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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Amyloidosis was induced in a number of strains of mice by repeated injections of casein and endotoxin. Spontaneous amyloid was obtained from Balb/C mice bearing a myeloma tumor (IgG2a producing MOPC 173 tumor) and from aged SJL/J mice. Both the induced and spontaneous forms were similar in their size, immunological reactivity, peptide maps and in the susceptibility of histological sections to oxidizing agents with or without trypsin digestion. Since case-induced murine amyloid resembles the nonimmunoglobulin from of human amyloid, it is concluded that an immunoglobulin form in mice has yet to be characterized.
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PMID:Similarity of casein- and endotoxin-induced, myeloma- associated and aged SJL/J amyloid in various strains of mice. 8 74

a) Leukocyte chemotactic activity, b) cytotaxic activity of patients' sera and c) influence of patients' sera on chemotactic activity of control leukocytes was studied in 18 patients with multiple myeloma, one patient with monoclonal IgE-gammopathy of undetermined significance and 32 controls. Chemotactic activity of patient leukocytes against Zymosan-activated normal serum and against Casein was reduced significantly. In addition, in 66% of the patients a chemotaxis inhibiting serum factor was observed. The Zymosan-induced generation of cytotaxic factors did not differ in patients or control sera. These data show that leukocyte inherent defects as well as serum factors give rise to reduced leukocyte chemotactic activity in patients with multiple myeloma. This impairment is likely to contribute to the increased susceptibility to infections in that disorder.
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PMID:[Disturbances in granulocyte chemotaxis in patients with multiple myeloma]. 55 23

We have examined some aspects of lymphocyte and macrophage function in experimental murine amyloidosis. Casein-induced murine amyloidosis is a good model for studying secondary human amyloidosis while myeloma-associated murine amyloidosis is a poor model for human myeloma-associated amyloidosis. The amyloid of casein-induced and myeloma-associated murine amyloidosis cross-reacted immunologically. Neither form of amyloidosis was associated with L chain fragments or excess L chain production. Cellular immunologic reactivity of casein-induced amyloidotic mice, as assessed by lymphocyte transformation with mitogens, was abnormal using spleen lymphocytes but completely normal when thymus and peripheral blood lymphocytes were examined. The depressed activity could be attributed to splenic amyloid deposits. Intracellular amyloid was detected in the spleens of casein-injected mice prior to extracellular amyloid deposits. Amyloid containing cells could also be cultured from the spleen in a much higher proportion than that found in vivo. These cells may represent a subpopulation committed to amyloid synthesis.
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PMID:Casein-induced murine amyloidosis: amyloid and immunoglobulin production and proliferative capacity of splenocytes. 81 78

Myeloma-associated and casein-induced murine amyloidosis were used as models to study the role of lymphocytes and macrophages in amyloid formation. Amyloidosis occurred rarely and in small amounts in Balb/C mice with immunoglobulin (Ig)-producing myeloma tumours but large amounts could be induced by injections of casein. Fluorescent staining of both forms of amyloid deposits by means of anti-casein- and anti-myeloma-amyloid antibodies indicated that they either crossreacted or coexisted. Nor abnormality of Ig biosynthesis was detected in amyloidosis, suggesting that abnormal degradation was responsible for production of the Ig form of amyloid. Although spleen lymphocytes of casein-injected mice with amyloidosis demonstrated diminished cellular immunologic responses, this did not indicate generalized immunologic incompetence. The non-Ig form of amyloid in casein-injected mice was shown to be produced by macrophages, and a technique was developed for increasing the yield of amyloid-containing cells.
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PMID:Experimental murine amyloidosis: a model system for studying amyloid formation. 108 Apr 30

Amyloidosis was induced in C57BL mice by daily injections of casein and in BALB/c mice by daily injections of endotoxin. There was no obvious disorder of immunoglobulin biosynthesis by spleen lymphocytes in these mice either before, during the development of, or in the amyloidotic stage. The pattern of immunoglobulin synthesis, assembly, and secretion was unaltered, the relative amount of heavy and light chains produced was normal, and there was an absence of immunoglobulin polypeptide chain fragments. Small amounts of amyloid were present in only 1 of 19 BALB/c and C3H mice (the IgG2a producing MOPC 173 tumor) bearing immunoglobulin-producing myeloma tumors and variants of these tumors. There was no relationship between excess light chain production by tumor plasma cells or spleen lymphocytes and the development of amyloidosis and there were no light chain fragments demonstrable. Antiserum prepared against casein-induced amyloid cross-reacted by immunofluorescence with the amyloid present in the MOPC 173 tumor-bearing mice, indicating the presence of common antigenic determinants in these two forms of amyloid. Attempts to study the biosynthesis of amyloid with incorporation of radioactively labeled amino acids were unsucessful.
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PMID:Immunoglobulin biosynthesis in myeloma-associated and casein- and endotoxin-induced murine amyloidosis. 109 61

