cathepsin-g and Glioma

cathepsin-g has been researched along with Glioma* in 2 studies

Other Studies

2 other study(ies) available for cathepsin-g and Glioma

ArticleYear
Hydrogen Peroxide-Induced Oxidative Stress Activates Proteasomal Trypsin-Like Activity in Human U373 Glioma Cells.
    Journal of molecular neuroscience : MN, 2016, Volume: 58, Issue:2

    Degradation of oxidized or oxidatively modified proteins is an essential part of the cellular antioxidant defense system. 4-Hydroxy-2-nonenal, a major reactive aldehyde formed by lipid peroxidation, causes many types of cellular damage. The major proteolytic system for modified protein degradation is the ubiquitin-proteasome pathway. However, our previous studies using U937 human leukemic cells showed that 4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is degraded by cathepsin G. In the present study, U373 human glioma cells were cultured in the presence of hydrogen peroxide (H2O2) to investigate the relationships of proteasome and/or cathepsin G activities and H2O2-induced GAPDH degradation. Treatment of cells with H2O2 for 5 h in culture decreased GAPDH activity as well as its protein concentration in a concentration-dependent manner. Two proteasomal activities (peptidylglutamyl-peptide hydrolase and chymotrypsin-like hydrolase activities) and cathepsin G activity were decreased by H2O2 treatment in a concentration-dependent manner, but proteasomal trypsin-like hydrolase activity increased with cell exposure to high H2O2 concentrations. Among the protease inhibitors examined here, H2O2-induced activation of trypsin-like activity and GAPDH degradation were inhibited by the proteasome inhibitor lactacystin. Furthermore, H2O2-induced activation of trypsin-like activity was also inhibited by another proteasome inhibitor MG-132. These results suggested that proteasomal trypsin-like activity played an important role in eliminating oxidatively modified GAPDH formed in these cells during H2O2 exposure.

    Topics: Cathepsin G; Cell Line, Tumor; Glioma; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); Humans; Hydrogen Peroxide; Neurons; Oxidative Stress; Proteasome Endopeptidase Complex; Proteasome Inhibitors; Proteolysis; Trypsin

2016
Thrombin and PAR-1 activating peptide increase iNOS expression in cytokine-stimulated C6 glioma cells.
    Journal of neurochemistry, 2001, Volume: 79, Issue:3

    Thrombin (THR) plays a key role in the brain under physiological and pathological conditions. Several of the biological activities of thrombin have been shown to be mainly driven through activation of protease-activated receptor-1 (PAR-1)-type thrombin receptor. Here we have studied the effect of THR and PAR-1-activating peptide (PAR1-AP), SFLLRN, on cytokine-induced expression of inducible nitric oxide (iNOS), a prominent marker of astroglial activation using the rat C6 glioma cells. In this cell line, THR (1-10 U/mL) and PAR1-AP (1-100 microM) induced a significant concentration-dependent increase both of IFN-gamma- (250 U/mL) or TNF-alpha- (500 U/mL) induced NO release. The observed increase of NO production was related to an enhancement of iNOS expression as measured in cell lysates prepared from different treatments by using SDS-PAGE followed by western blot analysis. The effect of THR, but not that of PAR1-AP, was significantly inhibited by hirulog(TM) (60 microg/mL), a specific and stochiometric THR inhibitor or by cathepsin-G (40 mU/mL), an inhibitor of PAR-1. In conclusion our data suggest a role for THR through activation of PAR-1 in the induction of astroglial iNOS, and further support the hypothesis that THR may function as an important pathophysiological modulator of the inflammatory response.

    Topics: Animals; Astrocytes; Cathepsin G; Cathepsins; Cell Division; Drug Synergism; Glioma; Hemostatics; Interferon-gamma; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Nitrites; Peptide Fragments; Rats; Serine Endopeptidases; Thrombin; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha

2001