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)

The specificities of five heterophile Hanganutziu and Deicher (HD) antibody-containing sera from four different cancer patients and one other diseased patients were compared. Three glycosphingolipids and one glycoprotein antigens and their chemically modified derivatives were used. The antibodies of all whole sera showed similar specificities. IgG and IgM antibody fractions of each serum were separated. Although antibodies of the same class showed similar specificities, differences were detected between the specificities of IgG and IgM. IgG antibody specificities were dependent on the hydrophobic (ceramide) group while IgM antibodies were directed more to the terminal sialic acid moiety of the glycosphingolipid antigens. The results suggested that a similar population of IgG-producing lymphocytes is stimulated in patients. Due to the similarities in specificities of HD antibodies, the results of this study will facilitate the future isolation of either IgG or IgM antibody-producing lymphocyte(s) from a patient with HD antibodies and the establishment of a monoclonal antibody through hybridization with a human myeloma cell line.
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PMID:Specificities of human heterophile Hanganutziu and Deicher (HD) antibodies to glycosphingolipids and a glycoprotein. 349 Oct 66

We generated a high-affinity and highly specific monoclonal antibody (BL4B11)-producing hybridoma against bullfrog lutropin (LH) beta by fusing mouse myeloma, X63.Ag8.653, with spleen lymphocytes obtained from BALB/c mice immunized with bullfrog LH-IV (pI 9.3) beta-subunit. The resultant antibody-secreting hybridoma was injected into intraperitoneally pristane-primed BALB/c mice to obtain a large amount of antibody. Noncompetitive binding tests revealed that the ascitic fluid (BL4B11) could be diluted up to 1:12,000 for 50% binding to 125I-labeled bullfrog LH beta and also bound strongly to bullfrog intact LH, but not to LH alpha, follitropin (FSH), FSH alpha, FSH beta, and rat glycoprotein hormones (LH, FSH, and thyrotropin (TSH) significantly. The immunoblotting results also showed a similar immunological specificity of BL4B11. Cross-reactivities of bullfrog LH, FSH beta, FSH, LH alpha, and FSH alpha against BL4B11 were 9.69, 3.76, 2.40, 1, and 1%, respectively, when compared with bullfrog LH beta in the competitive inhibition assay system. The affinity constant (Ka) of the BL4B11 was 1.09 X 10(9) M-1. In the sexually mature bullfrog pituitary, immunoreactive LH cells which were revealed by this BL4B11 were distributed throughout the pars distalis except the rostral region. They were especially large, numerous, and polygonal, with well-developed cytoplasm. In the rostral region, immunoreactive LH cells were larger and more intense than those in the central region. In the case of young bullfrog, several immunoreactive LH cells were found only in the dorsocaudal region of the pars distalis. The distribution and histological characteristics of immunoreactive LH cells were different from those of immunoreactive TSH cells revealed by anti-human TSH beta serum.
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PMID:Production and characterization of a monoclonal antibody against the beta-subunit of bullfrog lutropin. 349 61

Spleen cells, from BALB/c mice that had been infected with lactate dehydrogenase-elevating virus (LDV) for 6 days and that had or had not been previously immunized with glutaraldehyde-inactivated LDV, were fused with NS-1 myeloma cells. The fusion frequency was at least 10 times higher than with spleen cells of normal or chronically infected mice. Only 1 of 297 wells containing hybridomas prepared with spleens from unprimed 6-day-infected mice produced LDV-specific monoclonal antibodies (mAb). In contrast, when mice were immunized with inactivated LDV before infection, 33 of 73 hybridoma-containing wells screened were LDV-specific. The mAbs produced were mainly of IgG2a, IgM, and IgG1 subclasses and exhibited an identical characteristic staining pattern of LDV-infected cultured macrophages. A single mAb of IgG2b isotype yielded a different staining pattern. Western blotting showed that all of 12 mAbs analyzed in more detail were specific for the LDV glycoprotein, VP-3, but none of these neutralized the infectivity of the homologous strain of LDV. They also did not significantly protect immunosuppressed 10-month-old C58 mice against LDV-induced paralytic poliomyelitis, as does passive immunization with polyclonal mouse anti-LDV IgG.
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PMID:Characteristics of monoclonal antibodies to the lactate dehydrogenase-elevating virus. 361 May 72

