Immunochemical studies on mouse myeloma proteins with specificity for dextran or for levan

Lundblad, Arne; Steller, Richard; Kabat, Elvin A.; Hirst, Judith Wegman; Weigert, Martin; Cohn, Melvin

doi:10.1016/0019-2791(72)90063-8

Cited by 77 publications

(20 citation statements)

References 30 publications

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“…J558 (13) and MOPC104E (12), while demonstrating specificity for a-1,3-linked oligosaccharides, are different as shown by the analysis of inhibition of dextran binding of these proteins by various nigerosyl derivatives. One explanation for the idiotypic difference between these proteins could be that they share certain idiotypic determinants in common, while differing in others.…”

Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 94%

“…Effect of hapten on the J558 idiotype J558 binds to a-1,3-linked dextrans and is inhibitable by the a-1,3-linked disaccharide, nigerose (13). Fig.…”

Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 99%

“…Since both MOPC104E and J558 have specificity for a-1,3-linked oligosaccharides (12,13), it was of particular interest to test MOPC104E for crossreaction with the J558 idiotype by the radioimmunoassay. As shown in Fig.…”

Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 99%

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Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

Carson

Weigert

1973

Proc. Natl. Acad. Sci. U.S.A.

122

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The idiotype of the mouse myeloma protein with anti-a-1,3 dextran activity, J558, has been characterized by a solid-phase radioimmunoassay. The idiotype of the J558 protein depends on a specific light and heavy chain interaction and is altered in the presence of the hapten, nigerose. Cross-reacting idiotypes were found on another mouse myeloma protein with a-1,3 dextran specificity, normal anti-dextran antibody, and certain reconstructed myeloma proteins composed of the J558 heavy chain and heterologous light chains.The immune response to a-1,3-linked dextrans in mice is controlled by an autosomal dominant locus linked to the genes of the constant region of the heavy chain. This locus determines the level of the response to dextrans containing a-1,3 glucosyl linkages, as well as the structure of the antibody. Certain strains that respond well to this antigen produce anti-dextran antibody restricted to the X class. Most or all anti-dextran antibodies share an antigenic determinant(s) (idiotype) that occurs on a 'yAX BALB/c myeloma immunoglobulin with specificity for a-1,3-linked dextrans. Thus, this idiotype provides a marker for the antibody variable region that is coded for by the locus controlling the dextran response (1).In this study, we show that this idiotype is dependent on variable regions of both heavy and light chains; and that the idiotype of the antibodies to the dextrans is related to their specificity, as demonstrated by studies on the influence of hapten, and the effect of amino-acid differences in the complementarity-determining regions of anti-dextran antibodies on the idiotype.

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Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 94%

“…Effect of hapten on the J558 idiotype J558 binds to a-1,3-linked dextrans and is inhibitable by the a-1,3-linked disaccharide, nigerose (13). Fig.…”

Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 99%

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Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

Carson

Weigert

1973

Proc. Natl. Acad. Sci. U.S.A.

122

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“…Culture medium was Iscove's modified Dulbecco's medium supplemented with 10% fetal calf serum, antibiotics, concanavalin A-induced rat spleen cell supernatant and 25 mM methyl-a-D-mannoside. Hy5.19Ag8 is a TNP-specific B hybridoma derived from BALB/c producing IgGl,x [15]; J558 is a B cell tumor also of BALB/c origin producing IgA,h with specificity for a(l-+3)dextran [16].…”

Section: Cell Linesmentioning

confidence: 99%

“…In this case excess antibody-TNP would favor binding to and coating of either CTL or B cells rather than their bridging. As a specificity control, we used the B cell tumor J558, a non-TNP-specific line also of BALB/c origin [16]. This target, which is readily killed by CTL recognizing it, was not killed by DQ23 at any concentration of F23.1-F(ab')2-TNPlo tested (Fig.…”

