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)

In normal human tissues, pepsinogen A mRNA was expressed only in the fundic mucosa of the stomach, whereas pepsinogen C mRNA was expressed in all regions of the stomach mucosa and also in the proximal duodenal mucosa. The distributions of these mRNAs were consistent with those of pepsinogens A and C in the gastroduodenal mucosa. Methylation analysis of DNAs from normal tissues with methylation-sensitive restriction enzymes, HpaII and HhaI, revealed that pepsinogen A and C genes are hypomethylated in tissues producing pepsinogens A and C, suggesting a role of DNA methylation in the regulation of the differential expression of the genes for the two human pepsinogens during normal differentiation. In stomach cancer tissues and cancer cell lines, the expressions of the pepsinogen genes were decreased or lost, in good accordance with their pepsinogen productions. No gross structural changes of the pepsinogen genes were observed in these cancers, but the methylation patterns of the pepsinogen genes were found to be altered in different ways in different cancers. The functional significance of the altered methylation is unknown; however, these results suggest that considerable heterogeneity of the methylation patterns occurs in human stomach cancers.
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PMID:Methylation and expression of human pepsinogen genes in normal tissues and their alteration in stomach cancer. 190 54

Gastric and intestinal phenotypic expression in 223 surgically obtained primary gastric cancers and their histogenetic relationship to intestinal metaplasia in the surrounding gastric mucosa were studied by mucin histochemistry and pepsinogen (Pg) immunohistochemistry. Histochemical differentiation of mucins (paradoxical concanavalin A, the galactose oxidase-Schiff sequence and sialidase-galactose oxidase-Schiff) and immunohistochemical staining of Pgs I and II, allowed differentiation of gastric cancer cells from different histological categories into gastric elements including mucous neck cells, pyloric gland cells and surface mucous cells or intestinal elements including goblet cell and intestinal absorptive cell types. Of 122 papillary and tubular adenocarcinomas, 33 (27.1%) consisted mainly of gastric-type cells and 42 (34.4%) predominantly of intestinal-type cells. The remainder (38.5%) consisted of mixtures of gastric- and intestinal-type cells. Of 101 poorly differentiated adenocarcinomas, signet ring cell carcinomas and mucinous adenocarcinomas, 59 (58.4%) consisted mainly of gastric-type cells and 20 (19.8%) mainly of intestinal-type cells. Seven out of 35 papillary and tubular adenocarcinomas consisting mainly of gastric-type cancer cells were surrounded by mucosa with intestinal metaplasia. Conversely, 10 out of 40 papillary and tubular adenocarcinomas consisting mainly of intestinal-type cancer cells were observed in nonmetaplastic gastric mucosa. Thus no relationship as regards intestinal phenotypic expression was found between gastric cancers and surrounding gastric mucosa.
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PMID:Gastric and intestinal phenotypic expression of human stomach cancers as revealed by pepsinogen immunohistochemistry and mucin histochemistry. 222 Mar 96

Serum pepsinogen levels were measured in 137 stomach cancer patients and compared with those of 288 normal cancer-free subjects. The serum pepsinogen levels of stomach cancer patients, especially pepsinogen I and the pepsinogen I/pepsinogen II ratio were significantly lower than those of normal controls and correlated well with the extent of chronic gastritis associated with the cancerous stomach. These results were in good accordance with the results of previous studies indicating that the cancer derived from the stomach where chronic gastritis/intestinal metaplasia is extensive. The high sensitivity and specificity of this non-invasive serum test to detect chronic gastritis suggested the possibility of its application to the mass screening of stomach cancer.
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PMID:The significance of low serum pepsinogen levels to detect stomach cancer associated with extensive chronic gastritis in Japanese subjects. 249 45

This study was carried out to elucidate a role of pepsinogen, one of the proteases that currently introduced as a promotor of tumor invasion, on gastric cancer spread. Production of pepsinogen in cancer tissue was analysed by means of three different methods of acid proteolytic activity (APA), polyacrylamide gel electrophoresis (PAGE), and immunoperoxidase staining (IPS), respectively in the 60 resected advanced gastric cancer specimens. Mean level of APA in cancer tissue was higher than that in the control intact muscle layer of the gastric body (p less than 0.05). Through IPS and PAGE, pepsinogen was detected in 53 and 78% of cancer tissue, respectively. Cancer tissue in the cardia produced higher pepsinogen than that in the pyrolus (p less than 0.05). Cancer tissue of Borrmann IV type illustrated higher level of pepsinogen than those of Borrmann II or III type (p less than 0.05). Furthermore, cancer tissue with advanced serosa invasion or that belonging Stage IV presented relatively higher levels. There was a significant correlation between nodal involvement and pepsinogen level (p less than 0.05). Thus, pepsinogen in the gastric cancer tissue tended to be detected with cancer spread. Pepsinogen produced in cancer tissue could loosen or separate intercellular connection of cancer cells to form isolated signet ring cells.
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PMID:[Studies on pepsinogen production in advanced gastric cancer tissue]. 268 97

