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)

1. A patient with occasional attacks of hypoglycemia had levels of serum immunoreactive insulin persistently fifty to one-hundred times the normal value. Immunoelectrophoresis revealed presence of monoclonal IgG in his serum. The patient's diagnosis was established as paraproteinemic lymphoid and plasmocytic reticulosis proximate to multiple myeloma; insuloma was not found. 2. On gel filtration of native serum, only part of the total immunoreactivity was found in the elution position of crystalline insulin; the major part emerged in the early fractions together with the large proteins. After acidification of the serum, however, practically the entire immunoreactivity was recovered in ethanol extracts and proved to be "little insulin" on gel filtration. Only, "little insulin" was also detected after gel filtration of serum incubated with urea. 3. It is suggested that the large component with insulin immunoreactivity obtained in gel filtration of native serum is an insulin-protein complex. The nature of the presumed complex is not clear. It is not a complex of the antigen-antibody type. Insulin "trapping" by monoclonal gamma globulin is considered.
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PMID:Inordinately high levels of serum immunoreactive insulin in monoclonal immunoglobulinemia (on the problem of "big, big insulin"). 112 9

Cytoplasmic (high-molecular-weight) DNA polymerase was partially purified from mouse myeloma. Upon chromatography on DEAE-Sephadex, following fractionation on phosphocellulose, the enzyme was resolved into three species named CI, CII, and CIII. The species CI and CII have equal sedimentation coefficients (10.5 S) in sucrose gradients without salt. In the presence of 125 mM ammonium sulfate the sedimentation coefficients are reduced to 8.6 S. The species CIII shows sedimentation coefficients of 5.7 S and 5.2 S without salt and in the presence of 125 mM ammonium sulfate, respectively. This species is assumed to be an artifact arising from either CI or to a minor extent from CII. The optima for pH, KCl and Mg2+ concentration, and the extent of inhibition by N-ethylmaleimide are the same. However, the enzymes differ in their responses to Mn2+ (substituting for Mg-2+), and to addition of ethanol, dimethylsulfoxide, and various phospholipids in the assay mixture. The enzymes prefer poly[d(A-T - d(A-T)] or partially degraded (activated) DNA as template rather than double-stranded or single-stranded DNA. The activity on activated DNA relative to that on poly[d(A-T) - D(A-T)] was found to be 93, 66, and 29% for DNA polymerases CI, CII, and CIII, respectively.
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PMID:High-molecular-weight DNA polymerases from mouse myeloma. Purification and properties of three enzymes. 116 71

Normal human pooled plasma was fractionated by a variety of methods. The IgE concentration of the different fractions was determined by a solid-phase radioimmunoassay. The results of these studies indicate, that polyclonal IgE behaves similarly to IgE of myeloma origin. A biospecific method was worked out to purify IgE from fraction III of the cold ethanol fractionation procedure.
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PMID:Behaviour of polyclonal human IgE in the course of fractionation. 123 46

Biologically active substances (BAS) were isolated from the tissues of Fasciola hepatica L. and from F. hepatica-infected rat liver by ethanol precipitation from aqueous tissue homogenates. A marked inhibiting effect of the newly isolated BAS on hepatoma MC29 cell culture proliferation and a slight inhibiting effect of the newly isolated BAS on myeloma cell culture proliferation was found. The strongest inhibiting effect was by BAS isolated from the tissues of F. hepatica. The inhibiting effect of the BAS isolated from F. hepatica-infected liver was stronger than the effect of the BAS isolated from normal liver tissue.
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PMID:Inhibition of proliferation of tumour cell cultures by biologically active substances isolated from the tissues of Fasciola hepatica and Fasciola hepatica-infected rat liver. 129 55

Extracts of human MCF 7 mammary carcinoma cells, the human lymphoblastoid cell lines AEH 1 and IM 9, T-cell derived CCRF cells, HL 60 myeloic leukaemia cells and murine myeloma cells SP 0 and NS I were analysed for immunoreactivity with polyclonal goat antibodies raised against homogeneous preparations of C-terminal fragments (32 kDa) of porcine uterine oestradiol receptor (ER). Whole cells and low speed cytosols were analysed for specific oestradiol-binding activity. ERs were enriched from cell extracts by either fractionated ethanol precipitation (0-25% (v/v) ethanol) and/or microscale-immunoaffinity chromatography. Immunoreactive proteins of identical molecular weight (approximately 65 kDa) were detected in all cell lines examined. Whole cell binding assays showed specific oestradiol-binding activity in MCF 7, IM 9 and CCRF cells. Borderline binding was found in HL 60 myeloid cells. No specific binding could be detected in AEH 1, NS I and SP 0 cells. Identical results were obtained using agar-electrophoresis after dextran-coated charcoal treatment. Immunoaffinity purified ERs from MCF 7, AEH 1 and HL 60 cells were subjected to limited proteolysis, where identical tryptic fragments were generated. In conclusion, we have confirmed by immunological methods that ERs are expressed in a variety of cell lines derived from the immune system and the haematopoietic system. The lack of specific hormone binding or very low-affinity hormone binding in some of the cells examined may be due to post-translational events or point mutations.
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PMID:Immunological detection of the oestradiol receptor protein in cell lines derived from the lymphatic system and the haematopoietic system: variability of specific hormone binding in vitro. 140 47

