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Chemical Compound Review

AC1MHWLS     (2S)-N-[(2S)-2-acetamido-4- methyl...

Synonyms: CCRIS 3604, CHEBI:468978, LS-87930, Leupeptin (LEU), EINECS 259-242-2, ...
 
 
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Disease relevance of N-Acetyl-L-leucyl-L-leucyl-L-argininal

  • Leupeptin also lowers protein breakdown in denervated rat muscles and affected muscles from mice with hereditary muscular dystrophy [1].
  • Leupeptin, isolated from Actinomycetes, is a potent and specific inhibitor of proteases [2].
  • Three of these compounds, leupeptin, pentamidine, and bis (5-amidino-2-benzimidazolyl) methane (BABIM) also restricted the intestinal replication of the murine strain of rotavirus when protease inhibitor and virus were administered simultaneously to suckling mice [3].
  • Leupeptin (50 mg/kg body weight twice a day) reduced the number of thrombi from 1298 +/- 395 to 646 +/- 218, when injected i.p. for 2 days before the inoculation of the cells (p less than 0.005) [4].
  • Analysis of gliosis and TUNEL in neuron layers of the frontal and entorhinal cortex suggested that leupeptin exacerbated Abeta40 toxicity [5].
 

Psychiatry related information on N-Acetyl-L-leucyl-L-leucyl-L-argininal

 

High impact information on N-Acetyl-L-leucyl-L-leucyl-L-argininal

  • Since homogenates of leupeptin-treated muscles had decreased cathepsin B activity, this lysosomal protease may play a role in protein turnover in normal and diseased muscles [1].
  • The protease inhibitor leupeptin decreases protein degradation in rat skeletal and cardiac muscle incubated in vitro, while protein synthesis remains unaltered [1].
  • The marginal presentation of vSAg7 observed using the furin-negative transfectants was eliminated after culture with the protease inhibitor leupeptin, suggesting that one or more endoproteases other than furin have a detectable but limited capacity to proteolytically activate vSAg7 [10].
  • As expected, leupeptin caused an accumulation of Ii chain and class II molecules (I-A(d)) in endosomes and lysosomes [11].
  • The monocyte-conditioned medium was found to cleave purified CTAP-III into NAP-2 through proteinases that were highly sensitive to PMSF, moderately sensitive to leupeptin and insensitive to EDTA [12].
 

Chemical compound and disease context of N-Acetyl-L-leucyl-L-leucyl-L-argininal

 

Biological context of N-Acetyl-L-leucyl-L-leucyl-L-argininal

 

Anatomical context of N-Acetyl-L-leucyl-L-leucyl-L-argininal

  • In addition, the sequestration step was measured separately as the transfer from cytosol to sedimentable cell structures of electroinjected [3H]raffinose or endogenous lactate dehydrogenase (LDH; in the presence of leupeptin to inhibit lysosomal proteolysis) [23].
  • Upon removal of leupeptin, Ii-p10 was degraded and released, I-A(b) dimers bound antigenic peptides, and the peptide-loaded dimers were transported slowly from lysosomes to the plasma membrane [24].
  • This EGF-induced loss of receptors was not observed when lysosomal proteinases were inhibited by leupeptin or when endosome/lysosome fusion was prevented by low temperature (16 degrees C) [25].
  • Autolysosomes, almost completely free from contamination by the other organelles such as ER, were prepared from leupeptin-treated rat livers according to the method of Furuno et al [26].
  • Radiolabeled OKT9 is itself degraded by K562 cells and this degradation is inhibitable by leupeptin or chloroquine [27].
 

Associations of N-Acetyl-L-leucyl-L-leucyl-L-argininal with other chemical compounds

 

Gene context of N-Acetyl-L-leucyl-L-leucyl-L-argininal

 

Analytical, diagnostic and therapeutic context of N-Acetyl-L-leucyl-L-leucyl-L-argininal

References

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  3. Protease inhibitors suppress the in vitro and in vivo replication of rotavirus. Vonderfecht, S.L., Miskuff, R.L., Wee, S.B., Sato, S., Tidwell, R.R., Geratz, J.D., Yolken, R.H. J. Clin. Invest. (1988) [Pubmed]
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  15. Activation of human Glu-plasminogen to Glu-plasmin by urokinase in presence of plasmin inhibitors. Streptomyces leupeptin and human plasma alpha1-antitrypsin and antithrombin III (plus heparin). Summaria, L., Boreisha, I.G., Arzadon, L., Robbins, K.C. J. Biol. Chem. (1977) [Pubmed]
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