Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two mouse monoclonal antibodies (MoAbs), B10 and 1H5, were generated by fusing mouse myeloma NS-1 cells with spleen cells from a BALB/c mouse immunized with Ueda-1 cells derived from human squamous cell carcinoma (SCC) of the floor of the mouth. Immunohistochemical analysis revealed that these MoAbs recognize the filamentous components of cytoplasm which were protein in nature. While the pattern of antigen distribution in various cell lines was not cell-type specific, reactivity of these antibodies with tissue sections was informative. MoAb 1H5 was preferentially reactive with well-differentiated squamous cell carcinoma, however, reaction with adenocarcinoma was observed infrequently. This antibody also preferentially reacted with the spinous layer of normal stratified squamous epithelium. MoAb B10, however, was reactive with nonepithelial tissues as well as with epithelial ones, and its level of binding bore no relationship to the grade of histologic malignancy. SDS-PAGE and Western blotting analysis, using cytokeratin extracts of Ueda-1 cells and human epidermis, demonstrated that MoAb B10 reacted with a wide range of keratin proteins of 65-67K, 58K, 56.5K, 56K, 52K, 50K, 48K, 45K, 40K, 38K, 36K, and 34K molecular weight (MW), while MoAb 1H5 reacted with keratin proteins of 65-67K, 58K, 56.5K, 56K, 52K, 48K, and 34K MW. These results suggest that MoAb 1H5 may recognize keratin subfamilies related to squamous differentiation, whereas MoAb B10 recognizes a wide range of keratin proteins, and may even react with other kinds of intermediate filament proteins (IFPs).
Cancer 1987 Dec 15
PMID:Monoclonal antibodies against human oral squamous cell carcinoma reacting with keratin proteins. 244 66

Free alpha subunit (PU alpha) was extracted and purified from the urine of normal term pregnant women, and examined for molecular weight, electric charge, affinity to lectins (ConA, RCA and PNA) and the ability to combine with hCG beta in comparison with hCG alpha dissociated from hCG in vitro. The molecular weight of PU alpha was greater than that of hCG alpha in gel chromatography, but smaller in SDS-PAGE. However the free alpha subunits from the urine of patients with cancer were estimated to be larger than those of hCG alpha by both methods. In isoelectric focusing, while hCG alpha exhibited a neutral charge, PU alpha exhibited a negative charge. After treatment with sialidase, both hCG alpha and PU alpha were shifted to the basic region, indicating that they contained terminal sialic acid residues. The affinity to lectins indicated that PU alpha may contain both asparagine-linked and O-linked oligosaccharides, while hCG alpha contains asparagine-linked oligosaccharide only. PU alpha scarcely showed any combining activity with hCG beta, whereas hCG alpha combined actively. The O-linked oligosaccharide, which is not present in hCG alpha, may cause PU alpha to fail to combine with hCG beta.
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PMID:[The characterization of free alpha subunit purified from the urine of normal term pregnant women]. 244 2

A monoclonal antibody (MAb 76) was produced by immunizing mice with a soluble cytoplasmic protein fraction from a human adenocarcinoma of the colon. MAb 76 showed specific immunoreactivity against a 76 kDa protein in immunoblot studies using total colon tumor cytosol proteins. Immunoprecipitation of phosphorylated cytosolic protein products with MAb 76 and subsequent analysis on SDS containing polyacrylamide gels revealed a single 38 kDa band, indicating that the 76 kDa antigen is associated with a 38 kDa phosphoprotein species. Indirect immunofluorescence analysis of primary tumor specimens and human colon tumor cell lines showed positive immunoreactivity with 6/7 human colon adenocarcinoma tissues and 15/18 human colon tumor cell lines. MAb 76 was unreactive with normal colon, liver and lung specimens from human, mouse and hamster. The epitope-bearing monomer detected by MAb 76 is immunologically conserved in a high percentage of colon tumor cells and tissues and may represent a cellular product that is characteristic of the transformed colon cell phenotype.
Cancer Lett 1988 Mar
PMID:Characterization and reactivity of a monoclonal antibody that recognizes a 76 kilodalton human colon tumor antigen. 245 9

