Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1261473 (sarcoma)
 25,952 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Suramin--a well-known antitrypanosomal agent--was found to exert a strong inhibitory effect on the RNA-directed DNA polymerase (reverse transcriptase) activity of several oncornaviruses such as Moloney murine leukemia virus, murine Rauscher leukemia viruses, Moloney murine sarcoma virus and avian myeloblastosis virus. Inhibition of enzyme activity was obtained with both endogenous viral RNA and (A)n . oligo(dT) as the template-primer. Suramin effected a 50% inhibition of the reverse transcriptase activity of oncornaviruses at a concentration range of 0.1--1 microgram/ml. In this aspect it compared favorably to ethidium bromide, another trypanocide drug which is considered as one of the most powerful inhibitors of oncornaviral DNA polymerases. The inhibition of reverse transcriptase activity by suramin was competitive with the template-primer, (A)n . oligo(dT), suggesting that the drug may interact with the template-primer binding site of the enzyme.
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PMID:Suramin: a potent inhibitor of the reverse transcriptase of RNA tumor viruses. 9 62

Cultures of mouse Balb 3T3 fibroblasts exposed to a noncytotoxic dose of ethidium bromide for 16-18 hr are unable to produce foci after infection with murine sarcoma virus. Such cultures regain susceptibility to infection when incubated for 6-8 hr in drug-free growth medium. Pretreated but not untreated cultures exhibit sensitivity toward brief (6 hr) exposure to cycloheximide, chloramphenicol, and actinomycin D before infection. Pretreatment with cordy-cepin inhibits the ability of cultures to produce foci after infection. The recovery of ethidium-bromide-treated cultures requires the synthesis of cellular proteins which may have some important role in the establishment of RNA tumor virus infection.
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PMID:Requirement for cellular protein synthesis in reversal of ethidium-bormide-induced inhibition of cell transformation by murine sarcoma virus. 17 4

The gene order of the ml Moloney sarcoma virus (mlMSV) specific pP60gag (P60) was determined by direct chemical analysis of the polyprotein. P60 was cleaved with cyanogen bromide (CNBr) into eight partial and complete fragments ranging in mass from 10,000 daltons to 58,000 daltons. Peptide maps of these fragments were compared to maps of p15, p12, and three CNBr fragments of p30. The polarity of p15 and p12 in a CNBr fragment of P60 was determined by carboxypeptidase A digestion; likewise the CNBr fragments of p30 were ordered by aminopeptidase digestion. The linear arrangement of P60 CNBr fragments gave the gene order of NH2-p15-p12-p30-COOH. The m3 isolate of MSV expresses a P70 gag polyprotein. Peptide maps of 48,000-dalton CNBr fragments of m3 P70 and ml P60 were similar and suggested that both polyproteins were similar through the NH2-terminal two-thirds of p30. However, the presence of peptides unique to the 10,500-dalton COOH-terminal fragment of m1MSV p30 and not present in the p30 of either m3MSV or Moloney leukemia virus suggested that the gag gene deletion in the m1 isolate begins in the p30 reading frame.
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PMID:Chemical determination of the m1 Moloney sarcoma virus pP60gag gene order: evidence for unique peptides in the carboxy terminus of the polyprotein. 21 95

Immunoglobulins were isolated by affinity chromatography from sera of two patients with melanoma, one with sarcoma, and one with carcinoma. The affinity columns were prepared by covalently linking the membrane-rich fraction of biopsied melanoma cells to cyanogen bromide-activated agarose beads. The membrane-rich fractions were prepared by two methods: (a) hypotonic cell lysis, and (b) homogenization and differential centrifugation. Melanoma sera were autologous to melanoma membrane preparations. The isolated immunoglobulins showed immunoreactivity against antigens prepared from melanoma, sarcoma, and carcinoma cells by complement fixation but not against antigens prepared from normal human liver and lung tissues. Absorption of the isolated immunoglobulins with rabbit anti-human immunoglobulin immunobeads resulted in complete elimination of the complement-fixing antibody titer in one instance, whereas reduction occurred in other samples. Similar absorption with rabbit anti-human immunoglobulin M immunobeads resulted in reduction, but not complete elimination, of the antibody titers against target tumor cell preparations. These results suggest the presence of immunoreactive immunoglobulin G in all immunoglobulins and immunoglobulin M in some. Absorption of the isolated immunoglobulins with cultured sarcoma cells reduced but did not completely abolish antibody activity against autologous or allogeneic melanoma target antigen, whereas it did completely abolish activity against sarcoma target antigen. However, absorption with cultured allogeneic melanoma cells abolished the antibody activity against melanoma as well as sarcoma target antigens. The antibody titers of the isolated immunoglobulins were not affected by absorption with cultured lymphoblastoid cells. Since cultured melanoma and sarcoma cells were known to contain oncofetal antigen(s), these results suggest that the isolated immunoglobulins from cancer sera by melanoma membrane affinity chromatography were of at least two specificities: (a) antioncofetal; and (b) antitumor associated. The former group may be comprised of antibody to cross-reactive antigens associated with different histological types of tumors. However, it was apparent that a portion of the antibody activity was against common tumor-associated antigen(s). These results provide further evidence for the presence of common antigen(s) associated with biopsy specimens of human malignant melanoma.
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PMID:Isolation and immunochemical characterization of antibodies from the sera of cancer patients which are reactive against human melanoma cell membranes by affinity chromatography. 42 6

