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

Binding of purified plasma fibronection to Crithidia luciliae kinetoplast DNA was demonstrated by fluorescence microscopy. The method was suitable for the detection of fibronectin in human plasma diluted 1:256 and 1 microgram/ml concentration of isolated fibronectin. Purified human Clq, monoclonal human myeloma proteins of IgG1 and IgG3 subclasses and calf thymus DNA inhibited the binding of fibronectin to kinetoplasts. The method can be used as a functional assay for fibronectin and for various materials containing fibronectin.
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PMID:Binding of fibronectin to DNA: new application of the Crithidia luciliae immunofluorescence test. 390 5

The attachment of murine myeloma, 3T3, and cutaneous fibrosarcoma cells to substrates of either fibronectin, type I collagen, or two types of tissue culture plastic was examined in the presence and absence of specific exogenous glycosaminoglycans. Fibrosarcoma and 3T3 cells were found to be nondiscriminatory with respect to their avidity of attachment to substrates of either of the proteins or of conventional tissue culture plastic, whereas the myeloma cells attached significantly less well to a substrate of collagen than to the other two matrices. On tissue culture plastic and collagen the fibrosarcoma cells attached more rapidly than did the other two cell types. Selective and partial inhibition of cell attachment to type I collagen, and, to a lesser extent, fibronectin, occurred upon preincubating these substrates with the sulfated glycosaminoglycans, heparin and heparan sulfate, at concentrations of 1 to 100 micrograms/ml; for 3T3 cells heparin was significantly more inhibitory (mean maximal inhibition of approximately 40%) than were two heparan sulfate fractions. Attachment of fibrosarcoma and 3T3 cells to a nitrogenated tissue culture plastic surface with a net positive charge (Primaria) was nearly 50% inhibited by heparin at the higher concentration and to a lesser extent by the two heparin sulfate fractions. Myeloma cell attachment to this same substrate was inhibited, to a lesser degree, by all three sulfated glycosaminoglycans. Hyaluronic acid, dermatan sulfate, and chondroitin 6-sulfate were inactive in our attachment assays. We suggest that the functional role of glycosaminoglycans in substrate attachment may vary depending on the cell type and the matrix involved in the specific interaction. In particular, the net charge of the substrate appears to be an important factor, and on positively charged surfaces these substances may serve a greater function. However, since nearly complete abrogation of cell attachment should have been achievable by some of the exogenous preparations if cell surface sulfated glycosaminoglycans were to comprise the major cellular binding sites for matrices, we conclude that it is unlikely that these complex polysaccharides function as the principal determinant of simple cell attachment.
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PMID:Glycosaminoglycans and the substrate attachment of murine myeloma, 3T3, and cutaneous fibrosarcoma cells. 401 Feb 29

Enzyme histochemical and immunohistochemical study was carried out on 16 cases of Hodgkin's disease in order to elucidate the origin of Hodgkin's cell and Reed-Sternberg cell. Both Hodgkin's cell and Reed-Sternberg cell do not have tumor markers such as lysosome enzyme, alpha-fetoprotein, and fibronectin, and these cells do not form either Es or EoxACm rosettes. A great number of cells in most cases contained intracytoplasmic immunoglobulin and showed gamma-glutamyl transpeptidase activity on the cell membrane and in cytoplasm. Since gamma-glutamyl transpeptidase is an enzyme related to the transport of amino acid into cell, it is assumed that there is an intake of amino acid in these cells followed by synthesis of protein. Enzyme histochemically, both Hodgkin's cells and Reed-Sternberg cells resemble multiple myeloma cells rather than B-cells in acute lymphocytic leukemia and chronic lymphocytic leukemia and T-cells or monocytes.
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PMID:Hodgkin's disease--a histochemical study with special emphasis on the character of Hodgkin's cell and Reed-Sternberg cell. 613 29

