Disease relevance of Ctrl

• Rats were injected with adenoviruses expressing control transgenes (Ctrl), latent TGF-beta(1) [TGF-beta(L)], or activated TGF-beta(1) [TGF-beta(A)] [1].
• Two additional groups with (Prob NR, n = 6) and without (Ctrl NR, n = 6) probucol pretreatment were arrested and subjected to 2 hours of ischemia without reperfusion [2].
• Liver nitrites, number of granulocytes, liver weight/body weight ratio, cytochrome P450 2E1 protein, and chymotrypsin-like activity changed in the same direction compared with control values [3].
• In addition, only the levels of elastase and chymotrypsin-like activity were found to be consistently higher in highly metastatic prostatic cancers than in either the normal prostate or low-metastatic prostatic cancers [4].
• The substrate specificity studies suggest a possible evolutionary relationship between the catalytic component of the ClpP of Escherichia coli and the multicatalytic proteinase chymotrypsin-like catalytic component [5].

High impact information on Ctrl

• Tonin, an esteroprotease isolated from rat submaxillary gland, is a serine protease with trypsin- and chymotrypsin-like activity [6].
• Induction of a novel Ca2+-dependent chymotrypsin-like serine protease by tumor promoters in rat livers [7].
• In summary, these results show that chymotrypsin substrate analogues efficiently inhibit the internalization of insulin and insulin receptors in adipocytes and implicate a possible role for endogenous chymotrypsin-like enzyme(s) or related substances in receptor-mediated endocytosis of insulin [8].
• Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells [9].
• The substrate specificity of rat mast cell protease I (RMCP I), a chymotrypsin-like serine protease localized in the secretory granules of mast cells, was compared to that of bovine alpha-chymotrypsin by using several peptide and protein substrates of known amino acid sequences [9].

Chemical compound and disease context of Ctrl

• We have previously shown that ritonavir, an HIV-1 protease inhibitor used in AIDS therapy, can modulate the proteasome function by inhibiting the chymotrypsin-like activity and enhancing the trypsin-like activity [10].

Biological context of Ctrl

• Increased hepatocyte apoptosis was observed in TGF-beta(A)-injected but not TGF-beta(L)-injected animals 24 h postinjection (10.5%) compared with Ctrl animals (0.37%) [1].
• Ala-Ala-Phe-chloromethyl (CH2Cl) inhibits chymotrypsin-like activity assayed with succinyl (Suc) -Leu-Leu-Val-Tyr-AMC, but surprisingly not hydrolysis of Ala-Ala-Phe-7-amido4-methylcoumarin (AMC) [11].
• Interestingly, a proteinase and a trypsin-like and a chymotrypsin-like peptidase activity could not be separated by customary chromatographic methods but were distinguishable by their sensitivities to various inhibitors, activators, and covalent modifiers, suggesting that the enzyme has three distinct active sites within a single protein [12].
• The irreversible chymotrypsin-like protease inhibitor TPCK (tosyl-L-phenylalanyl chloromethyl ketone) inhibited membrane potential changes in rat neutrophils in response to phorbol myristate acetate, N-formylmethionylleucylphenylalanine and the calcium ionophore A23187 in a time- and dose-dependent manner [13].
• These activities have often been referred to as 'chymotrypsin-like', 'trypsin-like' and 'peptidylglutamyl-peptide hydrolase' activities according to the type of residue in the P1 position, although it is now clear that mammalian proteasomes have at least five distinct catalytic sites [14].

Anatomical context of Ctrl

• Four hours after PH, 0.25 and 14.1% apoptotic hepatocytes were seen in Ctrl- and TGF-beta(A)-injected rats, respectively [1].
• All atypical mast cells also contained low levels of the chymotrypsin-like protease of normal mast cells [15].
• Tumor cell membranes solubilized in Triton X-100 had activity in the p-toluenesulfonyl-L-arginine methyl ester assay for trypsin-like enzymes and the N-benzoyl-L-tyrosine ethyl ester assay for chymotrypsin-like enzymes [16].
• Rat peritoneal macrophages contain a chymotrypsin-like protease and its specific inhibitor, both being associated with chromatin of the cells [17].
• In the present study, we cultured rat metatarsal bones in the presence of proteasome inhibitor I (PSI), a known inhibitor of the chymotrypsin-like activity of the 20S proteasome [18].

Associations of Ctrl with chemical compounds

• Much smaller increases were seen in the A1254/Ctrl group [19].
• Eighteen donor hearts were divided into 3 groups of 6 and arrested either 1 hour after intraperitoneal injection of 3 ml oil with (Prob Tx) or without (Oil Tx) probucol (300 mg/kg) or without injection (Ctrl Tx) [2].
• Circulating thyroxine (T(4)) concentrations were sharply reduced at GD 21 in the A1254-exposed group, and on PND 3, 7, 14, and 21 in the A1254/A1254 and the Ctrl/A1254 groups [19].
• To study this, isolated rat hearts were subjected to ischemia-reperfusion (I/R) (20 min/40 min), without (control = Ctrl) or with receptor-dependent [phenylephrine (PE), 50 microM; adenosine (ADO), 125 microM] or -independent [phorbol myristate acetate (PMA), 100 nM] activation of PKC [20].
• Additionally, FI rats had significantly greater predicted trough gentamicin levels than Ctrl or FD rats [21].

Other interactions of Ctrl

• The proteolytic cleavage process for the conversion of membrane-associated ICAM-1 to sICAM-1 was sensitive to Batimastat (BB94) and phosphoramidon, two inhibitors of metalloproteases, whereas inhibitors of serine-, cysteine-, aspartic-, and chymotrypsin-like proteases had no effect on this process [22].
• The dual trypsin- and chymotrypsin-like enzymatic specificity of rK9 was assessed by determining specificity constants (k(cat)/K(m)) for the hydrolysis of fluorogenic substrates, the peptide sequences of which were derived from proparathyroid hormone (pro-PTH) and from semenogelin-I [23].
• Rat mast cell protease 1 (RMCP-1), a chymotrypsin-like serine protease expressed specifically by connective tissue-type mast cells, is recovered in a macromolecular complex with heparin proteoglycan [24].
• The serine proteases belong to either the chymase (chymotrypsin-like substrate specificity) or tryptase (trypsin-like specificity) family [25].
• Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G [26].

Analytical, diagnostic and therapeutic context of Ctrl

• Additional studies of substrate specificity involving gas-phase sequence analyses of digested natural substrates revealed an inherent but low chymotrypsin-like activity of trypsin [27].
• Using site directed mutagenesis, cysteines of this disulfide bridge were replaced by alanines in trypsin, in chymotrypsin, and in Tr-->Ch-[S1+L1+L2+Y172W], a mutant trypsin with high chymotrypsin like activity [28].
• Following p-aminobenzamidine- and D-phenylalanine-agarose affinity chromatography both trypsin- and chymotrypsin-like protease activities were found [29].

References