We measured serum pepsinogen I (PG I) levels in 137 stomach cancer patients by the previously described radioimmunoassay and compared them with those of normal cancer-free subjects by a gastric mass survey in a certain workplace. The value and limitations of the measurement of serum PG I level in the diagnosis of stomach cancer were analyzed statistically according to the histology and stage of the disease. The mean serum PG I level of stomach cancer patients was 21.3 micrograms/l [early stage (N = 53): 24.9 micrograms/l; advanced stage (N = 84): 19.2 micrograms/l; well-differentiated (N = 62): 19.5 micrograms/l poorly-differentiated (N = 75): 22.7 micrograms/l]. It was significantly lower than that of the age-matched cancer-free subjects. As to the stage and histology of the disease, early stage poorly-differentiated adenocarcinoma and the same stage well-differentiated adenocarcinoma took the mean serum PG I level of 30.6 micrograms/l (N = 26, p less than 0.05) and 20.2 micrograms/l (N = 27, p less than 0.001). In the advanced stage, they were 19.3 micrograms/l (N = 49, p less than 0.001) and 18.6 micrograms/l (N = 35, p less than 0.001), respectively. Using a cut off point of 25 micrograms/l to separate subjects with stomach cancer, sensitivity was 61% and specificity, 80%. These results suggest a possibility of serological screening of the subjects with stomach cancer and indicate that the measurement of serum PG I level will probably contribute much to the improvement of the effectiveness of a gastric mass survey.
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PMID:[Serum pepsinogen I level in patients with stomach cancer--its value and limitation in clinical use]. 273 17

Serum pepsinogen levels were examined by immunoradiometric assay method for evaluating its clinical usefulness in gastric cancer. In patients with gastric cancer, serum PG-I tended to decrease but PG-II stayed normal level, resulting in low PG-I/PG-II ratio. Combination of PG-I and PG-I/PG-II discriminated 53.7% of gastric cancer, 70.6% of scirrhous type gastric cancer, and 66.7-100% of those arisen in the upper portion of the stomach, but 13.7% of normal subjects. As the aged normal subjects tended to show decreased PG-I/PG-II ratio (about 30% of the normal subjects aged over 40 years were discriminated as abnormal), the usefulness for detection of gastric cancer seems to be limited, but some types of gastric cancer such as scirrhous type or one arisen in the upper portion may be discriminated by this method. It is also suggested that this method may detect the recurrence of the cancer in some patients.
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PMID:[Evaluation of serum pepsinogen I and II of patients with gastric cancer]. 281 Sep 10

Slow-moving proteinase (SMP), pepsinogen I (PG I), and pepsinogen II (PG II) are aspartic proteinases normally found in gastric mucosa. Because of differences in their cellular origins, normal gastric epithelial cells can be phenotyped by immunohistochemical staining with a panel of antisera to each proteinase. In this study, we determined aspartic proteinase phenotypes of malignant cells in 74 cases of gastric cancer by immunohistochemical staining with rabbit antiserum to human SMP, PG I, and PG II. Of the 74 cancers, 20 were histologically of the diffuse type and 54 were of the intestinal (or mixed) type. Intestinal metaplasia was characterized by the presence of SMP (but not PG I or PG II) in absorptive epithelial cells. SMP was found in 40 (54%) of the cancers (vs 31% for PG II and only 5% for PG I) and in both the intestinal and diffuse types. Of the 40 SMP-positive cancers, 14 also expressed PG II. In the latter tumors, staining of adjacent sections revealed that some malignant cells expressed only SMP or only PG II, whereas others expressed both proteinases. Overall, 49 (66%) of the cancers contained cells with proteinase phenotypes characteristic of cells in nonmalignant gastric mucosa and 23% contained cells with proteinase phenotypes characteristic of more than one cell type. The results indicate that both intestinal- and diffuse-type gastric cancers often differentiate to cell types that produce aspartic proteinases and that about one fourth contain a heterogeneous population of malignant cells.
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PMID:Slow moving proteinase in gastric cancer and its relationship to pepsinogens I and II. An immunohistochemical study. 305 74

Monoclonal antibodies were used to examine the immunohistochemical expression of pepsinogens I and II in 31 early and 76 advanced gastric cancers. Of the 107 carcinomas studied, 19 contained pepsinogen II and only 3, found exclusively in pepsinogen II-positive cases, contained pepsinogen I. Gastric cancer produces pepsinogen II more frequently than pepsinogen I, and production of the latter is significantly associated with the former. Histologically, there were 54 intestinal-type and 53 diffuse-type cancers. The former produced pepsinogen II more frequently than the latter. In the diffuse type, the four pepsinogen II-positive cases were found exclusively in females. Although the pepsinogen expression was independent of the macroscopic features in advanced gastric cancer, it was found that the protruded-type early gastric cancer produced pepsinogen II more frequently than the depressed type. Incidences of pepsinogen positivity were not different between early and advanced gastric cancers or between cancers with or without lymph node metastasis, suggesting that production of pepsinogen is independent of tumor growth.
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PMID:Pepsinogens I and II in gastric cancer: an immunohistochemical study using monoclonal antibodies. 314 2

Changes have been studied in human and rat pepsinogen phenotypes induced by N'-methyl-N'nitro-N-nitrosoguanidine (MMNG) in in vitro rat experiments and in vivo cultures of human and rat isolated gastric chief cells. In vivo the fastest migrating electrophoretic band decreased or disappeared as early as 3 weeks after the start of MNNG treatment. The changes, observed in 17 of 32 rats receiving MNNG, were permanent and consistently associated with pronounced histopathologic changes seen 10 months later (17 of 17). Comparable phenotypic changes were observed after 7 days only in MNNG-treated rat chief cell cultures. In human chief cell cultures a decrease of the Pg3 band, which is consistent with the "carcinogenic" phenotype, was observed in two of six preparations treated with MNNG. This early preceding change in phenotype preceding tumor formation may be useful as a diagnostic tool for the onset of gastric cancer.
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PMID:Changes in rat and human pepsinogen phenotypes induced by N'-methyl-N'nitro-N-nitrosoguanidine. 316 8

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


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