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)

Bacterial strains of Haemophilus species and Streptococcus pneumoniae were examined for synthesis of the enzyme immunoglobulin A1 (IgA1) protease. Of 36 H. influenzae strains examined, 35 produced IgA1 protease; strains included all six capsular types, unencapsulated variants of types b and d, and untypable H. influenzae. Eight Haemophilus strains (non-H. influenzae) were studied, and two produced IgA1 protease. All 10 strains of S. pneumoniae produced IgA1 protease; these strains included 9 different capsular polysaccharide types and 1 untypable strain. Both IgA1 proteases cleaved myeloma IgA1 and secretory IgA but not myeloma IgA2, IgM, or IgG as determined by immunoelectrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that both enzymes cleaved IgA1 myeloma sera, but not IgA2, into two fragments. The apparent molecular weight of the cleaved fragments was dependent both on the apparent molecular weight of the cleaved fragments was dependent both on the specific IgA1 protease assayed and the specific IgA1 substrate utilized. It is postulated that both carbohydrate variation between the IgA1 substrates studied and the ability of S. pneumoniae glycosidases to cleave carbohydrates from glycoprotein offer an explanation for the different fragment sizes observed.
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PMID:Immunoglobulin A1 protease production by Haemophilus influenzae and Streptococcus pneumoniae. 4 Aug 80

Amyloid proteins are probably derived from a variety of precursor glycoproteins. It is postulated that there may be at least two key events in the pathogenesisi of amyloidosis. The first is an increase in the load of glycoprotein being brought to a site of degradation. In the case of myeloma this might be in the form of excess immunoglobulin light chains. In the case of secondary amyloidosis the form taken could be enzyme-alpha-globulin complexes. The second is an inability of the degrading site to handle the arriving substrate at a sufficiently rapid rate, the rate limiting step being at some point along the degradation pathway. We postulate that an acquired enzyme deficiency prevents removal of the carbohydrate moiety of the presented glycoprotein. This results in the accumulation of a normal intermediate (amyloid protein) during the breakdown of the glycoprotein substrate. Evidence for the operation of these mechanisms is discussed and their detailed nature and implications considered.
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PMID:The pathogenesis of amyloid deposition: a new hypothesis. 6 2

A cell hybrid has been selected from fusion of a mouse myeloma and rat spleen cells immunized against mouse lymphoma cells that produces monoclonal antibody against the mouse lymphocyte surface glycoprotein, T200. Antibody binding assays employing the monoclonal antibody show that there are about 50,000-100,000 molecules of T200 glycoprotein on mouse thymocytes and that similar antigens are present on spleen and bone marrow but not detected on nonlymphoid tissues. Examination of the labeled molecules precipitated from detergent extracts of spleen cells and thymocytes iodinated by the lactoperoxidase technique by SDS-PAGE confirm that there are structural differences between the antigens found on B and T lymphocytes. The B-cell glycoprotein consists of at least one component of apparent mol wt 220,000 on SDS-PAGE, while the T-cell glycoprotein has an apparent mol wt of about 190,000.
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PMID:Interspecies spleen-myeloma hybrid producing monoclonal antibodies against mouse lymphocyte surface glycoprotein, T200. 7 61

A monoclonal anti-beta 2-microglobulin (BBM.1 antibody) was produced by cell fusion between the mouse myeloma, P3-X63-Ag8, and spleen cells from a BALB/c mouse immunized with Molt 4, a human T cell line. BBM.1 antibody was fully inhibited by soluble beta 2-microglobulin and purified HLA-A, B antigens and reacted with human-mouse somatic cell hybrids only if they had chromosome 15 and expressed human beta 2-microglobulin. It was cytotoxic in complement-dependent lysis and of the IgG class. BBM.1 and a monoclonal anti-HLA-A, B, C glycoprotein antibody, W6/32 (Barnstable, C. J. et al., Cell 1978. 14:9.), were used to quantitate relative amounts of beta 2-microglobulin and HLA-A, B, C glycoproteins on different human cell types. Thymocytes and the Molt 4 cell line showed a considerable excess of beta 2-microglobulin over HLA-A, B, C glycoproteins, as measured by W6/32 reactivity. B cell lines, peripheral blood lymphocytes, fibroblasts, a HeLa cell derivative, and HSB2, another T cell line, had equal amounts. Immunological cross-reactions between HLA-A, B, C antigens and beta 2-microglobulin and their homologues in other species were detected with the BBM.1 and W6/32 antibodies. The W6/32 antigenic determinant appears to be more highly conserved than that recognized by the BBM.1 antibody.
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PMID:Characterization of a monoclonal anti-beta 2-microglobulin antibody and its use in the genetic and biochemical analysis of major histocompatibility antigens. 9 22