We have produced several monoclonal antibodies which appear to be directed against different antigenic determinants of rat plasma fibronectin. Fibronectin was purified from rat plasma by affinity chromatography on gelatin-Sepharose and arginine-Sepharose columns. Mice were immunized and hybridomas were prepared by fusing spleen cells with Sp2/0-Ag14 myeloma cells using poly(ethylene glycol). Three hybridomas (RFN1, RFN2 and RFN3) were selected for characterization. All are IgG molecules, one is IgG2a, one IgG2b and one IgG1. Titers of ascites fluids produced using these hybridomas range from 102 400 to greater than 409 600. The antibodies cross-reacted to different degrees with human fibronectin. Rat fibronectin was radioactively labeled and cleaved using human polymorphonuclear leukocyte elastase. Four major peptides, Mr approx. 160 000, 140 000, 60 000 and 30 000 were produced. Each of the hybridoma antibodies immunoprecipitated different elastase peptides. RFN1 precipitated the Mr 160 000 peptide, RFN2 precipitated the Mr 160 000 and the Mr 140 000 peptide and RFN3 precipitated the Mr 60 000 peptide as well as low molecular weight material migrating at the buffer front. These antibodies will be useful in studies of structure/function relationships of rat fibronectin.
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PMID:Production and preliminary characterization of monoclonal antibodies to rat plasma fibronectin. 618 52

Five independent hybrids producing monoclonal antibodies to human plasma fibronectin have been obtained by fusing P3/X63-Ag8 myeloma cells with immune mouse splenocytes. The specificity of these monoclonal antibodies (MABs) for fibronectin was demonstrated by three independent tests: binding to the purified soluble molecule, immunofluorescence staining of insoluble extracellular matrices produced by endothelial cells in vitro, immunostaining of fibronectin tryptic peptides after separation on SDS-PAGE and transfer to nitrocellulose sheets. Two antibodies (MAB 29 and 52) recognized selectively human fibronectin while the others (MAB 5, 30 and 59) reacted also with plasma fibronectin from calf, hamster and chicken. Four distinct epitopes were recognized by the MABs studied. MAB 5, 30, 52 and 59 reacted with distinct antigenic sites, while MAB 29 and 52 bind to the same site. Antigenic fragments were identified by immunostaining of fibronectin tryptic peptides. MAB 5 reacted with a collagen binding fragment with a molecular weight of 120 K. In addition, each of the MAB 29, 30, 52 and 59 reacted with peptides with a molecular weight of 40 K that bind to gelatin. Since these antibodies do not inhibit fibronectin-collagen interaction, it is concluded that their corresponding epitopes are clustered in a region close, but not coincident, to the collagen binding site of fibronectin.
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PMID:Monoclonal antibodies to the collagen binding domain of human plasma fibronectin. 620 85

A series of monoclonal antibodies to human glomerular antigens was prepared by immunisation of a mouse with isolated whole glomeruli, followed by boosting with particulate glomerular basement membrane and fusion of murine spleen cells with the NSI-myeloma line. Hybridoma supernatants were screened jointly by a radioimmunoassay involving binding to isolated glomeruli, and by a 4-layer immunoperoxidase technique applied to polyester wax-embedded sections. Seven monoclonal antibodies with different specificities (PHM7-PHM13) were established and repeatedly cloned. Each antibody displayed a distinctive distribution within the glomerulus, including different patterns of staining of mesangial cells, mesangial matrix and glomerular basement membrane, in addition to extra-glomerular basement membranes and extracellular matrix. All antibodies also stained cellular outgrowths of isolated glomeruli cultured in vitro, and showed additive binding to cultured cells by radioimmunoassay. Physical characterization using absorptions with purified substrates, plus specific chemical and enzymatic digestions, indicated that PHM12 is directed against type IV collagen. PHM13 is directed against fibronectin as shown by absorption with purified fibronectin and immunoprecipitation of a 220 000 MW glycoprotein. The remaining 5 monoclonal antibodies, which react with carbohydrate (PHM7) or protein (PHM8-PHM11) determinants, were shown to be nonreactive with type IV collagen, fibronectin or other known glomerular components including sialic acid, laminin, amyloid P-component or various glycosaminoglycans. These monoclonal antibodies therefore appear to define a new series of human glomerular antigens, or possibly closely related antigenic determinants, which are synthesized by glomerular cells and incorporated into the mesangium and glomerular basement membrane. These antibodies, by providing markers for at least 2 antigens known to be important in glomerular cell-matrix interactions, should prove useful in research into the mechanisms involved in renal pathology.
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PMID:Production of monoclonal antibodies to fibronectin, type IV collagen and other antigens of the human glomerulus. 620 56

