The human S Mu bp-2 gene was mapped to chromosome 11 q13.2-q13.4 by in situ hybridization.
David A. Ferrick - One of the best experts on this subject based on the ideXlab platform.
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Characterization of horse (Equus caballus) ImMunoglobulin Mu Chain-encoding genes
Immunogenetics, 1997Co-Authors: M. D. Schrenzel, Donald P. King, Mark L. Mcknight, David A. FerrickAbstract:Horse ( Equus caballus ) ImMunoglobulin Mu Chain-encoding ( IgM ) variable, joining, and constant gene segments were cloned and characterized. Nucleotide sequence analyses of 15 cDNA clones from a mesenteric lymph node library identified 7 unique variable gene segments, 5 separate joining segments, and a single constant region. Based on comparison with human sequences, horse variable segments could be grouped into either family 1 of ImMunoglobulin ( Ig ) clan I or family 4 of Ig clan II subclan IV. All horse sequences had a relatively conserved 16 base pair (bp) segment in framework 3 which was recognized with high specificity in polymerase Chain reaction by a degenerate oligonucleotide primer. Horse complementarity determining regions (CDR) had considerable variability in predicted amino acid content and length but also included the presence of relatively conserved residues and several canonical sequences that may be necessary in formation of the β Chain main structure and conformation of antigen-binding sites through interaction with light Chain CDR. Sequence analysis of joining regions revealed the presence of nearly invariant 3′ regions similar to those found in human and mouse genes. A single horse IgM constant region comprising 1472 bp and encoding 451 residues was also identified. Direct comparison of the horse constant region predicted amino acid sequence with those from eleven other species revealed the presence of 53 invariant residues with particularly conserved sequences within the third and fourth exons. Phylogenetic analysis using a neighbor-joining algorithm showed closest similarity of the horse Mu Chain-encoding constant region gene to human and dog sequences. Together, these findings provide insights into the comparative biology of IgM as well as data for additional detailed studies of the horse imMune system and investigation of imMune-related diseases.
Hermann Eibel - One of the best experts on this subject based on the ideXlab platform.
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b cell tolerance in mice transgenic for anti cd8 ImMunoglobulin Mu Chain
Journal of Experimental Medicine, 1991Co-Authors: Frank Brombacher, Georges Kohler, Hermann EibelAbstract:To analyze in vivo the induction of B cell tolerance against a T cell surface antigen, we generated transgenic mice expressing an anti-CD8.2 Mu heavy Chain gene. We show that self-specific B cells are efficiently tolerized if they express the membrane-bound form of the transgenic Mu Chain on their surface but that they can escape tolerization if they express only the secreted form. In the latter, we find an enhanced expression of anti-CD8.2 antibodies after polyclonal B cell activation. As a result, transgenic anti-CD8.2 antibodies bind to the CD8+ T cells but they did not induce their elimination. Furthermore, we observed the preferential expression of a limited subset of endogenous light Chains with the transgenic Mu Chain. This suggests a positive or negative selection for particular heavy and light Chain combinations in B lymphocytes.
Takeshi Tsubata - One of the best experts on this subject based on the ideXlab platform.
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the products of pre b cell specific genes lambda 5 and vpreb and the ImMunoglobulin Mu Chain form a complex that is transported onto the cell surface
Journal of Experimental Medicine, 1990Co-Authors: Takeshi Tsubata, Michael RethAbstract:We constructed expression vectors coding for the two pre-B-specific genes, VpreB and lambda 5, and transfected them together with a Mu vector (Mu tm) into Ig- myeloma cells. In a transfectant expressing all three introduced genes, the Mu tm Chain is transported on the cell surface. A biochemical analysis demonstrated that, in these cells, the Mu tm Chain is associated noncovalently with an 18-kD protein and covalently with a 22-kD protein, which are most likely the products of VpreB and lambda 5, respectively. Our results, thus, strongly suggest that the products of lambda 5 and VpreB bind to Mu Chains and have the same capacity as conventional Ig L Chains to allow surface expression of Mu Chains.
