stomach neoplasms/protease

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Expression of Cystatin C in human stomach neoplasms.

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Cystatin C is a member of the cysteine protease inhibitor family and functions to decrease protease production. A recent study showed that it is aberrantly expressed in many malignant tumors in association with tumor invasion and metastasis. Our study aimed to detect Cystatin C expression in stomach

A human monoclonal antibody recognizing a surface antigen on stomach cancer cells.

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Lymph-node lymphocytes of a patient with stomach cancer were fused with the mouse-human heterohybridoma, HM-5. A clone (2F9) was isolated that showed stable production of an IgM antibody reactive with NUGC-4 stomach cancer cell line. This antibody reacted predominantly with a cell surface antigen on

A comprehensive analysis of common genetic variation in MUC1, MUC5AC, MUC6 genes and risk of stomach cancer.

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OBJECTIVE MUC1, MUC5AC, and MUC6 are main constituents of the mucus barrier in the stomach, which protects the underlying epithelium from acid, proteases, mechanical trauma, and pathogenic microorganisms. Accumulating evidence implicates potential roles of MUC1, MUC5AC, and MUC6 genetic variation in

Immunohistochemical analysis of Omi/HtrA2 expression in stomach cancer.

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The serine protease Omi/HtrA2 is released from mitochondria into the cytosol after apoptosis stimuli, inducing apoptosis in a caspase-independent manner through its protease activity and in a caspase-dependent manner by neutralizing the inhibition of inhibitor of apoptosis proteins (IAPs) on

[Demonstration of glycoprotein antigens associated with stomach tumors].

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After precipitation of the glycoproteins from gastric tumor tissues by caprylic acid, immunochemical methods were applied to the research of specific gastric tumor antigens; this precipitation process by caprylic acid was less aggressive than the use of urea or proteases. The purification of a

Activation of ASC induces apoptosis or necrosis, depending on the cell type, and causes tumor eradication.

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The adaptor protein ASC (also called TMS1) links certain NLR proteins (e.g., NLRC4, NLRP3) and caspases. It is involved in the chemosensitivity of tumor cells and inflammation. Here, we found that ASC activation using NLRC4 mimicry or an autoinflammatory disease-associated NLRP3 mutant induced

Hepatocyte growth factor activator inhibitor type 2 lacking the first Kunitz-type serine proteinase inhibitor domain is a predominant product in mouse but not in human.

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Hepatocyte growth factor activator inhibitor type 2 (HAI-2) is a new Kunitz-type serine protease inhibitor, which is purified and cloned from human stomach cancer cell line MKN45. The mature HAI-2 protein contains two Kunitz domains and the first domain is mainly responsible for the inhibitory

Upregulation of HGF activator inhibitor type 1 but not type 2 along with regeneration of intestinal mucosa.

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Hepatocyte growth factor (HGF) activator inhibitor type 1 (HAI-1) and type 2 (HAI-2) are new Kunitz-type serine protease inhibitors that were recently purified and cloned from the human stomach cancer cell line MKN45 as specific inhibitors against HGF activator. Both proteins contain two Kunitz

[Evalution of activity of acid aspartic proteinase in Candida strains isolated from oral cavity of patients with increased risk of mycosis].

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We have evaluated the activity of acid aspartic protease in 195 strains of Candida isolated from the oral cavity of three groups of patients. The first group comprised patients with cancer of the larynx qualified for surgery, the second- patients with neoplastic disease ( Hodgkin s disease,

Genomic structure and chromosomal localization of the human hepatocyte growth factor activator inhibitor type 1 and 2 genes.

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Hepatocyte growth factor activator inhibitor type 1 (HAI-1) and type 2 (HAI-2) are recently discovered Kunitz-type serine protease inhibitors which can be purified and cloned from human stomach cancer cell line MKN45 as specific inhibitors against hepatocyte growth factor activator (HGFA). HAI-2 was

Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis.

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Matriptase/MT-SP1, a type II membrane serine protease widely expressed in normal epithelial cells and human carcinoma cells, is thought to be involved in cancer progression. To clarify this possibility, we overexpressed exogenous matriptase in the human stomach cancer cell line AZ521. In vitro, the

Loss of caspase-1 gene expression in human gastric carcinomas and cell lines.

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The caspases are a family of aspartic acid-specific proteases that fulfill varied and often critical roles in mammalian apoptosis or in the proteolytic activation of cytokines. Caspase-1 (interleukin-1beta-converting enzyme) is a member of the cysteine protease family, which cleaves target proteins

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