Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two IgG1 type monoclonal antibodies ALT-01 and ALT-04 were prepared by two different immunization schedules. ALT-01 was generated by fusing murine myeloma NS-1 cells with splenocytes from a BALB/c mouse immunized by human lung squamous carcinoma cells, which were coated by antisera to mixed human lymphocytes. For preparation of ALT-04, human lung squamous carcinoma xenograft-bearing nude mice were injected I. P. with the spleen cells of normal BALB/c mice in order to acquire immunofunction. The spleen cells from these tumor-bearing nude mice were fused with NS-1 cells. Then, these hybridomas were screened and cloned for 3 times. Two antibodies were shown to recognize the surface antigen on human lung carcinoma cells and several kinds of tumor cell lines but not those on normal cell lines. ALT-01 reacted to neither human lung carcinoma tissue nor its xenograft. ALT-04 reacted to human lung carcinoma tissue, of which, reaction to adenocarcinoma was the strongest but not to various normal tissues. Immunoprecipitation followed by SDS-polyacrylamide gel electrophoresis and autoradiography was used to detect the associated antigen in 35S-labeled human lung carcinoma cells. Antigens, reacting to ALT-01, show one band of Mr 38,000 but those to ALT-04 reveal two bands of Mr 48,000 and 36,000.
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PMID:[Reactivity of monoclonal antibodies ALT-01 and ALT-04 and identification of lung cancer-associated antigens]. 344 54

Over 4350 human Ig-secreting hybrids have been generated through the fusion of human lymphocytes with NS-1 (mouse), LICR-2, SKO-007, GM4672, or UC729-6 (human) myeloma and lymphoblastoid cell lines. NS-1 proved to be the most satisfactory fusion partner, and 83% of the stable Ig-secreting clones were derived from NS-1 fusions. Three hundred five hybrids produced human monoclonal antibodies (hmAb) reactive with cell surface or intracellular antigens expressed by cultured human tumor cell lines, and 111 of these have undergone detailed serological specificity analysis. Several general points have emerged from our study of hmAb: A significant proportion of the human B-cell clones produce antibody reactive with cellular antigens. The majority of these antigens have an intracellular location and are broadly distributed. Intracellular and cell surface differentiation antigens and other antigens with restricted distribution have been defined by hmAb, including two cell surface antigens not detected on normal cells. The relationship of these findings to cancer is unclear, as hmAb reactive with antigens showing distinctive distribution have been generated from the lymphocytes of normal individuals as well as tumor-bearing patients.
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PMID:Specificity analysis of human monoclonal antibodies reactive with cell surface and intracellular antigens. 345 55

The cell surface antigen associated with the transformed state of cells that could grow in an anchorage-independent manner was analyzed by use of techniques of DNA transfection and hybridomas secreting the monoclonal antibody (MoAb). Spleen cells of C57BL/6 mice immunized with a highly tumorigenic, chemically induced murine cultured colon 36 tumor (C-C36) of BALB/c origin were hybridized with NS-1, a hypoxanthine phosphoribosyltransferase-deficient myeloma line of BALB/c mice. Screening of hybridomas revealed an antibody that reacted with C-C36 and transformed Swiss 3T3 cells growing in soft agar after transfection of 3T3 cells with C-C36 DNA. The hybridomas that did not react with nontransformed 3T3 and the less tumorigenic BALB/c hemangioendothelioma line D10 were then selected. An MoAb was designated "#71295." This MoAb immunoprecipitated the antigen that consisted of 65,000- and 14,000-molecular-weight components with soluble C-C36 membrane antigens. It also reacted with 2 other chemically induced syngeneic colon tumor lines, cultured colon 26 tumor line and cultured colon 51 tumor line, and with fibrosarcoma Meth A. However, #71295 was not found in NS-1, D14, and BALB/c normal thymus, liver, colon, and kidney tissues. In addition, this MoAb could not inhibit the anchorage-independent growth of C-C36 and transformed 3T3 cells. These results suggest that although the molecule defined by #71295 might not be associated with the anchorage independence of cell growth, it could be a newly expressed determinant on the cell surface that is related to the events of cell transformation.
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PMID:Identification of transformation-related antigen by monoclonal antibody on Swiss 3T3 cells induced by transfection with murine cultured colon 36 tumor DNA. 346 94

Immunization of a BALB/c mouse with cells from the human neuroblastoma line LAN-1 and fusion of the spleen cells with mouse myeloma cells, NS-1, led to the production of a monoclonal antibody (Mab) with a rather unique reactivity for neuroblastoma. This Mab, named 5 A7, detects an antigen of an apparent molecular weight of 65,000-67,000, localized mainly in the cytoplasm and released into culture medium, as revealed by immunoprecipitation and immunoblotting experiments. By immunoperoxidase staining using a biotin-avidin technique, Mab 5 A7 demonstrates a restrictive staining for neuroblastoma cell lines. Following extensive testing on freshly frozen specimens of neuroblastoma and other tumors, Mab 5 A7 shows a highly selective reactivity for neuroblastomas (13 of 14) and some cells of one primitive neuroectodermal tumor (ependymoblastoma). No reactivity could be detected with Mab 5 A7 on the 57 other tumor tissues tested. Among the normal fetal or adult tissue specimens tested, positive staining is found only on adult brain, colonic crypts, some renal tubules, and fetal medulla of the adrenal gland. Among bone marrow specimens tested, only those infiltrated by neuroblastoma cells gave a positive staining. Normal or malignant hematopoietic cells showed no reactivity with Mab 5 A7. Our results with Mab 5 A7 suggest that this reagent not only provides a valuable probe for the immunohistological diagnosis of neuroblastoma on fresh tumor specimens but also allows the detection of bone marrow infiltration by neuroblastoma cells.
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PMID:Highly selective recognition of human neuroblastoma cells by mouse monoclonal antibody to a cytoplasmic antigen. 351 88