Immunizing mice with a transitional cell cancer (TCC) tissue in the renal pelvis, we produced a monoclonal antibody (EH14) against new epithelial antigens. After the mice were immunized repeatedly, their splenic cells were harvested and fused with NS/1 myeloma cells. The normal kidney tissue of the same patient was used on Dot blots to select the hybridoma. A a result, one hybridoma whose antibody (EH14) reacted very strongly with TCC but only faintly with normal kidney tissue or normal bladder mucosa was obtained. On immunohistochemistry, EH14 stained all of the 29 TCC tissues. EH14 also stained uterus cancer (7/7) and gastric cancer (6/6) as well as the normal squamous cell and many types of the normal epithelium. All of the lymphnodes containing metastatic bladder cancer were strongly stained with EH14. EH14, however, did not stain interstitial tissues, muscles and sarcomas. The molecular weight of the antigen recognized by EH14 was 14KD and 28 KD on Western blot analysis, and the antigen was stable with formalin or ethanol. The antigen was not the same as that reported previously, and may be useful as a histological marker of TCC.
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PMID:[Study of a monoclonal antibody against new epithelial membrane antigens of transitional cell carcinoma]. 219 79

Optimal expression of the high-affinity Fc receptor for IgG (FcRI) by the human monocyte cell line U-937 requires the presence of low density lipoprotein (LDL), and neither cholesterol nor high density lipoprotein can provide the component necessary for optimal FcRI expression. Here we show that FcR-mediated phagocytosis also requires LDL. U-937 cells were cultured in medium containing interferon gamma and either fetal calf serum (FCS) or delipidated FCS (DLFCS). The phagocytosis of IgG-coated erythrocytes was measured by a colorimetric assay. U-937 cells cultured in DLFCS medium had less than 16% of the phagocytic activity of cells cultured in normal FCS medium. Phagocytosis of IgG-coated erythrocytes could be inhibited 85% by the addition of murine IgG2a myeloma protein (5 micrograms/ml). U-937 cells cultured in DLFCS medium supplemented with pure cholesterol in ethanol (10 micrograms/ml) had only 30% of the phagocytic activity of cells grown in FCS medium. Addition of very low density lipoprotein (0.2 mg of protein per ml) to DLFCS medium also failed to increase phagocytosis. However, the addition of LDL (0.2 mg of protein per ml) to DLFCS medium restored 90% of the phagocytic activity. Since neither pure cholesterol nor very low density lipoprotein restored normal phagocytic function to U-937 cells despite a normalization of cellular cholesterol content, the restoration of phagocytosis observed with LDL replacement cannot be explained by mere delivery of cholesterol by LDL. Thus, LDL is required for the expression of FcRI and FcR-mediated phagocytosis by U-937 cells and may be an important regulator of phagocytic activity of monocytes and macrophages in vivo.
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PMID:Identification of low density lipoprotein as a regulator of Fc receptor-mediated phagocytosis. 236 19

