Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024623 (gastric cancer)
 36,219 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Formation of ribothymidine by the ribose exchange reaction between thymine and uridine with the cell-free extract of mouse Ehrlich ascites tumor cells was demonstrated. Since phosphate ions appear to be not required for this reaction, perhaps it proceeds by the mechnism of direct exchange of nucleoside N-ribosyltransferase. The transfer activity was found in the precipitates when the crude extract was fractionated with 30-60% saturated ammonium sulfate. Ribothymidine formation was also demonstrated between thymine and ribonucleosides other than uridine with this tumor extract. Production of ribothymidine from thymine and uridine was detected also by the use of extracts from lung, brain, and regenerating liver of normal rats, and from newborn rats (whole body). An extract of Rhodamine sarcoma exhibited the ribose exchange activity, while that of human gastric cancer did not.
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PMID:Formation of ribothymidine from thymine and ribonucleosides by the cell-free extract of tumors and rat tissues. 34 Apr 51

The prescription of a barium sulfate suspension suitable for the purposes of the double contrast radiograph of the stomach is reported. All chemical substances necessary for this may be got in every pharmacy. The method of the radiological examination inaugurated by Shirakabe is described with a slight methodical change. It is suited for all kinds of diagnoses (hiatal hernias, diverticula, ulcera, benign and malignant tumours, changes of the relief of mucosal foulds and so on) does not serve only for the early recognition of gastric cancer.
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PMID:[Simple prescription for double-contrast presentation of the stomach]. 121 Apr 76

Based upon our previous report indicating the presence of retrovirus-like particles in human gastric cancer cells, we analyzed the putative endogenous reverse transcriptase activity these particles should have. To evaluate the specificity of reverse transcription over that displayed by normal cellular DNA polymerases, the following discriminatory criteria were used: 1) resistance to high concentrations of Actinomycin D; 2) sensitivity to preincubation with ribonuclease A; 3) behavior in cesium sulfate isopycnic gradients and 4) size-shifting of putative template-product complexes after RNase exposure in agarose gel electrophoresis. We report a significant endogenous reverse transcriptase activity associated with membrane-encapsidated particles from terminally-illed patients but not in normal counterparts. Although these structures closely resemble retro viruses, a new model is proposed to explain our findings.
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PMID:Further characterization of RNA-dependent-DNA polymerase activity in human gastric cancer. 128 60

A human monoclonal antibody, BMMK-33G, was established by a fusion of human B-lymphoblastoid cells, HO-323, with lymphocytes of axillary lymph nodes obtained from a breast cancer patient. High-performance thin-layer chromatography (HPTLC)-immunostaining and enzyme-linked immunosorbent assay (ELISA) revealed that BMMK-33G was interestingly directed to enough sulfatide (Galactosylceramid-I2-sulfate), which is one of the sulfate ester containing glycolipids. By immunohistochemical staining, BMMK-33G intensely reacted to breast cancer, pancreatic cancer and gastric cancer. It also reacted to many normal human tissues including mammary glands, but these stainings were weaker than those for cancer. This report describes BMMK-33G, a human monoclonal antibody against sulfatide which may be very useful for studying not only tumor immunology but also autoimmune diseases.
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PMID:A human monoclonal antibody derived from axillary lymph nodes of a breast cancer patient reactive to a sulfated glycolipid. 160 9

A new antigen associated with pancreatic cancer was prepared by immunoaffinity chromatography using Fab'-Sepharose beads. This antigen was a glycoprotein of large molecular weight (Mr greater than 8,000,000) in its native state, estimated by size exclusion chromatography on Sephacryl S400. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotting analysis, several cancer-associated glycoconjugates, including CA19-9, CA50, Span-1, Dupan-2, and sialyl SSEA-1, were detected on the antigenic moiety of Mr 90,000. By an enzyme immunoassay for the antigen, elevated levels were found in pooled sera obtained from patients with various malignant and non-malignant diseases and normal subjects. However, the enhanced expression of CA19-9, Lewisa, or Lewisb epitope on the antigen molecule was restricted to the pooled sera from patients with pancreatic cancer. Furthermore, antigens from pancreatic or gastric cancer expressed ligands with intense and specific reactivity for Bauhinia purpurea (BPA), peanut (PNA), and Vicia villosa (VVA) lectins. The present assay system of the antigen, using both monoclonal antibodies (CA19-9, Lewisa, and Lewisb) and lectins (BPA, VVA and PNA), will provide a useful approach to the diagnosis of pancreatic cancer.
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PMID:Preparation of pancreatic cancer-associated mucin expressing CA19-9, CA50, Span-1, sialyl SSEA-1, and Dupan-2. 168 94

Cathepsin L activity was partially purified by S-Sepharose FF chromatography, concanavalin-A Sepharose chromatography, phenyl-Superose column chromatography, Mono S column chromatography, and TSK G3000SWXL column chromatography from gastric cancer tissue. The optimal pH of cathepsin L from gastric cancer tissue was 7.4, and the activity was retained even at alkaline pH. Heat stability tests showed that cathepsin L from gastric cancer tissue was heat stable; that is, 65% activity was retained after incubation at 56 degrees C for 60 min. The molecular weight of cathepsin L from gastric cancer tissue was estimated as 115 kD by gel filtration or 110 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme showed a different affinity for wheat germ agglutinin-Sepharose than cathepsin L from gastric normal mucosa. These results suggest that cathepsin L from gastric cancer tissue may play an important role in gastric cancer invasion through the destruction of the surrounding extracellular matrix by its proteolytic activity.
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PMID:Variant cathepsin L activity from gastric cancer tissue. 211 94