Recombinant human interstitial collagenase, an N-terminal truncated form, delta 243-450 collagenase, recombinant human stromelysin-1, and an N-terminal truncated form, delta 248-460 stromelysin, have been stably expressed in myeloma cells and purified. The truncated enzymes were similar in properties to their wild-type counterparts with respect to activation requirements and the ability to degrade casein, gelatin, and a peptide substrate, but truncated collagenase failed to cleave native collagen. Removal of the C-terminal domain from collagenase also modified its interaction with tissue inhibitor of metalloproteinases-1. Hybrid enzymes consisting of N-terminal (1-242) collagenase.C-terminal (248-460) stromelysin and N-terminal (1-233) stromelysin.C-terminal (229-450) collagenase, representing an exchange of the complete catalytic and C-terminal domains of the two enzymes, were expressed in a transient system using Chinese hamster ovary cells and purified. Both proteins showed similar activity to their N-terminal parent and neither was able to degrade collagen. Analysis of the ability of the different forms of recombinant enzyme to bind to collagen by ELISA showed that both pro and active stromelysin and N-terminal collagenase.C-terminal stromelysin bound to collagen equally well. In contrast, only the active forms of collagenase and N-terminal stromelysin.C-terminal collagenase bound well to collagen, as compared with their pro forms.
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PMID:The role of the C-terminal domain in collagenase and stromelysin specificity. 131 62

In an attempt to isolate monoclonal antibodies specific for bovine lymphocytes, spleen cells from mice immunized with bovine lymphocytes were fused with the mouse myeloma cell line SP-2/0. The resulting hybridoma cell lines were tested for reactivity with bovine lymphocytes, polymorphonuclear neutrophils, RBC, gamma-globulin, kappa-casein, beta-casein, alpha-S1-casein, and beta 2-microglobulin (beta 2m) and with beta 2m from rabbits, goats, and human beings. None of the clones secreted anti-bovine lymphocyte-specific antibody. However, 4 secreted monoclonal antibodies to bovine beta 2m. They also reacted with beta 2m from rabbit, goat, and human being. One monoclonal antibody also was found to be reactive with bovine immunoglobulin. Monoclonal antibodies to beta 2m could serve as a tool to (1) explore the homology of the beta 2m molecule among various species, (2) examine the relationship of beta 2 m with the constant region of the immunoglobulin molecule, (3) quantitate bovine beta 2m in various body fluids and major histocompatibility antigens on cell surfaces, (4) help characterize those antigens in cattle, and (5) be used for tissue typing of those antigens.
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PMID:Production and characterization of monoclonal antibodies to bovine beta 2-microglobulin. 304 82

PMN leukocytes from untreated patients with multiple myeloma (MM), Hodgkin's disease (HD) and non-Hodgkin lymphoma (NHL) were studied in vitro for their phagocytic and chemotactic function. Alkaline phosphatase score and the reduction of nitroblue tetrazolium (NBT) in these leukocytes were also determined. Most of the functions of PMN leukocytes from untreated patients with MM were impaired, compared to control leukocytes, while those from patients with HD and NHL were impaired only in their chemotactic response to casein and endotoxin-activated serum (EAS).
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PMID:Functions of polymorphonuclear (PMN) leukocytes of patients with lymphoproliferative diseases. 400 61

Thirteen clones of hybrid cells which synthesize antibodies directed against the Rous sarcoma virus (RSV) transforming protein, pp60src, were isolated. Mouse myeloma cells were fused with spleen cells from mice that had been immunized with purified pp60src from bacterial recombinants which direct the synthesis of the RSV src gene. The hybridomas which survived the selection medium were screened by immunoprecipitation of pp60src from 32P-labeled lysates of RSV-transformed cells. Monoclonal antibodies produced by subclones derived from 13 hybridomas recognized pp60src encoded by the Schmidt-Ruppin and Prague strains of RSV and the cellular homolog of pp60src. Antibody from clone 261 had a high affinity for the viral yes gene product, and antibodies from clones 443 and 463 recognized the transforming proteins encoded by viruses containing the related transforming genes fps and ros. Several other clones had a low affinity for the viral yes, fps, and ros gene products which could be detected by in vitro phosphorylation of the transforming proteins after immunoprecipitation with the monoclonal antibody. All of the monoclonal antibodies allowed phosphorylation of pp60src and casein in an immune complex-bound reaction.
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PMID:Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. 631 92

Rat milk contains at least three major caseins with apparent molecular weights of 41,000 (alpha-casein), 25,000 (beta-casein), and 22,000 (gamma-casein) (estimated in 10% sodium dodecyl sulfate-polyacrylamide gels). These three caseins and alpha-lactalbumin, a major whey protein, were purified from rat milk. The purified caseins and alpha-lactalbumin were used to immunize BALB/c mice, and spleen cells from these mice were hybridized with cells of the mouse myeloma SP-2/0 cell-line. We have isolated a small library of hybridoma cell-lines secreting monoclonal antibodies specific for each of the major caseins and alpha-lactalbumin from rat milk. Antibodies were tested for immunoreactivity with each of the purified milk proteins and with total rat milk proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Some heterogeneity in apparent molecular weight was observed for purified alpha-casein, gamma-casein, and alpha-lactalbumin. Monoclonal antibodies against alpha-casein, gamma-casein, and alpha-lactalbumin recognized all of the molecular weight forms of the antigen for which they were specific. Each monoclonal antibody was specific for one of the caseins or alpha-lactalbumin and did not react with the other caseins or alpha-lactalbumin, suggesting that there is limited structural homology among these proteins. All of the monoclonal antibodies against the rat caseins reacted with components of mouse milk, and the monoclonal antibodies against rat gamma-casein reacted with a component of human milk of apparent molecular weight 27,000. No interspecies reactivity was observed with the antibodies against rat alpha-lactalbumin. These monoclonal antibodies are being used to develop sensitive assays for each of these major rat milk proteins.
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PMID:Immunochemical characterization with monoclonal antibodies of three major caseins and alpha-lactalbumin from rat milk. 670 6


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