The hyalin material in massive cutaneous hyalinosis, a disease characterized by extensive tumorous periodic acid-Schiff-(PAS) positive extracellular cutaneous deposits, has been elucidated by biochemical and immunologic methods. Three major components were found: kappa light chains, a mannose-rich glycoprotein, and type I collagen. Trace amounts of fibrinogen, fibronectin, laminin, IgG, pregnancy-specific glycoprotein, albumin, and keratan sulfate, but not keratin, were also present. The kappa light chains were monoclonal, cryoprecipiting, and more basic than the kappa chains from two myeloma patients. The glycoprotein, which could not be identified as any known glycoprotein, had an apparent molecular weight of 90,000 D. Amino acid analysis showed that glutamic acid, aspartic acid, leucine, and threonine were abundant, whereas hydroxyproline, hydroxylysine, and sulfhydryl amino acids were absent. The carbohydrate content of the protein was approximately 20%. The major monosaccharides were mannose and N-acetylglucosamine. Galactose, N-acetylneuraminic acid and fucose also were present. The third major component of the hyalin material was identified as type I collagen. A humoral immune response to the storage material was found: the patient's serum contained IgM and IgG class antibodies against the mannosylglycoprotein (90 kD glycoprotein) and against type I collagen.
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PMID:Massive cutaneous hyalinosis. Identification of the hyalin material as monoclonal kappa light chains, adhesive 90 kD glycoprotein, and type I collagen. 620 74

Heparan sulfate glycosaminoglycan, isolated from the cell surface of nonadhering murine myeloma cells (P3X63-Ag8653), does not bind to plasma fibronectin, but binds partially to collagen type I, as assayed by affinity chromatography with proteins immobilized on cyanogen bromide-activated Sepharose 4B. Identical results were obtained when myeloma heparan sulfate was cochromatographed, on the same fibronectin and collagen columns, with cell surface heparan sulfates collagen columns, with cell surface heparan sulfates from adhering Swiss mouse 3T3 and SV3T3 cells. These latter heparan sulfates do, however, bind to both fibronectin and collagen, as reported earlier (Stamatoglou, S.C., and J.M. Keller, 1981, Biochim. Biophys. Acta., 719:90-97). Cell adhesion assays established that hydrated collagen substrata can support myeloma cell attachment, but fibronectin cannot. Saturation of the heparan sulfate binding sites on the collagen substrata with heparan sulfate or heparin, prior to cell inoculation, abolished the ability to support cell adhesion, whereas chondroitin 4 sulfate, chondroitin 6 sulfate, and hyaluronic acid had no effect.
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PMID:Correlation between cell substrate attachment in vitro and cell surface heparan sulfate affinity for fibronectin and collagen. 622 58

The ability of purified human myeloma IgG proteins to interact with human plasma fibronectin was studied by enzyme immunoassays. Seven of eight different myeloma IgG proteins representing all four IgG subclasses bound to solid phase fibronectin in a dose-dependent manner. The binding of myeloma IgG to solid phase fibronectin could be inhibited by soluble fibronectin and gelatin, but not by heparin or bovine serum albumin. Evidence for an antigen-antibody type interaction was not observed by double diffusion analysis. Affinity chromatography of radiolabelled cell culture medium over IgG-Sepharose showed that only fibronectin bound to the IgG-conjugates. The affinity of IgG molecules for fibronectin may play a role in cryoimmunoglobulinaemia associated with certain pathological states.
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PMID:Affinity of myeloma IgG proteins for fibronectin. 634 76

Isolated and washed cryoimmunoglobulins from 15 patients were studied for the presence of fibronectin by immunodiffusion tests. Two of the isolated cryoglobulins proved to the pure monoclonal immunoglobulins (IgGl kappa and IgGl lambda), nine contained both monoclonal IgM kappa and polyclonal IgG and four were composed of polyclonal IgG, IgM and IgA by immunoelectrophoresis. Double immunodiffusion analysis detected the presence of fibronectin in each of the separated cryoimmunoglobulins. In a solid phase radioimmunoassay, I125 labelled purified fibronectin proved to bind to isolated human monoclonal myeloma proteins of IgGl kappa and IgG3 lambda subclasses. Fibronectin seems to be present not only in mixed polyclonal but also in mixed monoclonal-polyclonal and in monocomponent cryoimmunoglobulins, and it may be bound to one of the immunoglobulin components of the cryoglobulins.
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PMID:Fibronectin in cryoimmunoglobulinaemias. 644 95


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