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)

Changes of prekallikrein in the cases with DIC were investigated, i.e., DIC cases including disseminated metastasis of gastric cancer, acute promyelocytic leukemia and endotoxin shock. Therefore, the trigger substances for this paper were the pathologic cells of the leukemia, the cultured well differentiated adenocarcinoma cells and endotoxin. (1) The lysates of the pathologic cells of the leukemia and the cultured cells showed prekallikrein activation. Endotoxin showed prekallikrein activation via factor XII. (2) Serine proteases (factor Xa, thrombin, plasmin and trypsin) activated prekallikrein in the plasma and the purified prekallikrein. (3) Antithrombin III, aprotinin and FOY inhibited prekallikrein activation. Antithrombin III was promoted by heparin in its inhibitory effect.
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PMID:Changes of prekallikrein in the cases with disseminated intravascular coagulation syndrome. 16 Jan 91

The duodenogastric reflux (DGR) is a suspected cause in some esogastric pathologies in adults: esophagitis, peptic gastric ulcers, stress ulcers, ulcers secondary to drugs, gastric cancer, and gastritis. The toxic substances of the reflux are essentially bile acids, lysolecithin, and trypsin. A number of diagnostic methods have been proposed in the adult. This study suggests a diagnosis technique for DGR in the child. Fasting gastric juice was collected by gastric intubation during 1 h and three substances were measured: phospholipids as markers of biliary reflux, trypsin as a marker of pancreatic reflux, and sialic acid as a marker of the degradation of gastric mucus. The sialic acid enabled us to evaluate some of the toxicity of DGR on the stomach. The study of 49 child subjects permitted us to show the existence, in the normal child, of biliopancreatic markers in the stomach under fasting conditions through a physiological DGR; to define the norms in the child, varying according to three age groups: 0-2 months, 2-12 months, and 1-4 years (the maximum values for an age above 4 years seemed to correspond to those in the adult); and to suggest the existence of a pathological DGR in children with antral gastritis or ulcers.
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PMID:Duodenogastric reflux in children: measurement of phospholipids and trypsin in gastric content. 218 18

The relative amounts of influenza C virus-specific receptors of 25 established lines of mammalian cells including four lines of human malignant melanoma origin were compared by virus binding experiments. All the human melanoma cell cultures studied possessed two to four times more receptors than were found on MDCK cells, a cell line known to be highly susceptible to influenza C virus. It may therefore be a feature common to human melanoma cells that O-acetylsialic acid, a determinant for the attachment of influenza C virus, exists in large quantities on their surface. This is not specific to melanoma cells, however, since several human cell lines derived from lung cancer, gastric cancer, and placenta specimens also exhibited high levels of virus binding. Twenty of 25 virus-binding cell cultures were further examined for their ability to support the replication of influenza C virus. In the presence of trypsin (5 to 20 micrograms/ml), the virus was found to undergo multiple cycles of replication much more efficiently in the HMV-II line of human melanoma cells than in MDCK cells. Additionally, by using HMV-II cells as a host, we succeeded in isolating two influenza C strains (C/Yamagata/1/88, C/Yamagata/2/88) from 241 throat swabs collected from patients with acute respiratory illness.
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PMID:A human melanoma cell line highly susceptible to influenza C virus. 273 78

To examine whether a monoclonal antibody, TFS-4, can distinguish small-cell lung cancer from non-small-cell lung cancers, an extensive survey of fresh lung tumors, cancers from other organs, and normal tissue specimens has been carried out. The antibody has been shown to react specifically with small-cell lung cancer (15 of 15) but not with squamous cell carcinoma (0 of 20), adenocarcinoma (0 of 20) of the lung, or large-cell lung cancer (0 of 2). It reacted neither with other malignancies, including colorectal cancer, gastric cancer, and malignant lymphoma, nor with such normal tissues as trachea, lung, liver, pancreas, colon, kidney, spleen, skin, striated muscle, bone marrow, or peripheral blood cells. Interestingly, the antibody cross-reacted with central nervous tissues. The antigenic determinant on small-cell lung cancer and that on human brain were both heat labile and trypsin sensitive, but resisted treatment with neuraminidase, suggesting that they represent similar peptides. TFS-4 may be of clinical use in the diagnosis of small-cell lung cancer, while the antigen may help investigate the nature and origin of small-cell lung cancer.
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PMID:Monoclonal antibody that distinguishes small-cell lung cancer from non-small-cell lung cancer. 302 18

