Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038358 (gastric ulcer)
 5,179 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The distributions of acid alpha1-glycoprotein, alpha1-fetoprotein, beta-galactosidase and gastrin in gastric carcinoma and gastric ulcer as well as in the neighbourhood of these lesions were studied by means of immunohistochemical methods on imprint preparation. We could not find significant differences between gastric carcinoma and the nonneoplastic lesions, except for the acid alpha1-glycoprotein. The results of this first study indicate that the immunochemical and immunohistological assay of acid alpha1-glycoprotein might be of practical value in diagnosing malignant changes of gastric mucosa.
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PMID:[Immunohistochemical studies on non neoplastic and neoplastic gastric mucosa. Determination of embryonic and specific antigens (author's transl)]. 5 51

The antigen common for continuous epithelial cell lines and gastric mucosa of humans described earlier was studied. This antigen was revealed in one more cell line, namely in that prepared from human mammary carcinoma MDA-MB-231, noncontaminated with HeLa cells. The antigen described can be detected in the exophytely growing adenocarcinomas of the stomach and in the mucosa of the carcinoma affected stomach at a distance of 10--12 cm from the site of affection; no such antigen was revealed in the endophytely growing carcinoma of the stomach and in mucosa areas surrounding gastric ulcer. The antigen is not a glycoprotein since glycoprotein fractions obtained by means of 1.2 M perchloric acid from the normal stomach mucosa homogenate and the E 16b extract were inactive in immunodiffusion with a sensitive serum. The electrophoretic mobility of the antigen was similar to that of globulin alpha1-beta2. This antigen is of interest since its detection or absence would possibly aid in determination of the initial type of cells from which development of carcinoma occurred, and in more precise recognition of the histological form of carcinoma of the stomach.
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PMID:[Study of the "continuous cell antigen" and the human gastric mucosa]. 10 92

Gastric juice was neutralized (nGJ) in vivo by 80 ml of a phosphate buffer containing radiolabelled vitamin B12 as dilution indicator. Unprocessed nGJ was analyzed in the double gel diffusion technique for the presence of serum proteins using monospecific antisera. Alpha1-Acid glycoprotein (AGP) was found in a high incidence (36 out of 38 subjects) in nGJ of gastric cancer patients. AGP was also observed less frequently in nGJ of patients with Billroth II resections (6/15), metaplasia (11/52), gastric ulcer (3/24), chronic atrophic gastritis (2/26) and chronic gastritis (3/63). AGP was absent in the control group (0/21), in patients with surface gastritis (0/38) and in subjects with normal acid secretion (0/45). Immunochemical studies demonstrated no identity of AGP with human "gastrointestinal tumor associated antigens." In 7 out of 17 AGP positive samples immunochemical differences between gastric and serum AGP were observed.
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PMID:Alpha 1-acid glycoprotein in gastric cancer juice. 80 43

The output and concentration of gastric glycoproteins in gastric juice from patients with chronic duodenal and gastric ulcer and from controls, have been determined in the basal state and following pentagastrin stimulation. Patients with gastric ulcer had a significantly higher basal glycoprotein output, basal glycoprotein concentration and stimulated glycoprotein concentration than patients with duodenal ulcer or controls. The basal and stimulated glycoprotein output in gastric juice from patients with duodenal ulcer and controls was independent of ABO blood group and secretor status. The carbohydrate composition of the gastric glycoproteins has also been determined in the basal state, and following stimulation of gastric juice by pentagastrin, which did not influence the carbohydrate composition of the molecules. The principal carbohydrate components were galactose, N-acetylglucosamine, fucose, N-acetylgalactosamine, and sialic acid. Small amounts of mannose and glucose were detected in some gastric glycoprotein samples. The carbohydrate composition of the glycoproteins varied according to the ABO blood group and secretor status of the individual. Glycoproteins form stimulated gastric juice from non-secretors of groups A and O had a higher sialic acid content than glycoproteins from secretors of the same blood groups. There were no significant differences in the carbohydrate composition of glycoproteins from patients with chronic gastric and duodenal ulcer compared with gastric glycoproteins from control subjects of the same blood group and secretor status.
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PMID:Gastric glycoproteins in chronic peptic ulcer. 106 83