Section: Analysis Of Ctl Bridging To B Cell Hybridomasmentioning

confidence: 99%

Targeting cytotoxic T cells to antigen‐specific B lymphocytes

Rammensee¹,

Julius²,

Nemazee³

et al. 1987

Eur J Immunol

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A recent development in immunomanipulation involves the targeting of cytotoxic T lymphocytes (CTL) to cell-bound antigens using bispecific antibodies. These antibodies have been engineered such that specificity is directed against the T cell receptor (TCR) or TCR-associated T3 molecules, as well as against the chosen antigen. The present study was aimed to force interactions between T and B cells by bridging their receptors. F23.1 antibodies, which are specific for gene products of the TCR V beta 8 gene family, were conjugated with TNP (2,4,6-trinitrophenyl) and this construct was used to bridge the receptors of V beta 8+ T cells with the receptors of TNP-specific B cells. The bridging was demonstrated by direct killing of both a TNP-specific B hybridoma and of blast cells from mice transgenic for mu, kappa of the TNP-specific antibody Sp6. Further, F23.1-TNP constructs in conjunction with V beta 8+ CTL were shown to specifically deplete Ig-secreting B cells from Sp6 transgenic mice. Conjugates of TCR-specific antibodies and antigen are theoretically useful in vivo to either deplete or expand B cells of a given specificity by coupling their receptors to the TCR of CTL or T helper cells, respectively.

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Characterization of mouse mast cell protease-8, the first member of a novel subfamily of mouse mast cell serine proteases, distinct from both the classical chymases and tryptases

et al. 1998

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Using a recently developed PCR-based strategy, a cDNA encoding a novel mouse mast cell (MC) serine protease (MMCP-8) was isolated and characterized. The MMCP-8 mRNA contains an open reading frame of 247 amino acids (aa), divided into a signal sequence of 18 aa followed by a 2-aa activation peptide (Gly-Glu) and a mature protease of 227 aa. The mature protease has an M(r) of 25072, excluding post-translational modifications, a net positive charge of +12 and six potential N-glycosylation sites. MMCP-8 showed a high degree of homology with mouse granzyme B in the critical regions for determining substrate cleavage specificity, indicating that MMCP-8, similar to granzyme B, preferentially cleaves after Asp residues. A comparative analysis of the aa sequence of MMCP-8 with other hematopoietic serine proteases shows that it is more closely related to cathepsin G and T cell granzymes than to the MC chymases. We therefore conclude that MMCP-8 belongs to a novel subfamily of mouse MC proteases distinct from both the classical chymases and tryptases. Southern blot analysis of BALB/c genomic DNA indicated that only one MMCP-8 gene (or MMCP-8 like gene) is present in the mouse genome. Northern blot analysis of rodent hematopoietic cell lines revealed high levels of MMCP-8 mRNA in a mouse connective tissue MC-like tumor line. However, MMCP-8 mRNA could not be detected in mouse liver, intestine, lung or ears, indicating very low expression in normal tissues. Analysis of the expression of different MMCP in the tissues of Schistosoma mansoni-infected BALB/c mice showed a strong increase in MMCP-8 levels in the lungs but not in the intestines of infected animals, suggesting the presence of a novel subpopulation of MC in the lungs that expressed MMCP-8, either alone or in combination with MMCP-5 and carboxypeptidase A. The dramatic increase in MMCP-1 and MMCP-2 levels but not of MMCP-8 in the intestines of parasitized animals also shows that MMCP-8 is not expressed in mucosal MC in the mouse. This latter is in clear contrast to what has been observed in the rat where the MMCP-8 homologues, RMCP-8, -9 and -10, can be considered as true mucosal MC proteases.

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Immunochemical studies on mouse myeloma proteins with specificity for dextran or for levan

Cited by 77 publications

References 30 publications

Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

Targeting cytotoxic T cells to antigen‐specific B lymphocytes

Characterization of mouse mast cell protease-8, the first member of a novel subfamily of mouse mast cell serine proteases, distinct from both the classical chymases and tryptases

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