A monoclonal antibody designated SBU-3 was produced by the fusion of mouse NS-1 myeloma cells with spleen cells from a BALB/c mouse immunized with sheep trophoblast microvilli. Lee et al (1985) have reported the immunohistological staining of sheep trophoblast with SBU-3 showing that, as early as 21 days of gestation, the monoclonal antibody recognizes an antigen restricted to the binucleate cells of the trophoblast which are located only at sites of invasion of the underlying uterine tissue. Subsequently the antigen appears in the maternal syncytial layer. Immunoprecipitation of 125I-labelled microvilli by SBU-3, characterization of the antigen on immunoblots, and biochemical analysis all suggest that this monoclonal antibody specifically recognizes a carbohydrate epitope on a series of glycoproteins of molecular weights between 30 000 and 200 000. SBU-3 antigen is present in allantoic fluid but is not detectable in any fetal or adult tissue studied, including maternal and fetal sera. It is suggested that this antigen may have a role in the placentation process.
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PMID:Characterization of a sheep trophoblast-derived antigen first appearing at implantation. 352 14

Monoclonal antibodies (MAbs) to placental alkaline phosphatase (PAlP) were raised by using the hybridoma technique. Spleen cells from immunized mice were fused with the mouse myeloma line NS-1 using 50% polyethylene glycol and cultured in a selection medium. Antibodies were screened by the enzyme immunoassay using immobilized solid-phase antigen and anti-mouse immunogloblin Fab' (rabbit)-beta-D-galactosidase complex. Four double-cloned hybridomas were obtained. The cross-reactivity with different kinds of alkaline phosphatases of the raised MAbs was examined. At first, MAb 11-D-10, with which placenta was stained but liver and small intestine were not stained in indirect immunofluorescence, was selected. Then, the cross-reactivity of MAb 11-D-10 was further investigated by immunoblotting (Western blotting). MAb 11-D-10 reacted with PAlP but did not react with hepatic and intestinal alkaline phosphatase at all. The binding activity of 125I-labeled MAb 11-D-10 with different choriocarcinoma cell lines (SCH, BeWo, NaUCC-1, NaUCC-2, and NaUCC-3) was highest in SCH, then in the order of BeWo, NaUCC-3, NaUCC-1 and NaUCC-2, and correlated to the PAlP content of the cells (SCH greater than BeWo greater than NaUCC-3 greater than NaUCC-1 greater than NaUCC-2). Also the intensity of indirect immunofluorescence of the above cell lines with MAb 11-D-10 correlated with the PAlP content of each cell.
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PMID:Purification of placental alkaline phosphatase and its monoclonal antibody. 353 20

Legionellae are widely spread in natural and man-made habitats. In many instances contaminated tap water has been linked to sporadic or endemic cases of human pulmonary infections, but it is not known why, in spite of frequent occurrence, legionellae only rarely cause disease. Monoclonal antibodies against Legionella pneumophila serogroup 1 (Philadelphia 1) were prepared in order to distinguish between subtypes of this serogroup. Balb/c mice were immunized i.v. three times with heat inactivated bacteria. Antibody formation was detected by an enzyme-linked immunosorbent assay (ELISA) technique using peroxidase-conjugated antimouse IgG. Spleen cells were then fused with NS-1 myeloma cells and cloned by limiting dilution. Four monoclonal antibodies were studied in detail. The study included 47 strains of L. pneumophila: 19 strains were of human origin and 28 were isolated from different environmental sources. Most were from tap water, but none from natural habitats. All strains belonged to serogroup 1 as defined by direct immunofluorescence (DFA) using monospecific FITC-labelled polyclonal antisera from rabbits. The strains were further characterized by beta-lactamase production, activity of catalase, oxidase and proteases, analysis of ubiquinones, and demonstration of membrane protein patterns by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. A strong homogenicity between all the strains could be revealed by these methods independent of their origin. One of the monoclonal antibodies (B-1) was able to distinguish between human and environmental isolates. Eighteen of the 19 human strains reacted very strongly in DFA using antimouse immunoglobulin. No reaction, however, was seen with all of the environmental strains. Immunoblots were performed for characterization of the distinguishing feature using membrane complexes of all strains on nitrocellulose strips. The blots were incubated with antibody B-1, and immune complexes were detected by 125I-protein A. Broad intense blackening was seen between 22 and 70 kilodalton. This result suggests that no single protein, but rather a smaller component such as an oligosaccharide attached to constituents of different molecular weights, might be responsible for the discriminating reaction.
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PMID:Discrimination between clinical and environmental strains of Legionella pneumophila by a monoclonal antibody. 353 65