A new monoclonal antibody has been developed which is capable of detecting structures in gastric mucus glycoproteins expressed in the fetus and in adult gastric mucosa in conditions such as gastric carcinoma. Cancer associated monoclonal antibodies were selected by testing them against various mucous glycoprotein samples from the alimentary tract, including salivary glycoproteins from both secretory and non-secretory subjects, and cancerous and normal gastric juice glycoproteins. They were tested against 1000 samples of gastric juice from an unselected population. Immunochemical characterisation suggested that the glycoproteins picked up by P4 and i11 include one of the compounds reacting with rabbit anti-fetal sulphoglycoprotein antigen serum. On the basis of a clinical trial and immunohistological evaluation further evidence was obtained of P4 as the most promising antibody for further experimentation. A total of 302 gastric juice specimens from patients with various gastric symptoms were analysed using the enzyme linked immunosorbent assay technique and P4 antibody. Of 10 gastric cancers, nine had P4 in the gastric juice. A positive correlation was found between gastric ulcer and the appearance of P4. Duodenal ulcers were not correlated to P4. Atrophic gastritis and P4 coincided less frequently. Raised P4 values were found in between 3% and 9% of subjects, depending on the population. Cancer cases showed high P4 values, which allows adjustment of the lower limit of a positive result to high level whereby a considerable number of non-cancerous P4 positives are omitted.
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PMID:Gastric cancer associated structure in mucus glycoproteins shown as a clinically useful marker. 148 73

Zinc sulfadiazine (ZnSD) 50, 100, 200 mg/kg ig inhibited the formation of gastric ulcer induced by indomethacin, stress and pyloric ligation in rats respectively and showed dose-dependently. ZnSD 200 mg/kg ig accelerated the healing of gastric ulcer induced by acetic acid. ZnSD 25 mg/kg ig was effective in preventing ethanol-induced damage of rat gastric mucosa. The amount of gastric mucus glycoprotein in gastric tissues was increased by ZnSD. In general, ZnSD did not influence the volume of gastric juice and pepsin output, but ZnSD 200 mg/kg ig decreased gastric acidity. In vitro, ZnSD also influenced the neutralization of acid. It is suggested that antiulcer action of ZnSD may be related to its preservation of the gastric mucosal barrier and neutralization of acid.
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PMID:[Anti-gastric ulcer activity of zinc sulfadiazine in rats]. 213 Jun 5

Many studies have postulated the role of gastric acid and mucosal microcirculation in the development of gastric ulcer. We considered that gastric mucosal glycoprotein played one of the most important roles as the defensive factors of te gastric mucosa. The purpose of this study is to investigate te location and distribution of glycoprotein in the gastric mucosa in normal and stressful condition. Male Wistar rats, weighing 250 g were used as the experimental animals. Alternation and distribution of glycoprotein in the gastric mucosa were studied by light and electron microscopic examination employing HRP-labeled lectin such as PNA, DBA, ConA, RCA, SBA, WGA and UEA-1 as a parameter before and after the development of stress ulcer. Around Thirty percent scalding burn of the rat body surface area was created. At 2, 5 and 24 hours after burn induction, the gastric mucosa was examined. PNA-binding sites which were primarily localized to the generative cell zone in the control rat appeared to extend from the upper layer to the intermediate or the basal layer of the gastric mucosa in accordance with the development of stress ulcer after burn. Most of the binding sites was detected in the parietal cells particularly along microvilli in the intracellular secretory canaliculi. The tubulovesicular system in the parietal cells became stainable with PNA in the stress-loaded rats. Alternation and binding pattern of lectin, especially of PNA may indicate the local response of the parietal cells of the gastric mucosa against the stress.
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PMID:[Alteration of the gastric mucosal glycoprotein in stress]. 238 80

