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)

A hybridoma cell line that secretes monoclonal antibody, MAb-ER-Br-1-15-4-18 is established. The MAb is highly specific for estrogen receptor (ER) from human breast tumor cells. In order to raise the antibody, the ER was first isolated from human breast tumor. Mice were immunized with the partially purified ER and the fusion of the spleen cells from the mouse, showing the highest serum titer, with the cells of the NS-1 mouse myeloma line, produced hybrid cells which continuously secreted antibodies specific for ER. Three of the hybridoma cultures which tested strongly positive were cloned using limiting dilution method and one of the cell lines was selected for further study. The recovery of the MAb from the cell culture was done by ammonium sulfate precipitation followed by dialysis and then hydroxylapatite liquid chromatography using linear gradients. The purity of the antibody was checked by polyacrylamide gel electrophoresis. The MAb was isotyped and found to be IgG1. When checked against other antigens the MAb showed a minimal cross-reactivity to ER from rabbit uterus and none to ovalbumin or rat liver ferritin. Further experiments showed that the MAb recognized the ER bound to the hormone and ER in the nucleus of breast tumor cells.
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PMID:Production and characterization of a monoclonal antibody to partially purified estrogen receptor from human breast tumor. 292 8

Monoclonal antibody F30 was produced by the fusion of murine myeloma cell line P3-X63-Ag8-653 with spleen cells from a BALB/C mouse immunized with established human pancreatic cancer cell line (PK-1) and the reaction specificity was analyzed. The antigen recognized by monoclonal antibody F30 was different from HLA-associated antigen, beta 2-microglobulin, fetal bovine serum components, ferritin, AFP, or CEA. Monoclonal antibody F30 reacted with all of six pancreatic cancer cell lines established in our laboratory. Cross-reactivity was detected with a colon cancer cell line or an esophagus cancer cell line among various tumor cell lines tested. No reaction was detected with red blood cells, lymphocytes, or lymphoid and myeloid cell lines. By immunoperoxidase staining of frozen sections, the F30-defined antigen was detected not only on pancreatic cancer cell membrane but also on other adenocarcinomas. In addition, the monoclonal antibody F30 had a more wide-spread distribution on normal epithelial cells in the gastrointestinal organs, respiratory system, and urinary system. F30-defined antigen was composed of two protein components with molecular weight of 190 and 160 K. It was indicated that the antigen was an integral protein in the cell membrane since the antigen was not detected in the spent culture medium of antigen-positive cells.
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PMID:Human pancreatic cancer associated antigen detected by monoclonal antibody. 351 31

A new enzymoimmunoassay, specific for the measurement of placental ferritin (PLF) isotype, has been described. Two monoclonal antibodies (McAbs) with different binding specificities to placental ferritin have been used in this assay. One antibody (CM-G-8) binds to all ferritins, whereas the second (CM-H-9) binds to placental ferritin only. In addition, a second enzymoassay was developed for the measurement of total common serum ferritin using CM-G-8 McAb. Serum levels of total ferritin and PLF were measured in healthy individuals and in patients with lymphoproliferative diseases and multiple myeloma. The majority of normal subjects were deficient in PLF in the serum. Increased serum levels of PLF were observed in patients with Hodgkin's lymphoma and non-Hodgkin's lymphoma of low and intermediate grades, as well as in patients with acute lymphocytic leukemia (ALL). Total ferritin was also elevated in these patients. Chronic lymphocytic leukemia (CLL) and multiple myeloma patients exhibited normal levels of common serum ferritin, whereas PLF in the serum was lacking.
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PMID:New monoclonal antibody enzymoassay for the specific measurement of placental ferritin isotype in hematologic malignancies. 381 52

Six anti-DNA hybridoma autoantibodies were prepared by fusing spleen cells from unimmunized MRL/MpJ/lpr/lpr female mice with BALB/c myeloma cells. The monoclonal antibodies were analyzed by solid-phase ELISA for antigen-binding specificities. Three antibodies (62A2, 85A5, and 43B2) bound ssDNA, TNP-KLH, and recognized an epitope(s) present on insolubilized proteins such as BSA, KLH, ferritin, and insulin. The antibodies bound, with a marked preference, TNP-KLH, either soluble or insoluble. The other three antibodies (35A1, 32C5, and 39D2) bound only ssDNA. However, this binding was inhibited by free flavinic acid. None of the six antibodies bound either cardiolipin or proteoglycans, indicating that they do not recognize the repeating negatively charge units common to cardiolipin, proteoglycans, and DNA. All six monoclonal antibodies were purified by affinity chromatography with TNP-Sepharose. Moreover, both anti-DNA and anti-TNP antibodies from sera of nonautoimmune and autoimmune mice were purified easily on TNP-Sepharose.
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PMID:Murine polyspecific antibodies. I. Monoclonal and serum anti-DNA antibodies cross-reactive with 2,4,6-trinitrophenyl derivatives. 387 76

Ferritin was demonstrated by electron microscopy in bone marrow plasma cells of four patients with multiple myeloma and in one patient with another malignant disease. The ferritin molecules were present in membrane bound vesicles and freely dispersed in the cytoplasm. The plasma cells were often localized around and in close contact with dendritic macrophages, which frequently were laden with ferritin. In some of these plasma cells ferritin was seen at specialized contact zones with macrophage extensions.
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PMID:The ultrastructural localization of iron in human bone marrow plasma cells. 405 Apr 34