The flavoprotein DT-diaphorase (EC 1.6.99.2) is believed to play an important role in the body's defense system. This enzyme has been purified 13,000-fold with a recovery of 58% from a cytosolic fraction of abdominal fat obtained from an obese patient undergoing elective surgery. Purification of the enzyme to electrophoretic homogeneity was achieved after two chromatographic steps: (1) affinity chromatography on azodicumarol Sepharose 6B; (2) anion exchange chromatography on DEAE Sephacel. The enzyme exhibits a monomer molecular mass of 32 kDa in SDS-PAGE and has 1 FAD prosthetic group per 32 kDa monomer. The FAD prosthetic group appears to be firmly attached to the apoproprotein. The enzyme reduces azodyes and quinones and demonstrates a broad substrate specificity. The enzyme has characteristics that are similar to DT-diaphorase purified from rodent liver, especially the rat liver enzyme. Estimated Km values for NADH, NADPH and menadione are 200, 140 and 3.3 microM, respectively. Vmax values for these substrates in the same order are 762, 667 and 294 mumol/mg.min. Dicumarol and warfarin exhibited competitive inhibition with pyridine nucleotides. The inhibition constants (Ki) for the drugs were estimated to be 10 nM and 2.2 microM, respectively. When compared to several other tissues, abdominal fat has one of the highest DT-diaphorase activities (Martin, L.F., Patrick, S.D. and Wallin, R. (1987) DT-diaphorase in morbidly obese patients. Cancer Lett., 36, 341-347), but the specific role of the enzyme in human fat is unknown.
Cancer Lett
PMID:Human DT-diaphorase, a potential cancer protecting enzyme. Its purification from abdominal adipose tissue. 246 Feb 16

Antinucleolar antisera were raised in rabbits, goats and sheep to nucleoli isolated from three human tumor cell lines. The antisera were shown to cross-react by immunofluorescence with human tumor cell lines originating from different organs and with frozen sections from a wide variety of human malignant and non-malignant tissues. Tumor versus normal tissue discrimination by several antisera was significantly improved by treatment of frozen tissues with a buffered glutaraldehyde/Triton X-100 solution prior to immunofluorescent staining. The molecular specificity of these antisera was determined by immunostaining electrotransfer nitrocellulose strips following SDS-PAGE of nucleolar preparations and nuclear extracts. Although different immunostaining patterns were obtained for individual antinucleolar antisera, nucleolar proteins of molecular weight 120, 100, 94, 68, 54, 38, 33, and 32 kDa were the most often recognized by antisera raised in the three different species. G187 antiserum strongly reacted with 100, 94, and 38 kDa proteins from freshly obtained leukemic specimens. The Immunoreactivity of the 100, 94, and 38 kDa proteins was unaffected by glutaraldehyde/Triton X-100 treatment when immunostained with antisera that demonstrated the greatest tumor specificity on sections treated with glutaraldehyde/Triton X-100. These three nucleolar proteins may be more highly associated with nucleoli of malignant cells than with nucleoli of normal cells.
J Cancer Res Clin Oncol 1989
PMID:Immunohistochemical and biochemical characterization of antisera raised to human tumor nucleoli. 250 20

We have found that preparations of rate-zonal purified Moloney murine leukemia virus originally obtained from the National Cancer Institute Resources Program, when separated by SDS-PAGE in the absence of mercaptoethanol (beta-MSH), exhibited a doublet envelope glycoprotein band of approximately 69/67 kD. When the same samples were run in the presence of beta-MSH, a single band at 70 kD (gp70) was observed. Western blot analysis with polyclonal antiserum identified both the 69- and 67-kD bands as envelope gene products. Tryptic peptide mapping of each of the gp67 and gp69 bands confirmed the serological data, with each showing conserved as well as unique peptides. These results imply that the Moloney murine leukemia virus samples examined above contain two structurally different envelope gene products. Western blot analysis using ecotropic and dualtropic specific sera suggest that gp69 is derived from an ecotropic virus, while gp67 is from a dualtropic virus. This is consistent with the results of an earlier study which showed that the majority of the cysteines (4/5) in dualtropic gp70 are lost by a single deletion relative to the ecotropic gp70 species. This would account for the difference in mobility observed in the SDS-PAGE profile in the absence of beta-MSH. It would indicate that the cysteines play an important role in defining structural differences that separate the ecotropic and dualtropic gp70s.
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PMID:Reduction-modifiable properties of Moloney murine leukemia virus gp70 as an indicator of envelope glycoprotein heterogeneity. 252 96