A monoclonal antibody, MH-A6, was produced by immunization with a human gastric cancer cell line, MKN 74, treated with neuraminidase. The antigen defined by the monoclonal antibody was detected on various tumor tissues and a limited number of normal tissues in immunoperoxidase assay, and the expression of MH-A6 antigen was not influenced by neuraminidase treatment except for some cases of tumor tissues. Interestingly, neuraminidase treatment enhanced binding of the antibody on some adenocarcinomas, but diminished binding of the antibody on squamous cell carcinomas. Both treatment of the immunizing tissues with trypsin and periodic acid diminished binding of the antibody. In isolation of MH-A6 antigen from MKN 74 cells by the monoclonal antibody coupled-affinity column, the epitope exists on molecules with molecular weights of 30,000 and 72,000, and with an acidic pH range in two-dimensional electrophoresis. CEA and CA 19-9 activities were not detected in purified MH-A6 antigen by solid-phase radioimmunoassay, and the reactivity of the MH-A6 antibody with CEA and CA 19-9 was not detected in enzyme-linked immunosorbent assay. Hemagglutination observed between erythrocytes (Lewisa, Lewisb, or NE-treated) and anti-Lewisa, anti-Lewisb sera, or anti-T-agglutinin (peanut lectin), respectively, was not inhibited by MH-A6 antigen. The results suggest that MH-A6 antigen is a tumor-associated antigen, probably glycoprotein, and different from CEA, CA 19-9, Lewisa, Lewisb, and Thomsen-Friedreich (T) antigen.
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PMID:Tumor-associated antigen defined by a monoclonal antibody against neuraminidase-treated human cancer cells. 342 53

Selective drainage method of remnant pancreatic stump (RPS) using latex rubber was devised, and I have obtained a good clinical result for the prevention of postoperative bleeding due to the leakage of pancreatic juice after distal pancreatectomy. In this study, amylase (Am:IU/L) and trypsin (Tr:ng/ml) values in exudate were measured to clarify the actual leakage of pancreatic juice. Thirty-three patients with gastric cancer who underwent total gastrectomy with distal pancreatectomy were chosen for this study; 21 cases of selective drainage (group A) and 12 cases of non-selective drainage (group B). The results are noted below. 1) Both Am and Tr values of group A in the exudate from remnant pancreatic stump were statistically higher than those of group B (p < 0.01). Mean values of group A and group B on the first post-operative day were 25.6 x 10(4) versus 2.6 x 10(4)IU/L (Am value) and 324.4 x 10(4) versus 12.2 x 10(4)ng/ml (Tr value), respectively. 2) The mean values rapidly decreased and bottomed on the sixth postoperative day. 3) Not only total drainage amount of Am (sigma Am: sum of Am value x exudate volume from each drain) but also sigma Tr in group B were markedly less than in group A (p < 0.01). It means that more than 40% of pancreatic juice remained in the abdomen without drainage in group B. In conclusion, effective and active drainage of remnant pancreatic stump for the initial three days at least is important to prevent complications and our selective drainage is one of the excellent methods.
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PMID:[Studies on leakage of pancreatic juice following distal pancreatectomy from the standpoint of transition of amylase and trypsin values in exudate]. 751 16

