Disease relevance of BRN 1405664

• A thiol protease inhibitor released from cultured human malignant melanoma cells [1].
• Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus [2].
• The thiol protease inhibitor E-64 specifically blocks autocatalytic activity of the leader protease of foot-and-mouth disease virus (FMDV) and interferes with cleavage of the structural protein precursor in an in vitro translation assay programmed with virion RNA [2].
• Treatment of E. histolytica trophozoites with specific cysteine proteinase inhibitor E-64 blocked or greatly reduced liver abscess formation at 48 h in SCID mice [3].
• In murine muscular dystrophy, hindlimb muscle contains a functionally defective thiol protease inhibitor (TPI) which has been implicated in the onset and progression of the disease in mice [4].

Psychiatry related information on BRN 1405664

• Olfactory discrimination learning is blocked by leupeptin, a thiol protease inhibitor [5].

High impact information on BRN 1405664

• It is inhibited by a thiol protease inhibitor but not by inhibitors of cathepsin B or of serine proteases [6].
• Notably, earlier findings of biological activity as a thiol protease inhibitor have no correspondence in the three-dimensional structure of Tlc, rather it appears that its proteolytic fragments could be responsible for this phenomenon [7].
• EGF-stimulated degradation of both receptor domains was inhibited by the thiol protease inhibitor leupeptin, suggesting lysosome involvement in the hydrolysis of the whole molecule [8].
• The ycp1-induced BLM resistance was completely reversed by the cysteine proteinase inhibitor E-64, a known inhibitor of BLM hydrolase [9].
• The thiol protease inhibitor leupeptin, a known calpain inhibitor, also inhibited calcium-dependent proteolysis in the presence and absence of polyamines [10].

Biological context of BRN 1405664

• Furthermore, a thiol protease inhibitor and specific cathepsin inhibitors impaired CD83 up-regulation in DC, indicating a role of endosomal proteases in the maturation-induced exposure of CD83 on the plasma membrane [11].
• Effect of E-64, a thiol protease inhibitor, on antibody formation in mice [12].
• The thiol protease inhibitor benzyloxycarbonyl-Leu-Val-Gly diazomethylketone neither prevented nor produced apoptosis [13].
• This insulin-induced down-regulation of IRS-1 was totally abolished by BAPTA-AM (cell-permeable calcium chelator), E-64d (cell-permeable thiol protease inhibitor), Cbz-Leu-Nleu-H and Cbz-Leu-Leu-Tyr-CHN2 (selective cell-permeable calpain inhibitor peptides) [14].
• Studies on myosin light chain phosphorylation in intact platelets, utilizing a cell-penetrating thiol protease inhibitor [15].

Anatomical context of BRN 1405664

• (3) The starvation-induced increase of the size of the fraction of easily releasable myofilaments could be significantly reduced by treatment of the starving animals with the proteinase inhibitor E-64 [16].
• Intramuscular injections of the thiol protease inhibitor, leupeptin, abolished Ca-activated neutral protease immunoreactivity in both muscle and peripheral nerve [17].
• A new thiol-protease inhibitor, E-64-c (N-[N-(L-3-carboxyoxirane-2-carbonyl)-L-leucyl]-isoamylamine), specifically suppressed the disappearance of the Z-line terminal by calcium in rat soleus muscle [18].
• Increased level of T-kininogen correlated well with the thiol protease inhibitor activity found in the plasma and exudate [19].
• Using a modified Boyden chamber and an artificial basement membrane, it was found first that cysteine proteinase inhibitor E-64 can abolish the ability of the EJ cells to invade through the artificial basement membrane to the underside of the filter [20].

Associations of BRN 1405664 with other chemical compounds

• Purified dynorphin-converting enzyme has a neutral pH optimum, and is subsantially inhibited by the thiol-protease inhibitor p-chloromercuriphenylsulfonic acid, but not by serine or metalloprotease inhibitors [21].
• Using an isolated working rat heart preparation, the effects of several protease inhibitors (serine protease inhibitors; nafamostat mesilate and gabexate mesilate, a thiol-protease inhibitor; NCO-700; and a urinary trypsin inhibitor, urinastatin) on the postischemic recovery of function and enzyme leakage were investigated in this study [22].
• Unfolding during urea denaturation of a low molecular weight phytocystatin (thiol protease inhibitor) purified from Phaseolus mungo (Urd) [23].
• It involves the uptake and binding of a fluorogenic thiol-protease inhibitor (fluorescein mercuric acetate, FMA) at the intracellular thiol-protease activity sites in protoplasts, leading to fluorescence emission at 523 nm following excitation at 499 nm [24].

Gene context of BRN 1405664

• The activities of Z-Phe-Arg-NMec(ZPA) hydrolase, cathepsin B and cathepsin H and the concentration of endogenous thiol protease inhibitor in fibroblasts from patients with galactosialidosis were found not to be significantly different from those in control fibroblasts [25].
• For this purpose GST was linked via a flexible spacer to the C-terminus of the thiol-protease inhibitor cystatin, whose binding properties for papain were to be studied [26].
• The calcium-induced release of alpha-actinin was not diminished in the muscle with in vivo-injection of a thiol protease inhibitor, E-64-c. Intramuscular concentrations of E-64-c were also measured after pulse labeling with [3H]E-64-c followed by subcellular fractionation [27].
• By employing a cell penetrating thiol protease inhibitor, EST: ethyl(+)-(2S,3S)-3-[(S)-3-methyl-1-(3-methylbutylcarbamoyl)buty lcarbamoyl]- 2-oxiranecarboxylate, the role of calpain, a major thiol protease in platelets, on 20K protein (myosin light chain) phosphorylation was examined in intact human platelets [15].
• The cathepsin B and L substrate Z-Phe-Arg-NMec was similarly degraded by all species, and activity was abolished by the cysteine proteinase inhibitor E-64 [28].

Analytical, diagnostic and therapeutic context of BRN 1405664

• A "long form" salivary thiol protease inhibitor, designated cystatin SA-I, was purified to homogeneity from human submandibular-sublingual saliva by sequential gel filtration and ion-exchange chromatography [29].
• 1. The urinary and plasma metabolites of 14C-loxistatin, a new thiol protease inhibitor, were studied after oral administration to rats [30].
• Four protein fractions containing thiol protease inhibitor activity were obtained by high performance liquid chromatography of Artemia embryo proteins on a C-18 reverse-phase column and these were designated as TPI-1a, -1b, -2, and -3 [31].
• Cytoplasmic accumulations in rat primary brain cell cultures following treatment with E-64, a thiol protease inhibitor [32].
• 2. The titration of the sulphydryl group in the active site of the enzyme with the proteinase inhibitor E-64 yielded one thiol group per molecule [33].

References