We developed a simple method of determining gastric juice viscosity using a cone plate viscometer and tested its clinical application in the staging of peptic ulcers. We found a significant positive correlation between viscosity and macromolecular glycoprotein concentration of gastric juice (P less than 0.001). Gastric juice viscosity in active and healing gastric ulcer patients was significantly lower than that in the scarring stage or hospital control patients (P less than 0.05 and P less than 0.01, respectively). In duodenal ulcer patients, a significant difference was found between the active and healing stages and hospital controls (P less than 0.01). However, the difference between the active and healing stages and the scarring stage was not significant. Gastric juice viscosity is a simple, reliable, clinically useful measure.
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PMID:Clinical significance of gastric juice viscosity in peptic ulcer patients. 340 93

Changes in the incorporation of 3H-glucosamine into the macromolecular glycoprotein during the healing process of acetic acid induced gastric ulcer in rats were sequentially examined in the ulcer region and the intact region at 2, 10, 40, 80 and 365 days after the operation. 1) The total radioactivity (Tissue + Medium) and the radioactivity which remained in the tissue after incubation of the ulcer region were increased significantly as compared with those of the control at 2 days after the operation (275, 175% of the control, respectively), and then total radioactivity returned to the control level. On the other hand, the radioactivity in the tissue was gradually decreased, and then it became 50% of the control at 365 days. In contrast, the incorporating activity into the macromolecular glycoproteins was decreased to 50% of the control at 2 days, and was once recovered to the control level at 10 days. After 40 days, it was again decreased to 50% of the control and became 30% at 365 days. 2) Changes in the incorporation of 3H-glucosamine into the macromolecular glycoproteins of the intact region of rats with ulcers were the same as that of the ulcer region. 3) Elution profiles of gel filtration of the macromolecular glycoproteins isolated from the relapse and recurrence region of rats with ulcers at 365 days were the same as that of the healing region, and their radioactivities were decreased to 30% of the control. The results suggested that such a decrease in the biosynthetic activity of the macromolecular glycoproteins extending over the whole gastric tissue is one of the reasons for the increased relapse and recurrence.
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PMID:[Changes in the biosynthetic activity of gastric glycoproteins during the healing process of acetic acid ulcer in rats]. 402 4

The isolation and composition of glycoproteins from mucosae of normal stomachs, of stomachs with gastric ulcer, and of stomachs with carcinoma is described. The glycoproteins from the mucosae of normal stomachs and with gastric ulcer showed virtually the same carbohydrate and amino acid content as the principal gastric glycoprotein isolated from gastric aspirates. They all revealed a common basic carbohydrate composition: galactose, fucose, glucosamine, and galactosamine were present in approximate molar ratios of 4:3:3:1. THE RESULTS SUGGEST THAT THE GLYCOPROTEINS ISOLATED FROM GASTRIC ASPIRATES FROM NORMAL AND NEOPLASTIC GASTRIC MUCOSAE SHARE A NUMBER OF STRUCTURAL FEATURES: (1) a protein core with a characteristic amino acid composition; (2) the range of sugars forming the carbohydrate side chains; (3) galactosamine approximately equimolar with the sum of threonine and serine; (4) galactose approximately equimolar with the sum of glucosamine and galactosamine; (5) absence of mannose; (6) a high carbohydrate content (80-85%); and (7) blood group activity. The neoplastic glycoproteins differed from the normal glycoproteins in that the quantitative relationships of the carbohydrate components of the neoplastic glycoproteins showed variations dividing the extracts investigated into groups, each group with a distinctive and constant carbohydrate composition. The blood group specificity of 15 out of 24 cases investigated differed from that of the hosts' red cells.
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PMID:A comparative study of the major glycoprotein isolated from normal and neoplastic gastric mucosa. 470 16


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