Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibodies (MoAb) were prepared by fusing spleen cells from BALB/c mice immunized with rat renal cortical homogenates to the mouse myeloma cell. One of them, designated MoAb26-3, revealed a positive antinuclear activity by screening an indirect immunofluorescence test on kidney cryostat sections. The reactivity of MoAb26-3 with double-stranded deoxyribonucleic acid (dsDNA) was confirmed by the Crithidia luciliae assay. The isotype of MoAb26-3 was determined to be IgM-kappa. To test the nephritogenicity of MoAb26-3, the hybridomas were grafted intraperitoneally into BALB/c mice. A deposition of IgM was observed along the base of the epithelial foot processes and on the luminal surface of the endothelium by immunoelectron microscopy. By direct enzyme-linked immunosorbent assay (ELISA), MoAb26-3 was shown to react not only with dsDNA but also with fraction 1A of renal cortical supernatant (F x 1A) and heparan sulfate. On the basis of inhibition ELISA, the dsDNA inhibited F x 1A and heparan sulfate binding of MoAb26-3 and F x 1A blocked the reactivity of Mo26-3 with dsDNA and heparan sulfate, while heparan sulfate showed a less inhibition on the binding of MoAb26-3 with F x 1A, dsDNA, and even with heparan sulfate. Using immunoprecipitation with radiolabeled F x 1A, MoAb26-3 was shown to react with MW 330,000, 440,000, and 700,000 bands which were the same with those which polyclonal Heymann nephritis serum could react. An intravenous injection of MoAb26-3 to rats resulted in the deposition of IgM along the glomerular capillary wall, but resulted in an only transient appearance of proteinuria.
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PMID:Characterization of a polyreactive monoclonal antibody to dsDNA, F x 1A, and heparan sulfate generated from BALB/c mice immunized with rat renal homogenates. 247 May 41

An IgG2a monoclonal antibody (MoAb) reacting with the brush border of the renal proximal tubule and glomerular capillary wall was produced by fusion of NS1 myeloma cells with spleen cells from BALB/c mice immunized with renal brush border preparations from rat kidney cortex. This antibody reacts with a 90,000 mol. wt protein which can be isolated by immunoprecipitation of radiolabelled brush border or glomerular preparations and localized on these structures by immunoperoxidase electron microscopy, thus demonstrating the presence of common antigenic determinants. Survey of various organs showed that the MoAb reacted with the brush border of the gut, but also with antigens associated with the distal vascular system. In the liver antigenic determinants were located along the sinusoid walls but mainly on bile canaliculi. Specific glomerular binding could be demonstrated in vivo by immunofluorescence after an intravenous injection of 2 mg of antibody or by paired label methodology using tracer amounts. Kinetics however were dramatically different from those observed in classical passive Heymann nephritis since glomerular binding was transient during the first hours after injection. Binding was also found in tubular structures, as well as in lung, liver, spleen and heart. These results identify a well defined antigen-antibody system responsible for the formation of transient extramembranous glomerular deposits and may be relevant to some human cases of glomerulonephritis. They may also provide new models to study glomerular and tubular transfer of membrane bound antibodies.
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PMID:A monoclonal antibody to brush border and passive Heymann nephritis. 636 76