The expression, tissue distribution, and preliminary characterization of a cell surface molecule, apparently a glycolipid, recognized by a monoclonal antibody, anti-PAA, were described. This antibody (anti-PAA) was produced by the fusion of myeloma cells NS-1 with spleen cells from a BALB/c mouse, which were sensitized with activated human T-cells generated by allogeneic stimulation in mixed-lymphocyte culture (MLC). Resting human peripheral blood T-cells, B-cells, and monocytes demonstrated weak anti-PAA binding. Binding of proliferating T-cells (phytohemagglutinin- and MLC-activated T-cells) and thymocytes to anti-PAA was two to six times greater than that of resting T-cells. A fifteenfold-increased binding was observed with acute lymphocytic leukemia T-cell lines. Epstein-Barr virus-transformed B-cell lines bound anti-PAA up to sixteenfold greater than resting B-cells. Tumor cell lines of various nonlymphoid origins demonstrated marked reactivity with this antibody. Both benign and malignant cells in hyperplastic tissues, of various origins, bound anti-PAA, whereas their normal, nonproliferating counterparts did not. Normal proliferating cells in these tissues, including cells of the placental chorionic villi and trophoblasts, also bound anti-PAA. Of all lymphoid and nonlymphoid cell lines examined, only chronic lymphocytic leukemia (CLL) cells and some cell lines derived from Burkitt's lymphoma showed weak or no binding. This antibody also failed to react with a variety of nonprimate cell lines. Anti-PAA antibody did not immunoprecipitate any protein from lymphoid tumor cell lines to which it demonstrated a quantitatively high degree of binding, nor did protease treatment of these lines decrease antibody binding. Anti-PAA did, however, bind to glycolipids extracted from these cell lines. Binding of this monoclonal antibody to a minor neutral glycolipid, isolated from the erythroleukemia cell line K562, was about sixfold greater than that of any other K562 neutral glycolipid or ganglioside. Anti-PAA demonstrated weak or undetectable binding to purified, predominant, lymphoid cell membrane's neutral glycolipids and gangliosides. The monoclonal antibody anti-PAA appeared, therefore, to recognize a unique, proliferation-associated, neutral glycolipid present on normal as well as on benign and malignant proliferating cells. The antigen appeared to be universally expressed on proliferating cells from all human tissues with the exception of some Burkitt's cell lines and CLL cells. Nonhuman cell lines, except those for closely related primates, did not express PAA.
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PMID:Unique proliferation-associated marker expressed on activated and transformed human cells defined by monoclonal antibody. 354 53

BALB/c mice were hyperimmunized with ACHN (ATCC CRL 1611, American Type Culture Collection, Rockville, Maryland), a stable in vitro cell line derived from a malignant pleural effusion in a 22-year-old man with renal cell carcinoma. The hyperimmune spleen cells were fused with NS-1 murine myeloma cells using polyethylene glycol. Hybridoma supernatants were screened for the presence of IgG reactive with detergent extracts of ACHN and nonreactive with detergent extracts of normal kidney tissue. A stable, rapidly growing clone named 5F4 was isolated. Supernatant from 5F4 was used as a primary antibody preparation for avidin-biotin complex immunoperoxidase staining of multiple cases of renal cell carcinoma, normal tissues, and other tumors. 5F4 produced IgG which reacted with a cytoplasmic structure in paraffin-embedded sections of all renal cell carcinomas tested. There was occasional, weak, granular, cytoplasmic staining of isolated tubular lining cells in adjacent normal kidney.
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PMID:A renal cell carcinoma neoplastic antigen detectable by immunohistochemistry is defined by a murine monoclonal antibody. 355

Four monoclonal antibodies reactive by immunofluorescence and by flow microfluorimetry with canine and porcine gastric parietal cell membranes were produced by fusion of mouse NS-1 myeloma cells with splenocytes from mice immunized with a population of canine gastric mucosal cells containing 60-70% parietal cells. One of these, an IgM antibody designated 2C1, reacted with the surface membranes of parietal cells by immunofluorescence, flow microfluorimetry, and immunogold electron microscopy; competed with 125I-labeled gastrin for binding to gastric cells; and inhibited by 56% maximal gastrin stimulation of [14C]aminopyrine uptake in parietal cells. The antibody immunoprecipitated 125I-labeled samples of a 78-kDa gastrin-binding protein purified from membrane extracts of porcine gastrin mucosa but did not recognize the same protein labeled covalently with 125I-labeled gastrin-(2-17)-hexadecapeptide. These observations suggest that the previously identified 78-kDa gastrin-binding protein is the gastrin receptor and that the antibody 2C1 is directed against the gastrin binding site of the gastrin receptor.
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PMID:Monoclonal antibody to the gastrin receptor on parietal cells recognizes a 78-kDa protein. 355 45


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