It is shown that L-cystine-bis-(N,N-beta-chloroethyl)-hydrazide-hydro-bromide possesses strong (50-100%) inhibitory effect in vivo against myeloma P-8, carcinosarcoma Walker, lymphosarcoma Pliss, sarcoma Yoshida, sarcoma Jensen and sarcoma 180 in doses 5-12 mg/kg/day. No suppression of the growth of Ehrlich ascites tumor was observed. The acute toxicity (LD50) of this substance on mice and rats is 71 mg/kg and 47 mg/kg respectively.
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PMID:A new substance effective against transplantable tumors in vivo: L-cystine-bis-(N,N-beta-chloroethyl)-hydrazide. 90 41

Change in immunosensitivity of various chemically modified cells to the specific antibody was investigated in the Donryu rat-Yoshida sarcoma system. Among various agents, Amphotericin-B and cetyltrimethylammonium bromide were effective in increasing the immunosensitivity. This effect was not due to the general damage of cell membrane but to the increase of antigen exposed on the cell-surface membrane.
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PMID:Change in immunosensitivity of Yoshida sarcoma produced by chemical modification of cell-surface membrane. 115 8

Formation of DNA-protein cross-links by the action of visible light in the presence of methylene blue was studied in calf thymus DNA-calf thymus histone complex and sarcoma-180 chromatin. The extent of cross-link formation decreases with a decrease in the histone to DNA ratio in the DNA-histone complex. In chromatin, it is at a maximum (93%) at a dye to DNA nucleotide ratio (D/P ratio) of 0.04 and is appreciable even at a very low dye concentration (75% at a D/P ratio of 0.0033). Sepharose 4B-CL column chromatography indicates that methylene blue acts as a mediator in the cross-linking process, but not as a linker in the DNA-protein cross-link. Dodecylsulphate-polyacrylamide gel electrophoresis patterns reveal that both histone and non-histone proteins are involved in cross-linking, but to a varied extent. Competition experiments with ethidium bromide demonstrated the necessity of intercalative binding of methylene blue in the formation of DNA--protein cross-links. Viscometric studies in 2 M NaCl indicate that the compact structure of chromatin is stabilized by cross-linking.
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PMID:Visible light induced DNA-protein crosslinking in DNA-histone complex and sarcoma-180 chromatin in the presence of methylene blue. 212 75

The polysaccharide fraction from the root of Angelica acutiloba Kitagawa showed a potent antitumor activity against ascitic form of Sarcoma-180, IMC carcinoma, and Meth A fibrosarcoma as well as the solid form of MM-46 tumor. An active polysaccharide, AR-4E-2, was purified by precipitation with cetyl-trimethylammonium bromide, anion-exchange chromatography on DEAE-Sepharose, and gel filtration on Sepharose CL-4B from the polysaccharide fraction. An active polysaccharide fraction showed a weak anti-complementary activity. AR-4E-2 was composed of arabinose, galactose, and rhamnose in the molar ratios of 3.3:1.0:0.7, and also contained 14.5% galacturonic acid and 3.2% protein. Methylation analysis and base-catalysed beta-elimination studies suggested that AR-4E-2 contained a rhamnogalacturonan moiety in which 2,4-di-substituted rhamnose residues were attached to 4-substituted galacturonic acid through position 2 of rhamnose. AR-4E-2 also contained highly branched 3,5-arabinan and (1----4)-galactan.
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PMID:Structural characterization and antitumor activity of a pectic polysaccharide from the roots of Angelica acutiloba. 235 65

We compared the colorimetric reactions between the 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl 2H-tetrazolium bromide (MTT) assay and the succinate dehydrogenase inhibition (SDI) test, in order to evaluate the usefulness of the SDI test for in vitro chemosensitivity testing. The addition of sodium succinate enhanced the colorimetric absorbance at 565 nm in the MTT assay in a dose- and a time-dependent manner, in mouse sarcoma-180 (S-180) cells. At 10 microM of sodium succinate, a dose used in the SDI test, the absorbance of the MTT assay increased by about 2.5-fold in the S-180 cells and in 10 human tumor tissues. The absorbance in the SDI test correlated well with the viable cell number of S-180 cells (r = 0.9993). These results show that the SDI test, using MTT as a tetrazolium salt, has a higher sensitivity for predicting cell viability, compared to the MTT assay.
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PMID:Sodium succinate enhances the colorimetric reaction of the in vitro chemosensitivity test: MTT assay. 318 53

A rapid and sensitive method was developed for the preparative separation of laminin subunits. Laminin was extracted and purified from mouse EHS sarcoma. On SDS-PAGE, the reduced and carboxymethylated molecule separated into two components corresponding to molecular weights of about 400 KDa (subunit A) and 200 KDa (subunit B). These two subunits were preparatively separated using heparin-agarose affinity chromatography. The larger subunit quantitatively adhered to the affinity column while the smaller one did not adhere. Amino acid analyses of the separated subunits showed distinct differences. Subunit B was further resolved into two distinct polypeptides of 200 KDa, B1 and B2, by means of reverse-phase HPLC. Although the amino acid compositions of B1 and B2 were very similar, the peptide maps generated by digestion of the B1 and B2 chains with Staphylococcus aureus V8 protease or by cyanogen bromide showed B1 and B2 to differ from each other. Thus, at least three different polypeptide subunits are present in this laminin and probably arise from separate gene origins. These studies provide a basis for the subsequent localization and analysis of the specialized structural and functional domains of laminin.
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PMID:Separation and characterization of the subunits of the laminin of EHS sarcoma. 320 18


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