Cell motility (i.e., movement) is an essential component of normal development, inflammation, tissue repair, angiogenesis, and tumor invasion. Various molecules can affect the motility and positioning of mammalian cells, including peptide growth factors, (e.g., EGF, PDGF, TGF-beta), substrate-adhesion molecules (e.g., fibronectin, laminin), cell adhesion molecules (CAMs), and metalloproteinases. Recent studies have demonstrated a group of motility-stimulating proteins which do not appear to fit into any of the above categories. Examples include: 1) scatter factor (SF), a mesenchymal cell-derived protein which causes contiguous sheets of epithelium to separate into individual cells and stimulates the migration of epithelial as well as vascular endothelial cells; 2) autocrine motility factor (AMF), a tumor cell-derived protein which stimulates migration of the producer cells; and 3) migration-stimulating factor (MSF), a protein produced by fetal and cancer patient fibroblasts which stimulates penetration of three-dimensional collagen gels by non-producing adult fibroblasts. SF, AMF, and MSF are soluble and heat labile proteins with Mr of 77, 55, and 70 kd by SDS-PAGE, respectively, and may be members of a new class of cell-specific regulators of motility. Their physiologic functions have not been established, but available data suggest that they may be involved in fetal development and/or tissue repair.
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PMID:Protein factors which regulate cell motility. 255 6

The secretion of elevated levels of proteinases is considered to be a distinct property of most transformed cells. The cellular and secreted levels of plasminogen activators and collagenases have been examined in the nonmalignant human osteosarcoma (HOS), the malignant Kirsten murine sarcoma virus transformed (KHOS/NP), the temperature sensitive revertant of virus transformed HOS (KHOS-240S) and N-methyl-N'-nitro-N-nitrosoguanidine transformed HOS (MNNG/HOS) clones. Virus and MNNG transformed clones exhibit 100- and 7-fold higher cellular and and 270- and 30-fold higher extracellular plasminogen activator (PA) activity as compared with untransformed HOS controls. The cellular PA activity of the revertant clone is similar to but the secreted level is slightly higher than the HOS controls. SDS-PAGE in the presence of casein and plasminogen is consistent with the major PA species of urinary type (u-PA) and with the absence of PA inhibitor in the parent and revertant clones. The cellular levels of active collagenase are low in all the clones. However, on activation by trypsin, the two active collagenase bands of similar intensity are observed for all the lines in SDS-PAGE in the presence of gelatin. While there appears to be some elevation of secreted collagenase prior to trypsin activation, the activated collagenases appear to have the same size and activity in all of the clones.
Cancer Lett 1989 Sep 15
PMID:Synthesis and secretion of plasminogen activators and collagenases in human cells transformed by Kirsten murine sarcoma virus and N-methyl-N'-nitro-N-nitrosoguanidine. 256 62

A preparation procedure is presented for the determination of tyrosinase-catalysed stereo-specific dopa oxidase activity in serum. Purification is obtained by separation on a Phenyl-Sepharose hydrophobic interaction column, followed by Con-A-Sepharose chromatography. Five out of seven sera from patients with widespread melanoma metastases were found to contain detectable quantities of tyrosinase. There was no tyrosinase activity in seven sera from patients with other malignancies, nor in six other control sera from individuals without malignancies. One serum which showed high tyrosinase activity was processed as above and studied by SDS-PAGE. A dopa-reactive band with an apparent MW of 66 kD was present in the gel, i.e. at the same place as that of the soluble tyrosinase of cultured human malignant melanoma cells. The protein was found to have the same pI at isoelectric focusing, and eluted in the same way from the preparation columns used, as did soluble tyrosinase.
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PMID:Tyrosinase activity in serum from patients with malignant melanoma. 256 28

Polyclonal and monoclonal antibodies were used to characterize human milk fat globule (HMFG) membrane antigens, using gel filtration, ion exchange chromatography and western blotting. Although originally generated against HMFG, monoclonal antibodies also reacted with skim milk. In western blotting, several antigen molecules were seen, of which some were detected by all available antibodies, and one only with monoclonal antibody III D5, previously shown to react with mammary and ovarian carcinomas bearing estrogen receptors. This or these antigens, with a molecular weight of about 53 kd, were isolated by fractionation in SDS-PAGE. A low polypeptide content was demonstrated but the antigenic structure could be stained with periodic-acid-Schiff and biotinylated peanut agglutinin, indicating the presence of galactose or N-acetylgalactosamine residues. While this 53-kd molecule is the only determinant exclusively stained by III D 5 antibody, it is suggested that it carries epitopes related to estrogen receptor activation.
Int J Cancer 1985 Feb 15
PMID:Characterization and partial purification of human milk fat globule membrane antigens by polyacrylamide gel electrophoresis and immunoblotting using monoclonal antibodies. 257 30


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