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ARG1 — CTSB

Text-mined interactions from Literome

Mizote et al., Dev Biol 1999 : We found that purified sperm protease readily hydrolyzes Boc-Gly-Arg-Arg-MCA and Z-Arg-Arg-MCA, that protease activity was inhibited by the trypsin inhibitors aprotinin and leupeptin, and that not only the purified protease, but also cathepsin B , induces activation in Xenopus eggs
Zhu et al., J Osaka Univ Dent Sch 1992 : The activation of cathepsin B by BK or des-Arg9-BK was inhibited by des-Arg9- [ Leu8 ] -BK or islet activating protein (IAP), and the activation of cathepsin B by L-Arg was inhibited by Leu-Arg ( kyotorphin-receptor antagonist ) or Botulinum C3-enzyme ... These results indicate that phospholipase C and serine/threonine kinases are involved in the activation of cathepsin B by BK, des-Arg9-BK or L-Arg. Genistein inhibited the activation of cathepsin B by des-Arg9-BK or L-Arg in a different fashion, suggesting that tyrosine kinase ( s ) is also involved in the activation ... Cathepsin B activation by BK or L-Arg but not des-Arg9-BK was inhibited by L-NMMA ( inhibitor of NO synthesis ), and the activation by L-Arg was enhanced by beta-glycerophosphate ( beta-GP : inhibitor of phosphatases ), while the activation by BK or des-Arg9-BK was inhibited by beta-GP ... These results suggest that BK-induced cathepsin B activation in the fibroblasts may be due to a combined effect of des-Arg9-BK and L-Arg
Wieczerzak et al., J Pept Sci 2007 : The MD simulation of the Z-Arg-Leu-Arg-Agly approximately cathepsin B complex suggests that, contrary to other potent inhibitors of cathepsin B , the current double Arg(1)/Arg ( 3 ) inhibitor , while maintaining the fold is able to form a unique ion cluster involving both Arg residues on the inhibitor part and two acidic Glu171 and Glu245 on the cathepsin B part, thus enhancing the affinity and subsequently the inhibiting power and selectivity of Z-Arg-Leu-Arg-Agly-Ile-Val-OMe to the observed extreme extent ... The MD simulation of the Z-Arg-Leu-Arg-Agly approximately cathepsin B complex suggests that, contrary to other potent inhibitors of cathepsin B , the current double Arg(1)/Arg ( 3 ) inhibitor , while maintaining the fold is able to form a unique ion cluster involving both Arg residues on the inhibitor part and two acidic Glu171 and Glu245 on the cathepsin B part, thus enhancing the affinity and subsequently the inhibiting power and selectivity of Z-Arg-Leu-Arg-Agly-Ile-Val-OMe to the observed extreme extent
Ichimaru et al., Inflamm Res 1996 (Periodontitis) : More than 95 % of Z-Arg-Arg-MCA hydrolytic activity in each GCF sample was inhibited by CA-074, specific inhibitor of cathepsin B