Human and mouse lymphocytes were surface-labeled by lactoperoxidase-catalyzed iodination, or by galactose oxidase oxidation followed by reduction with tritiated sodium borohydride. The labeled cells were lysed with Nonidet P-40. Proteins binding to Helix pomatia A hemagglutinin (HP) were isolated by affinity chromatography on HP-Sepharose and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography. A major cell surface glycoprotein (apparent mol. wt. 150 000, using reducing conditions) on human lymphocytes was responsible for almost all binding of HP. This protein was present on normal and malignant thymus-derived lymphocytes, e.g. thymocytes, blood T cells and T leukemia cell lines. It was also found on chronic lymphocytic leukemia cells, one null cell leukemia line, one unidentified leukemia line, one lymphoblastoid cell line of B origin and on one stem cell lymphoma line. In contrast, this protein was not found on various B cells at different steps of differentiation, e.g. four B lymphoma lines or one myeloma line. It was also absent from a histiocytic leukemia line. However, two of the four B lymphoma lines and the myeloma line had another HP-binding surface glycoprotein (mol. wt. 200 000) instead of the 150 000 protein. Studies of mouse lymphocytes similarly showed that thymus-derived lymphocytes (normal and malignant) but not normal adult B cells expressed a major HP-binding surface glycoprotein of apparent mol. wt. 130 000 (reducing conditions).
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PMID:Helix pomatia A hemagglutinin: selectivity of binding to lymphocyte surface glycoproteins on T cells and certain B cells. 30 19

Multiple myeloma can be regarded as model disease for quantification of tumor mass, investigation of tumor cell kinetics and of tumor response to therapy. The quantification of the tumor cell number allows evaluation of prognosis and monitoring of disease as well as of therapy induced responses. Treatment of multiple myeloma is primarily based on the alkylating drugs cyclophosphamide and melphalan. In recent years other cytostatic substances, also effective in the treatment of this disorder have been introduced. However, the sensitivity determination of the individual myeloma stem cells seems to be the only possible method which possibly increases the response rate significantly. In accordance with these considerations we have, in preliminary clinical investigations, observed a good correlation between the in vitro determined cytostatic drug sensitivity and the in vivo response to therapy. Further progress in the treatment of multiple myeloma is to be expected with the introduction of interferon into the therapeutic regimen. Administration of this glycoprotein has resulted in significant reduction of tumor mass in more than half of all patients treated up to this time.
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PMID:[New aspects in the clinical course determination and therapy in multiple myeloma]. 55 24

In 92 patients with multiple myeloma and IgG monoclonal proteinemia concentrations of seventeen different serum proteins were specifically determined. Prealbumin, albumin, alpha, HS-glycoprotein, alpha-macroglobulin, transferrin and immunoglobulins IgA, IgM and IgD were significantly decreased in patients with IgG myeloma. On the contrary the means found for the typical acute phase proteins i.e. haptoglobin, orosomucoid and CRP were significantly elevated. No significant differences were demonstrated for less typical acute phase protients, i.e. alpha1-antitrypsin, ceruloplasmin and C3-component as well as for hemopexin and beta2-glycoprotein I. CRP values were strongly elevated in some sera, however in majority of patients they were within the normal limits. Negative correlation was found between monoclonal IgG and the most of the studied proteins inclusive immunoglobulins IgA, IgM and IgD. No correlation was demonstrated between the monoclonal IgG and the triad of typical acute phase proteins. Positive correlation was found between monoclonal IgG and the total serum protein and further among the proteins negatively correlated with monoclonal IgG as well as among the individual acute phase proteins. Explanation of the correlations reported has been suggested.
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PMID:Individual serum proteins and acute phase reactants in monoclonal immunoglobulinopathies (a study in patients with IgG myeloma). 64 23

Two commonly used brands of reagent strip (dipsticks) were evlauated for their sensitivity to Bence-Jones and seven other urinary proteins. Both brands showed significant differences in sensitivity to albumin, glycoprotein, ribonuclease and lysozyme; both were most sensitive to albumin and least sensitive to globulin. Furthermore, their comparative sensitivities to these proteins also differed markedly. These differences in sensitivity could lead to underestimation of protein content in urine specimens. Tests on urines from patients with multiple myeloma showed that a negative urinary dipstick test result did not rule out the presence of the disease.
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PMID:Sensitivity of in vitro diagnostic dipstick tests to urinary protein. 64 3

Production of monoclonal antibodies against a wild strain of rabies virus. Cell fusion of SP 2/O, a murine myeloma against a wild strain of rabies virus has originated five monoclonal antibodies (M.A.) specific for virus nucleocapsid , one M.A. specific for virus glycoprotein and one M.A. specific for a viral membrane protein.
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PMID:[Production of monoclonal antibodies against a wild strain of rabies virus]. 130 44

Opsonic glycoprotein, alpha 2-HS-glycoprotein concentration was studied in the serum of 753 patients with various hematological, malignant, immunological, metabolic, endocrine and liver diseases and 68 healthy controls. Decreased serum alpha 2-HS-glycoprotein levels were detected in patients with acute leukemias, chronic granulocyte and myelomonocyte leukemias, lymphomas, myelofibrosis, multiple myeloma, metastatizing solid tumors, systemic lupus erythematosus, rheumatoid arthritis, acute alcoholic hepatitis, fatty liver, chronic active hepatitis, liver cirrhosis, acute and chronic pancreatitis, and Crohn's disease. Elevated levels were measured in patients with B and NANB/C hepatitis. Further decreased levels were observed in some groups with secondary infections. Serum alpha 2-HS-glycoprotein levels are affected by many factors, influencing the synthesis and elimination of the protein. The detection of serum alpha 2-HS-glycoprotein concentration has no specific diagnostic value as a marker for tumors or other diseases, however, its determination can be useful for the assessment of a non-specific regulator of the host defence.
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PMID:[Diagnostic value of the determination of serum alpha2-HS-glycoprotein]. 140 55


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