One hundred and twenty-one patients with gastric cancer of Borrman IV (type 4) were classified into two types according to the macroscopic appearance of their tumors, namely, those tumors with giant folds (type G, n = 84) and those without giant folds (type P, n = 37). A large percentage of the cases in both type groups had advanced stage carcinoma. Type G was found to be predominant in young women and the incidence of high-grade lymph node metastasis was higher in type G than in type P. Histochemically, it was shown that the tumor interstitium of type G contained obviously many more acid mucopolysaccharides (AMPS) than the localized Borrman II (type 2) gastric cancer, which was used as a control. The results of enzymatic digestion tests suggested that the amounts of hyaluronic acid, chondroitin sulfate, and sialic acid were greater in type G than in type P or the localized type, the differences involved being marked between type G and the localized type.
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PMID:Clinico-histochemical studies on type 4 carcinoma of the stomach--with special reference to mucopolysaccharides and sialic acid in tumor tissue. 247 Sep 45

NUGC4 cells derived from a human gastric cancer gave 6% Hanganutziu-Deicher (HD) antigen-positive cells by flow cytometric analysis using an affinity-purified chicken antibody to N-glycolyneuraminyl-lactosyl-ceramide (HD3 ganglioside). The cells showed no HD antigenic ganglioside by thin-layer chromatography enzyme-immunostaining; however, they were revealed to contain HD antigenic proteins with molecular masses of 150, 100, 90, 70, 65, 60, 47, and 40 kDa, by both immunoblotting after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoprecipitation of [35S]-methionine-labeled proteins, followed by SDS-PAGE and autoradiography. Neuraminidase treatment destroyed the antigenicity of all proteins, indicating that these molecules are glycoproteins and have N-glycolyneuraminic acid at the non-reducing terminal of carbohydrate chains as an HD antigenic epitope.
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PMID:Detection of glycoproteins as tumor-associated Hanganutziu-Deicher antigen in human gastric cancer cell line, NUGC4. 265 91

Cobalamin (vitamin B12) binding protein was purified from gastric cancer extracts and from serum-free culture medium of cancer cell line KATOH-III. The molecular weight, determined by immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was 70,000 and the pI was 2.8 to 3.2. From biochemical and immunological properties, this cobalamin binding protein was considered to be an isoprotein of cobalamin R binder. Monoclonal antibodies were produced against saliva R and cobalamin binding protein in culture medium to study their antigenic determinants. Monoclonal antibody 55-D reacted to an epitope of peptide in both binders, whereas WK-1 and H-12 reacted to determinants of a carbohydrate moiety, including sialic acid, in cancer cell-derived binder. In addition, we carried out an enzyme-linked immunoassay and examined plasma levels of immunoreactive R binder in patients with gastric cancer (n = 72), benign gastrointestinal disease (n = 30), and healthy individuals (n = 40). Even in patients without liver metastasis, the level of immunoreactive R binder detected by monoclonal antibody H-12 was elevated in some patients and decreased after excision of the tumor. R binder was also elevated in cancer tissue extract. Immunoreactive binder was histochemically detected in the cytosol of cancer cells and metaplastic cells of the gastric mucosa. The present findings suggest that cobalamin R binder is de novo synthesized in gastric cancer cells and that its plasma level increases in some patients. This binding protein may be a useful diagnostic and therapeutic parameter.
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PMID:Immunological characterization and clinical implication of cobalamin binding protein in human gastric cancer. 272 Jun 70

A newly established cancer marker, the PFK inhibition test, has been further examined for its capacity to detect malignant neoplasms irrespective of the organs in which cancer cells start proliferating. We tested 1,160 sera from cancer patients and compared them with 756 normal sera, using histograms and normal paper for analysis of accumulated frequency. PFK activity through the influence of normal sera showed normal distribution, and cancerous sera shifted to the inhibitory site with an irregular shape. From these analyses, the patients were classified into the following types: normal range: PFK greater than SD (standard deviation of PFK activity in normal sera); suspicious range: SD greater than PFK greater than 2SD, must be given the PFK test again; and dangerous range: PFK less than 2SD, further examination must be carried out to detect cancer. Fifty percent of the sera from all the cancer patients inhibited PFK beyond 2 SD of normal sera. We also analyzed organ-associated PFK distribution, eg, gastric, colorectal, and mammary cancer. In gastric cancer, PFK inhibition was stronger in accordance with how far a particular stage of cancer had progressed. However, 50% of sera from stage I gastric cancer patients was positive beyond the cut-off line of 2 SD. We examined 104 sera from patients diagnosed as benign prostatic hypertrophy and found malignant cells in 10 patients whose sera tended to be positive in PFK inhibition. The PFK inhibitory factor in the body fluids of cancer patients was fractionated by Sephadex G-75 gel filtration and DEAE ion exchange chromatography. The approximate molecular weight of this factor was 13,000 daltons. The factor was resistant to heat and acid (0.1 N HCl and H2SO4) and was sensitive to 0.1 N NaOH and phosphate buffer. Diluted sulfuric acid and ammonium sulfate made an inactive NaOH-treated sample active when lyophilized following dialysis against distilled water. PFK inhibition by cancerous sera was eliminated by fructose-2,6-bisphosphate (the strongest activator of PFK) in a dose-dependent manner. PFK attached to agarose beads was found to be reversible even after being inhibited by cancerous body fluids and ATP water solution. Although PFK is apt to decay in a low pH range, the established procedure did not destroy PFK, but induced a direct inhibition of PFK by ATP through the ATP inhibition site on the PFK molecule. The PFK inhibitor may possibly function as a proton carrier and release protons to activate the ATP inhibition site.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:PFK inhibition test for cancer detection: clinical applications and mechanisms of PFK inhibition. 295 72


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