Disease relevance of Suc-leu-leu-val-tyr-mca

• Succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide (Suc-LLVY-MCA) hydrolyzing activities of the 20S and 26S proteasomes in the gerbil cortex following transient forebrain ischemia were examined [1].

High impact information on Suc-leu-leu-val-tyr-mca

• IFN-gamma stimulation results in a downregulation of the chymotrypsin-like Suc-LLVY-MCA peptide hydrolyzing activity of 20S proteasomes whereas the trypsin-like activity remains unaffected [2].
• After hydrogen peroxide treatment of K562 cells, degradation of the model proteasome peptide substrate suc-LLVY-MCA and degradation of oxidized histones in nuclei increases significantly within minutes [3].
• In vitro, the 20S proteasome shows an increased proteolytic activity toward oxidized polypeptides and the suc-LLVY-MCA peptide specific for its chymotrypsin-like activity [4].
• Proteasomes eluted in the other peak were partially resolved into three subpeaks and based on their preferential hydrolysis of casein, Z-GGL-MCA, and suc-LLVY-MCA, were designated C, L and Y, respectively [5].
• The three fatty acids all activated the hydrolysis of succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide (Suc-LLVY-MCA) and benzyloxycarbonyl-Leu-Leu-Glu-2-naphthyl-amide (Cbz-LLE-2NA) at low concentrations (one-third to one-sixth of that required for activation by SDS) [6].

Biological context of Suc-leu-leu-val-tyr-mca

• Suc-LLVY-MCA degrading activity of the platelet proteasome showed positive cooperativity between two or more catalytic sites because the coefficient was 1.54 when analyzed by use of the Hill plot [7].

Anatomical context of Suc-leu-leu-val-tyr-mca

• The egg jelly-induced acrosome reaction of the sea urchin, Strongylocentrotus intermedius, was inhibited by succinyl-Leu-Leu-Val-Tyr-4-methyl-coumaryl-7-amide (Suc-Leu-Leu-Val-Tyr-MCA), but not by Suc-Ala-Ala-Pro-Phe-MCA [8].
• To characterize a chymotrypsin-like hydrolytic activity in the cell surface membranes of intact opossum kidney (OK) cells, we partially purified a protease from the membrane fractions of OK cells using Suc-Leu-Leu-Val-Tyr-MCA (Suc, succinyl; MCA, 4-methylcoumaryl-7-amide), a synthetic substrate for chymotrypsin, as the substrate [9].
• The localization of the proteolytic activity was tested by fractionation of the compartments of rat liver mitochondria using the flourogenic peptide suc-Leu-Leu-Val-Tyr-MCA as substrate [10].

Associations of Suc-leu-leu-val-tyr-mca with other chemical compounds

• The range of concentrations of linolenic acid for the activation of Suc-LLVY-MCA hydrolysis was very narrow [6].

Gene context of Suc-leu-leu-val-tyr-mca

• Using Suc-Leu-Leu-Val-Tyr-MCA, a specific substrate for PA protease, M1 was demonstrated to inhibit the amidolytic activity of PA, whereas M1 did not inhibit that of chymotrypsin or trypsin at all [11].
• Thus, while calpain was inhibited by similar concentrations of ZLLal and ZLLLal, the inhibitory potencies of ZLLLal against the ZLLL-MCA- and Suc-LLVY-MCA-degrading activities in proteasome were 1,100 and 140 times stronger than those of ZLLal, respectively [12].

References