It has been shown that some types of tumour cells produce activated transforming growth factor beta-1 (TGF-beta 1). However, the mechanism for the activation of TGF-beta 1 derived from tumour cells has not been fully elucidated. The present study was undertaken to characterise an activator of latent TGF-beta 1 secreted from a human gastric cancer cell line, KATO-III. Western blot analyses using antibodies for TGF-beta 1, latency associated peptide (LAP) and latent TGF-beta 1-binding protein (LTBP) revealed that, in the cell lysate of KATO-III, TGF-beta 1 protein was expressed as a small latent complex of TGF-beta 1 and LAP. This was also confirmed by a gel chromatographic analysis of the cell lysate obtained from KATO-III. A 2.5 kb transcript of TGF-beta 1 mRNA was detected in KATO-III cells by Northern blot analysis. A gel chromatographic analysis of the conditioned medium from KATO-III cells revealed, in addition to the active form of TGF-beta 1, a factor which activated latent TGF-beta 1 from NRK-49F cells at fractions near a molecular size of 65,000. This factor was inactivated by heat (100 degrees C), acidification, trypsin and serine protease inhibitors. TGF-beta 1 activity in KATO-III cell lysate was not detected in the untreated state, but potent TGF-beta 1 activity was detected after acid treatment. These results suggest that KATO-III releases not only a latent TGF-beta 1 complex but also a type of serine protease, different from plasmin, plasminogen activator, cathepsin D, endoglycosidase F or sialidase, which activates the latent TGF-beta 1 complex as effectively as acid treatment.
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PMID:Identification of a transforming growth factor beta-1 activator derived from a human gastric cancer cell line. 766 80

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

Twelve human monoclonal antibodies (HuMAb) were established by the fusion of (mouse x human) heteromyeloma cells with B-lymphoblastoid cells derived from the regional lymph nodes of three patients with squamous cell carcinoma of the lung. They were tested for reactivity to two kinds of proteins (purified protein derivatives and bovine serum albumin) by ELISA, Sq-19 (squamous cell carcinoma) culture cells by indirect membrane immunofluorescence tests, and Sq-19 tumor xenograft by immunohistological study. Among them, one HuMAb 904F (IgM, lambda) was selected. In indirect membrane immunofluorescence tests, this 904F antibody reacted with various kinds of cell lines, e.g. lung cancer, esophageal cancer, endometrial cancer, and stomach cancer. It did not react with malignant hematopoietic and diploid fibroblast cell lines. Immunohistologically, it stained the tumor nests of squamous cell carcinoma, adenocarcinoma, and large cell carcinoma of the lung. It also stained those of esophagus and colon, but not those of small cell carcinoma of lung, or stomach. On frozen-section specimens of normal tissues from various organs, it showed only limited areas of positive staining. Limited positive findings were observed at a reticular zone of the adrenal gland, at the esophagus as weak staining, and at islets of the pancreas as very weak staining. Western blotting analysis demonstrated that it recognized a 54 kDa trypsin-sensitive molecule which is expressed on the surface of tumor cells. These results suggest the 904F monoclonal antibody detects a novel tumor-associated antigen which is recognized by the human immune system.
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PMID:A novel human monoclonal antibody directed to a tumor-associated antigen. 839 67

alpha 2-macroglobulin-trypsin complexlike substance (MTLS) was determined in plasma of pancreatic and nonpancreatic diseases using a two-step enzyme immunoassay to study the diagnostic and pathophysiological significance of MTLS. Plasma levels of MTLS in acute pancreatitis (mean +/- SD = 265.6 +/- 346.2 ng/ ml, n = 9), calcified chronic pancreatitis (128.6 +/- 257.4, n = 13), and noncalcified chronic pancreatitis (13.5 +/- 12.5, n = 10) were significantly higher than that in controls (3.6 +/- 1.8, n = 81). In other diseases such as gastric cancer, hepatoma, diabetes mellitus, and gallstones, MTLS values were not different from those of control. Plasma MTLS values showed low correlation with serum trypsin, elastase 1, pancreatic amylase, lipase, and pancreatic secretory trypsin inhibitor (PSTI). The elevation of plasma MTLS values in acute pancreatitis suggests that plasma MTLS levels reflect that protease is inappropriately activated in pancreatic acinar cell and released into the circulation and that the determination of MTLS can be useful for diagnosis and pathophysiology of acute pancreatitis and chronic pancreatitis.
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PMID:Plasma alpha 2-macroglobulin-trypsin complexlike substance (MTLS) in pancreatic disease. 895 9


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