Four stable IgM monoclonal antibody-producing hybridomas were generated by fusing mouse myeloma cells with spleen lymphocytes from C57BL/6 mice hyperimmunized against the syngeneic B16 melanoma. All four monoclonal antibodies (R31/15, R37/4, R37/6, and R37/7), in common with polyclonal antiserum from immunized mice, recognized antigens on the same complex of related cell surface molecules specified by endogenous AKR-type murine leukemia virus, designated the B16-gp/70/80/85 antigen complex. Reactivity with this antigen complex was demonstrated by radioimmunoprecipitation. Specificity for viral Mr 70,000 glycoprotein-related antigens was indicated by absorption of antibody activity by endogenous AKR virus and by inhibition of antibody binding to B16 melanoma cells by monospecific antiserum to murine leukemia virus Mr 70,000 glycoprotein. Neither polyclonal nor monoclonal antibodies recognized antigens on fish, guinea pig, swine, or human melanoma cell lines. Polyclonal antiserum reacted with several other mouse melanomas and with certain mouse lymphoma lines induced by, or harboring, endogenous murine leukemia viruses, but the monoclonal antibodies were unreactive except for recognition of antigens on Harding-Passey mouse melanoma cells by antibody R37/4 and on RL male 1 mouse lymphoma cells by antibody R37/7. Only monoclonal R37/7 was cytotoxic for cultured B16 melanoma cells in an antibody- and complement-dependent assay with guinea pig complement, although all antibodies were cytotoxic with rabbit complement. In reflecting the predominant humoral immune response to the B16 melanoma detected in syngeneic mice during tumor growth, these monoclonal antibodies will permit experimental amplification of that response to help determine how that immunity influences tumor growth and metastatic dissemination.
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PMID:Syngeneic monoclonal antibodies to B16 melanoma viral antigens. 365 42

The Mr 52,000 glycoprotein is regulated by estrogen and released by breast cancer cells in culture (B. Westley and H. Rochefort, Cell, 20: 352-362, 1980). This rare protein was partially purified from 25 liters of medium conditioned by MCF7 cells and injected into Biozzi's selected mice. The spleen lymphocytes of one immunized mouse was fused with the murine myeloma P3-X63-Ag8-653. Sixteen hybridomas producing monoclonal antibodies to the Mr 52,000 protein were isolated, and seven of them were cloned and purified. The seven monoclonal antibodies were all of the immunoglobulin G1 isotype, and their dissociation constants ranged from 0.35 to 2.3 nM. The antibodies specifically recognized the secreted Mr 52,000 protein as evidenced by double immunoprecipitation and by immunoblotting after electrophoretic separation and transfer. Double-determinant immunoradiometric assay indicated that the seven purified monoclonal antibodies recognized three distinct regions of the Mr 52,000 protein, and it was used to assay the Mr 52,000 protein in biological fluids. These antibodies did not react with the external plasma membrane of MCF7 cells, as shown by immunofluorescence analysis. By contrast, the cytoplasm of MCF7 cells (but not T47D and RBA cells) was stained by the peroxidase-immunoperoxidase complex after plasma membrane permeation, indicating that the protein is secreted by exocytosis rather than shed from the plasma membrane.
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PMID:Characterization of monoclonal antibodies to the estrogen-regulated Mr 52,000 glycoprotein and their use in MCF7 cells. 388 Nov 71

A screening method is described to select monoclonal antibodies (Mabs) that bind to ocular melanoma-associated antigens (MAAs) retained in formalin-fixed, paraffin-embedded tissue sections. Small sections of epithelioid or spindle-cell-type uveal melanomas were cut into 2 mm cubes and reembedded in one block. Microslides were cut from this block and used to screen hybridoma supernatant fluid. Using this screening method, three MAbs were selected from two separate fusions of mouse myeloma cells with spleen cells of mice immunized previously with either ocular melanoma cells obtained fresh at enucleation or cells of a cutaneous melanoma cell line. Although all three MAbs showed similar specificities, MAb8-1H showed the strongest immunohistochemical reaction and was studied further in detail. MAb8-1H bound to 91% (71/79) of the choroidal or ciliochoroidal melanomas tested, indicating a high prevalence of this antigen in uveal melanomas. The antigen defined by MAb8-1H was isolated, purified, and partially characterized as a 40,000-50,000 dalton, highly glycosylated protein rich in glycine, serine, and glutamic acid, as is typical of a mucin-type glycoprotein.
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PMID:Tissue distribution and biochemical properties of an ocular melanoma-associated antigen. 390 53

Sera from 51 patients with multiple myeloma, 48 patients with monoclonal gammopathy of undetermined significance (MGUS), and 10 patients with Waldenstrom's macroglobulinemia (78 men and 31 women) were analyzed by radioimmunoassay for four placental proteins: the common alpha-subunit of glycoprotein hormones (alpha), chorionic gonadotropin and/or its free beta subunit (CG-beta), placental lactogen (PL), and "pregnancy-specific" beta 1-glycoprotein (SP1), to see if these would be useful tumor markers to distinguish benign from malignant monoclonal gammopathies. The 95th percentiles for serum alpha concentrations in our male patients and normal men were 7.0 and 2.0 ng/ml, respectively. When male patients with renal failure (known to be associated with elevated serum alpha) were excluded, the 95th percentile for serum alpha for the remaining 73 non-uremic men was 4.0 ng/ml. Of these, 7 with MGUS, 2 with macroglobulinemia, and 17 with myeloma had serum alpha concentrations above the 95th percentile for normal men, and analysis of covariance showed that both age and disease category were significantly related to serum alpha concentration. When the serum alpha concentrations from our 73 non-uremic men and 119 normal men were pooled, the 90th percentile was 2.7 ng/ml, and 16 of the 19 individuals in the top 10th percentile came from our non-uremic men (p less than 0.00002). For serum SP1, analysis of data combining our 109 patients with 93 controls again revealed a disproportionate number of the top 10% in our patient population. The 95th percentiles for serum alpha in our female patients, and for serum CG-beta in both sexes, were not significantly elevated above controls. Serum PL concentrations exceeded the 95th percentile of normal in only 5% of our patients, and were not further analyzed. Serum alpha and SP1 concentrations, but not those of CG-beta or PL, were significantly higher for our patients than for controls. These placental proteins are unlikely to be generally useful as tumor markers for monoclonal gammopathies, however, because of the overlap among "benign" and malignant groups, and because of a lack of correlation with stage of the disease as observed in our myeloma patients.
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PMID:Placental proteins as tumor markers in human monoclonal gammopathies: results in 109 patients. 393 36

