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)

Using a simple hemoglobin method on the basis of Anson-Mirsky's method, acid protease levels in serum were measured at pH 1.8 (pepsin) and pH 3.5 (gastricsin) in 18 healthy controls and 14 patients with duodenal ulcer, 19 patients with gastric ulcer and 18 patients with gastric cancer. Though acid protease activity in pH 1.8 in duodenal ulcer has a tendency to show a little higher level than healthy controls, there is no significant difference in acid protease levels between controls and each of three diseases.
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PMID:Estimation of serum acid proteases at pH 1.8 and pH 3.5 in patients with duodenal ulcer, gastric ulcer and gastric carcinoma. 2 29

Morphological and biochemical changes reflecting the process of genesis of experimental stomach cancer were studied and compared in experiments carried out on 170 rats to whom N-methyl-N'-nitro-N-nitrosoguanidine had been given in drinking water. The concentration of the compound in drinking water was 167 mg/l. Malignization mostly developed during the ingrowth of the epithelial complexes involved in the process of carcinogenesis into the submucous membrane, in rare cases, into the mucous membrane itself. The results of experiments showed that biochemical changes preceded morphological alterations. The signs of inhibition of the synthesis of the isoenzyme spectrum of pepsinogen-pepsin revealed the qualitative changes of biochemical processes of the epithelium. A possible dependence of morphological features of the process of carcinogenesis on the evolutionally-established functional peculiarities of rat stomach epithelium is discussed.
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PMID:Morphological and biochemical changes induced in rat stomach by N-methyl-N'-nitro-N-nitrosoguanidine. 47 27

1. Electrophoretic separation of proteases from human gastric mucosal extracts of five patients with gastric ulcer, one with duodenal ulcer and three with gastric cancer were investigated by agar-gel electrophoresis at pH 8.3 and pH 5.0. 2. In the fundic mucosal study, there were seven faster moving proteases in all nine cases, but the slowest moving protease showed a slightly different picture in each case. In the antral mucosal study, two of eight cases showed mainly group II pepsinogens, seven of nine cases, however, showed the same results as in the fundic mucosal study. 3. In the cases of the nine mucosal extracts activated at pH 1.5 or pH 4.0, they all showed the same electrophoretic separation at each pH level. At these two pH levels, however, quite different electrophoretic patterns were observed. The presence of pepsin 3 appeared to diminish at the higher levels of pH, although that of pepsin 5 and pepsin 7 appeared to increase at pH 4.0 and above. Pepsin 6 appeared for the first time at pH 4.0 and existed at higher pH levels. 4. We thus conclude that electrophoretic patterns of pepsins in the gastric mucosal extracts are changeable depending on the pH level of the incubating medium, and further that diversity of pepsins in gastric juices may also depend on the pH level of gastric juices.
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PMID:Studies on the pepsinogens of human gastric mucosal extracts. 74 87

Up to 19--20 fractions of separate RNA species and groups have been revealed in malignant tumors of the stomach and mucous membrane of patients with stomach cancer, ulcer and polyposis of the stomach by means of the method of analytical and preparative electrophoresis in 2.5% polyacrylamide gel. A more intensive incorporation of 14C uridine both into the nuclear and separate fractions of cytoplasmic RNA was observed in stomach tumors in comparison with the stomach mucous membrane of man. Pepsinogen-pepsin was synthesized by bound polysoms of the stomach mucous membrane. In stomach malignant tumors of man the polysomes were not capable of synthesizing this enzyme. Fractions of messenger RNA with sedimentation constants 16S-17S, possessing the ability to stimulate pepsinogen-pepsin synthesis in vitro, have been isolated from cytoplasmic RNA of a pig stomach mucous membrane.
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PMID:Realization of genetic information programming the synthesis of pepsinogen-pepsin in the mucous membrane and tumors of the stomach in man. 79 Feb 10

This case-control study of Hawaiian Japanese indicated that gastric ulcer in the proximal portion of the pyloric antrum has features similar to those of gastric cancer. Such ulcers occurred at sites most frequently and most severely affected by intestinal metaplasia, although metaplasia tended to be more extensive with cancer than with ulcer. Metaplastic mucosa was more vulnerable to the action of pepsin and acid than was normal mucosa. The risk of ulceration would rise when a sufficiently lagrge area of the antrum was intestinalized and when the corpus continued to produce significant quantities of these substances. This study showed a strong association between salt intake, ulcer, and metaplasia. Significant but less dramatic associations were demonstrated between metaplasia and the use of traditional Japanese foods and smoking. The question was raised as to whether salt promotes ulceration or whether it potentiates the action of a mutagen that causes intestinal metaplasia.
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PMID:Epidemiologic pathology of gastric ulcer and gastric carcinoma among Japanese in Hawaii. 83 57

Serum pepsinogen I and pepsinogen II levels in 369 healthy controls, 38 duodenal ulcer, 30 gastric ulcer and 46 stomach cancer including 21 early and 25 advanced gastric cancer patients were measured by enzyme-linked immunosorbent assays using pepsin moiety-reacting monoclonal antibodies to pepsinogens I and II. Serum pepsinogen I and pepsinogen II levels were higher in the duodenal and gastric ulcer groups than in the control. Although there was no significant difference in serum pepsinogen II between stomach cancer and control, serum pepsinogen I was significantly lower in the former than in the latter and also in advanced gastric cancer than in early gastric cancer. A specific negative correlation of serum pepsinogen I with patient age was observed in stomach cancer but not in peptic ulcer or control groups. Receiver operating characteristic analysis was performed and indicated that serum pepsinogen I, compared with serum pepsinogen II or the pepsinogen I/pepsinogen II ratio, is the most effective marker for stomach cancer.
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PMID:Enzyme-linked immunosorbent assays for serum pepsinogens I and II using monoclonal antibodies--with data on peptic ulcer and gastric cancer. 316 82