We have examined human leukocyte preparations for the presence of surface-bound IgE by electron microscopy. Basophil-enriched leukocytes were reacted with burro anti-IgE, a hybrid antibody to burro IgG and ferritin, and ferritin, with or without prior incubation of the cells with an IgE myeloma protein. In the absence of preincubation with IgE small amounts of ferritin were fixed to the surface of basophils but on no other cells. When cells were preincubated with IgE the amount of ferritin fixation on the basophils was markedly increased and a small amount of ferritin was also bound to platelets but again to no other leukocytes. The distribution of ferritin on the basophil surface appeared dependent upon the temperature at which the cells were kept during and after reaction with the various reagents. Basophil sections from cells kept at 0 degrees C had ferritin bound to the surface membrane in patches distributed around the entire circumference. Basophil sections from cells prepared at room temperature had ferritin distributed assymetrically covering a surface membrane segment one-fifth to one-half of the circumference. In control studies in which monomeric IgG was substituted for the IgE and burro anti-IgG was used instead of burro anti-IgE, no cellular fixation of ferritin was observed.
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PMID:Electron microscopic localization of immunoglobulin E on the surface membrane of human basophils. 410 24

Ferritin conjugates of two plant agglutinins, concanavalin A and ricin, have been used as specific electron microscopic stains for covalently-bound saccharide residues on membrane fragments from a myeloma-cell homogenate. The results indicate that different saccharide residues are uniformly localized to a single surface of each membrane fragment. In particular, the ferritin-concanavalin A conjugate binds exclusively to the cisternal side of membrane fragments of the rough endoplasmic reticulum. If it is postulated that the biogenesis of eukaryotic plasma membranes involves an assembly-line process from precursor intracellular membranes, these observed asymmetric distributions of saccharides on cell membranes can be explained.
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PMID:Distribution of saccharide residues on membrane fragments from a myeloma-cell homogenate: its implications for membrane biogenesis. 411 11

The preparation, properties, and some applications of ferritin conjugates of two plant agglutinins, concanavalin A and Ricinus communis agglutinin, are reported. These conjugates serve as specific electron-dense stains for cell- and membrane-bound saccharide residues of the alpha-D-mannopyranosyl and beta-D-galactopyranosyl configurations, respectively, and as examples of a wide range of ferritin-plant agglutinin conjugates useful as high resolution saccharide stains. By using a technique for preparing flattened membrane specimens, it was found with a variety of mammalian cell plasma membranes (lymphocyte, lymphoma, and myeloma and normal, spontaneously and virally transformed fibroblasts) that the ferritin conjugates were localized exclusively to the exterior face of the membrane, with essentially none found on the cytoplasmic face. On the exterior face the topographical distribution of ferritin conjugates appeared to be random. The asymmetrical distribution of saccharide residues to the outer membrane face can be explained by an "assembly line" process whereby new plasma membrane is made from intracellular precursor membranes. It also suggests that the saccharide-containing components of the plasma membrane do not rotate at any appreciable rate from one membrane surface to the other.
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PMID:The distribution and asymmetry of mammalian cell surface saccharides utilizing ferritin-conjugated plant agglutinins as specific saccharide stains. 412 77

The serum ferritin concentration is increased in both acute myeloblastic leukaemia and Hodgkin's disease. In acute leukaemia the mean concentration is about ten times the normal level and is associated with a high concentration of transferrin-bound iron. In Hodgkin's disease abnormal ferritinaemia is associated with a low concentration of transferrin-bound iron and appears to result from a block of reticuloendothelial iron release. Increased concentrations of circulating ferritin have also been observed in a few cases of chronic leukaemia and myelomatosis.
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PMID:Ferritinaemia in leukaemia and Hodgkin's disease. 451 89

Evidence for recovery of surface membrane and its fusion with Golgi cisternae has been obtained previously in several glandular cells. This study was conducted to determine whether or not membrane is similarly retrieved from the surfaces of plasma cells from lymph nodes (of rats immunized with horseradish peroxidase [HRP]) and mouse myeloma cells (RPC 5.4 and X63 Ag 8 cell lines). Electron-dense tracers (cationic and anionic ferritin, HRP) were used to trace the pathways followed by surface membrane recovered by endocytosis, and immunocytochemistry was used to identify the secretory compartments. When plasma cells or myeloma cells were incubated with cationized ferritin (CF), it bound to the cell surfaces and was taken up in endocytic vesicles, for the most part bound to the vesicle membrane. After 30-60 min, it was found increasingly within lysosomes and in several secretory compartments- notably in multiple stacked Golgi cisternae and secretory vacuoles. By immunocytochemistry the secretory product (immunoglobulins) and CF could be demonstrated in the same Golgi components. When myeloma cells were incubated with native (anionic) ferritin or in HRP, these tracers were taken up in much smaller amounts, primarily within the contents of endocytic vesicles. With continued incubation, they appeared only in lysosomes. When cells were doubly incubated, first in CF and then in HRP, both tracers were taken up (often within the same endocytic vesicle), but they maintained their same destinations as when incubated in a single tracer alone: the content marker, HRP, was localized exclusively within the lysosomal system, whereas the membrane marker, CF, was found within elements along the secretory pathway as well as within lysosomes. The findings demonstrate the existence of considerable membrane traffic between the cell membrane and the Golgi cisternae and lysosomes in both normal plasma cells and myeloma cells. Because myeloma cells behave like the glandular cells studied previously with regard to pathways of retrieved surface membrane, they represent a suitable and promising system for further studies of mechanisms and pathways of membrane retrieval and recycling in secretory cells.
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PMID:Pathways followed by membrane recovered from the surface of plasma cells and myeloma cells. 615 78


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