Hybridoma cultures producing monoclonal antibodies were derived from fusions of the parent myeloma P3-X63-Ag8-U1 with spleen cells of BALB/c mice which had been immunized with the Lewis lung carcinoma (3LL) of C57BL/6 mice. Four monoclonal antibodies (A8-2.7, C6-1.2, D12-2.7), and G8-1.6) showed high reactivity to 3LL cells but showed no or low reactivity to other tumor cells, cultured cell lines, and normal tissues from C57BL/6 mouse. The C6-1.2 antibody was confirmed to have a binding capacity specific to 3LL cells by absorption assay and inhibition assay. Antigenic analysis indicated that the C6-1.2 antibody bound to 3LL surface glycoprotein (approximately 45,000 daltons), and other antibodies reacted with proteins (less than 10,000 daltons) on the cell surface of 3LL. Administration of C6-1.2 antibody i.v. reduced the metastasis into the lungs of 3LL in C57BL/6 mice.
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PMID:Monoclonal antibodies to Lewis lung carcinoma. 404 23

We describe a previously uncharacterised glycoprotein antigen of rat brain. The antigen was localised by immunofluorescence on 10 micron cryostat tissue sections, and was found to be present intracellularly in neurons. No other cell types or structures within the brain were stained. The antigen is recognised by a mouse monoclonal antibody called NGP41. The antibody was produced after immunising a mouse with glycoproteins purified by lentil lectin affinity chromatography of solubilised rat brain membranes. Spleen cells from the immunised mouse were fused with the myeloma P3X63Ag8. The antigen is expressed by neurons in all brain regions, and also in the dorsal root ganglion neurons of the peripheral nervous system. In all brain regions, the large projection neurons are the most intensely stained by immunofluorescence, but some small neurons also express the antigen. Although dendrites were not stained, sections of sciatic nerve were stained by NGP41, suggesting that the antigen is expressed by axonal processes. The cell bodies of neurons in the inferior olive were stained by NGP41, but their terminals on Purkinje cell dendrites in the cerebellar cortex were not stained, suggesting that the antigen is absent or expressed below the limit of detection in terminals. Both crude brain membranes and a lentil lectin affinity purified brain glycoprotein fraction absorbed the antibody, suggesting that the antigen is a membrane bound glycoprotein. In immunoblotting experiments, the antigen was detected in homogenates of brain and spinal cord membranes, where it appeared as a triplet of bands with molecular weights of 41K, 38K and 36K. Antigen was not detected by immunoblotting in homogenates of six different tissues of non-nervous origin. The antigen was enriched in glycoprotein fractions from adult and juvenile cerebellum as assessed by immunoblotting. Adult brain glycoprotein preparations had a triplet structure similar to that in the homogenates, although most of the antigenic activity of the juvenile preparation was found in a position corresponding to the upper two bands of the triplet.
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PMID:Recognition by a mouse monoclonal antibody of a glycoprotein antigen of rat brain which is expressed intracellularly by neurons. 608 6

BALB/c mice were injected with an affinity-chromatography-purified placental transferrin receptor preparation. Spleen cells were fused with NS-1 myeloma cells. Sixteen hybrids producing monoclonal antibodies specific for the transferrin receptor and two hybrids specific for transferrin were identified by radioimmunoassay (RIA). Five hybrids were selected for cloning on the basis of antibody specificity and affinity. None of the antibodies inhibited the binding of transferrin to K562 cells. The binding of antibody ID9 to K562 cells was partially inhibited by transferrin or a polyclonal goat anti-transferrin receptor antiserum. Of the five antibodies, two (IIB6 and IIB2) reacted only with the purified receptor and solubilized cells and not with whole cells. The other three antibodies, when tested with normal human cells and leukaemia and tumour cell lines, showed identical reaction patterns. The antibodies precipitated a glycoprotein from K562 cells with an apparent molecular weight of 94,000, estimated from sodium dodecyl sulphate-polyacrylamide gel electrophoretograms run under reducing conditions, and a molecular weight of 188,000 when run under unreduced conditions. All antibodies have a high affinity with Ka values ranging from 1.44 X 10(9) to 3.56 X 10(10) (l/mol). The antigen precipitated by all five antibodies showed identical peptide maps after partial proteolytic digestion.
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PMID:Monoclonal antibodies to a purified human transferrin receptor. 609 40


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