Pepsin is a potent proteolytic enzyme stored and secreted by chief cells in an inactive precursor form, pepsinogen. Its secretion is modulated by both cAMP and calcium-dependent mechanisms. Abnormalities in levels of pepsinogen and its various isozymogens have been linked clinically, epidemiologically, and experimentally to peptic ulcer disease and gastric carcinoma. The ulcerogenesis of pepsin stems from its ability to breach gastroduodenal mucosal barriers. Furthermore, certain isozymogens seems abundant and hyperactive in patients with peptic ulcer disease. The etiology and significance of low pepsinogen levels with disproportionate elevations of pepsinogen II and pepsin 5 in gastric cancer and its precursors is less clear. Further exploration of the patho-physiologic role of pepsin is likely to be of considerable importance in initiating further advances in the understanding and treatment of upper gastrointestinal disease.
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PMID:Pepsinogen. Prolate ellipsoid or unrecognized pathogen? 330 25

The serum level of pepsinogen I (PG I) and pepsinogen II (PG II), and the PG I/PG II ratio were compared with the surface area of the fundic mucosa, as determined endoscopically by the Congo red staining method. Reduction in the area of the fundic mucosa due to gastritis was associated with stepwise reduction in the PG I levels and the PG I/PG II ratios. Reduction in the area of the fundic mucosa was also associated with decreases in the basal acid output, maximal acid output (MAO), the basal pepsin output and the stimulated pepsin output. The best sensitivity and specificity levels for the diagnosis of normal mucosa and severe gastritis were obtained with the PG I/PG II ratio and the MAO. A retrospective study of 58 patients with gastric cancer and 162 cancer-free patients showed that a PG I/PG II ratio identified 86.2% of all carcinomas and 87.5% of early carcinomas. Although this test gave a positive rate of 36% among the cancer-susceptible age group controls, its use would lower the cost of mass screening by targeting a smaller test population.
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PMID:Serum pepsinogens as a screening test of extensive chronic gastritis. 359 51

The paper deals with the description of a simple, time-saving and sufficiently precise procedure of determining the activity and level of pepsinogen-pepsin in the gastric juice of healthy subjects and those at high risk for stomach carcinoma by means of photography. The level of pepsinogen-pepsin in the gastric juice of stomach cancer patients is generally found to be very low or nil. A considerable drop in the enzyme's activity is also observed in cases of polyposis of gastric mucosa as well as in ana- and hypoacidic states. The procedure may be used for assessment of the secretory function of gastric mucosa and screening for groups at high risk for stomach carcinoma.
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PMID:[Use of the pepsinogen-pepsin test in examining persons at high risk of stomach cancer]. 679 18

The supernatant of a cell line of squamous cell carcinoma of the head and neck (SCCHN), PCI-50, was previously shown to induce activation, promote proliferation and increase antitumor cytotoxicity of freshly purified human natural killer (NK) cells and CD4+ T lymphocytes [Arch Otolaryngol Head Neck Surg (1994) in press]. This supernatant was found also to promote the growth of a variety of hematopoietic cell lines, including Jurkat, THP-1, K562, NK-92 or Epstein-Barr-virus-transformed B cell lines. The Jurkat cell line was selected as a reporter cell in an 18-h proliferation assay established to measure the growth-promoting activity of PCI-50 supernatant. The presence of soluble tumor-derived factors able to induce proliferation of Jurkat cells was demonstrated in the supernatant produced by several other SCCHN cell lines but not in that produced by a gastric cancer cell line (HR) or renal cell carcinoma line (5117G8). The growth-promoting PCI-50 supernatant was shown to contain 28 +/- 0.5 pg/ml interleukin-6 (IL-6) in vitro but was negative for interferon gamma, IL-1, IL-2, IL-4, tumor necrosis factor alpha, granulocyte/macrophage-colony-stimulating factor and IL-12. The addition of any of these recombinant cytokines to Jurkat cell cultures did not significantly promote growth, while PCI-50 supernatant was consistently growth-stimulatory. This supernatant neither enhanced intracellular Ca2+ concentration in Jurkat cells nor induced up-regulation of activation antigens on the cell surface, although it supported growth of Jurkat cells in the absence of IL-2. The growth-promoting activity in the PCI-50 supernatant was acid-labile at pH 2 for 4 h, heat-resistant at 96 degrees C for 1 h and sensitive to treatments with trypsin and pepsin. Preincubation of the PCI-50 producer cells with tunicamycin or cyclohexamide reduced the level of growth-promoting activity in the supernatant. A partial purification of this activity was achieved using Amicon filtration, chromatography on concanavalin-A-Sepharose and then a hydroxyapatite column and high-pressure liquid chromatography gel filtration. The partially purified glycoprotein had a molecular mass of 50-70 kDa, as determined by gel filtration.
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PMID:Proliferation of hematopoietic cell lines induced by a soluble factor derived from human squamous cell carcinomas of the head and neck. 800 Oct 29


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