Human serum low density lipoprotein (LDL) is a large (Mr = 2-3 X 10(6), complex particle composed of lipid, protein and carbohydrate. We obtained about 40 mouse spleen-myeloma hybrid cell lines which produce antibodies against LDL. Three of them, SC2, SC3 and SC10, have been cloned and subcloned and their antibody products characterized. They recognize three non-overlapping epitopes in native LDL. Two of them, SC3 and SC10, also are capable of recognizing very low density lipoprotein, (VLDL), whereas SC2 reacts only weakly with VLDL. All three antigenic determinants remain intact, and accessible to antibodies on the LDL protein apo B, prepared by delipidation in a 'non-denaturing' detergent, sodium deoxycholate. However, apo B prepared by organic solvent, ether-ethanol, or sodium dodecyl sulfate (SDS) delipidation, while reacting strongly with SC10, is only poorly recognized by SC2 or SC3. Proteolysis of LDL with trypsin, chymotrypsin, Staphylococcus aureus protease, papain or thermolysin gives, in each case, several non-identical protein fragments which are separable by SDS-polyacrylamide gel electrophoresis. Upon immunoblotting, some of these fragments are now recognized by either SC3 or SC10 but not SC2, some are recognized by both SC3 and SC10, and others are immunologically unreactive. The protein bands that are separated by SDS gel electrophoresis are composed of several non-identical fragments and contain the antigenic sites to differing degrees. Some of the immunologically reactive fragments do not appear to contain carbohydrate. Reduction and carboxymethylation do not destroy the immunoreactivity of LDL toward any of the antibodies; however, modification of lysine residues by citraconic anhydride markedly diminishes the reactivity of LDL toward SC3. It is likely that the two antibodies SC3 and SC10 are directed against different linear amino acid sequences or very stable domains, whereas the third, SC2, is directed against a more fragile conformational domain of apo B.
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PMID:Isolation and characterization of three monoclonal antibodies to human serum low density lipoprotein apoprotein B. 242 25

A new monoclonal antibody, 1C5, was produced by fusion of spleen cells obtained from mice immunized with CAC-1, a human cell line of cervical adenocarcinoma of the uterus, and NS-1 myeloma cell. The objectives of this study were to obtain moAb that can be used for routine histology and cytology, and to examine the histogenesis of cervical adenocarcinoma. 1. 1C5 reacted with 88% of cervical adenocarcinoma of the uterus, but did not react with cervical squamous cell carcinoma of the uterus and other squamous cell carcinoma. However, 1C5 reacted with some adenocarcinomas, such as endometrial carcinoma of the uterus and ovarial carcinoma. 2. The staining pattern by 1C5 was different, in cervical adenocarcinoma from that in endometrial carcinoma of the uterus, and also different in the endocervical type from that in the endometrioid type of cervical adenocarcinoma. Therefore, 1C5 is useful in distinguishing between two types of adenocarcinoma of the uterus. 3. 1C5 did not react with normal squamous cells or normal columnar cells of the uterine cervix, or with normal endometrial cells of the uterus. However, the columnar cells in a limited area of the squamocolumnar junction were strongly stained with 1C5. 4. 1C5 reacted with ethanol-fixed, and routine formalin-fixed and paraffin-embedded tissue. Thus, 1C5 may be used for clinical diagnosis. 5. 1C5 was found to be IgG1. 6. The molecular weight of the 1C5-defined antigen was 26,000 daltons, and the epitope of the 1C5-defined antigen was carbohydrate moiety. 7. We examined the histogenesis of cervical adenocarcinoma of the uterus by utilizing the reactivity of 1C5.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[The production and characterization of monoclonal antibody, 1C5, reactive with cervical adenocarcinoma of the uterus]. 247 40

The native structures of protein phosphatases have not been clearly established. Several tissues contain high molecular weight enzymes which are converted to active species of Mr approximately 35,000 by denaturing treatments or partial proteolysis. We have used a monoclonal antibody directed against purified bovine cardiac Mr = 38,000 protein phosphatase to determine whether this species is the native catalytic subunit or a proteolytic product of a larger polypeptide. Monoclonal antibody was obtained from a cloned hybrid cell line produced by the fusion of Sp2 myeloma cells with spleen cells from a mouse immunized with phosphatase coupled to hemocyanin. This antibody was specific for the Mr = 38,000 phosphatase as determined by immunoblot analysis of purified enzyme or cardiac tissue extracts after native or sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A single immunoreactive protein of Mr = 38,000 was present in cardiac tissue extracts including extracts prepared from freeze-clamped rat heart rapidly denatured in hot sodium dodecyl sulfate buffer. Precipitation of cardiac extract with 80% ethanol did not alter the Mr of the phosphatase nor did it liberate new immunoreactive material not observed in the extract. Ethanol precipitation caused the dissociation of both phosphatase activity and immunoreactivity from a high Mr form to a form of Mr between 30,000 and 40,000. An immunoreactive protein of Mr = 38,000 was identified in several bovine and rat tissues as well as tissues from rabbits, mice and chickens and human HT-29 cells. From these data we conclude that the Mr = 38,000 cardiac phosphatase is a native catalytic subunit of higher molecular complexes which are dissociated by ethanol precipitation. A very similar, or identical, protein is present in several tissues and species suggesting that this catalytic subunit is a ubiquitous enzyme important in many dephosphorylation reactions.
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PMID:Structural characterization of cardiac protein phosphatase with a monoclonal antibody. Evidence that the Mr = 38,000 phosphatase is the catalytic subunit of the native enzyme(s). 299 81


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