The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

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

Synonyms: CCRIS 3604, CHEBI:468978, LS-87930, Leupeptin (LEU), EINECS 259-242-2, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

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


  1. Leupeptin, a protease inhibitor, decreases protein degradation in normal and diseased muscles. Libby, P., Goldberg, A.L. Science (1978) [Pubmed]
  2. Effect of leupeptin, a protease inhibitor, on induction of bladder tumors in rats by n-butyl-n-(4-hydroxybutyl)nitrosamine. Kakizoe, T., Takayasu, H., Kawachi, T., Sugimura, T., Takeuchi, T. J. Natl. Cancer Inst. (1976) [Pubmed]
  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]
  4. Inhibition of experimental blood-borne lung metastasis by protease inhibitors. Saito, D., Sawamura, M., Umezawa, K., Kanai, Y., Furihata, C., Matsushima, T., Sugimura, T. Cancer Res. (1980) [Pubmed]
  5. Protease inhibitor coinfusion with amyloid beta-protein results in enhanced deposition and toxicity in rat brain. Frautschy, S.A., Horn, D.L., Sigel, J.J., Harris-White, M.E., Mendoza, J.J., Yang, F., Saido, T.C., Cole, G.M. J. Neurosci. (1998) [Pubmed]
  6. Inhibitors of Ca(2+)-dependent endopeptidases modulate morphine-induced effects in rats. Lyupina, Y.V., Sudakov, S.K., Yarygin, V.N. Eur. J. Pharmacol. (1996) [Pubmed]
  7. Purification of a trypsin-type protease from human umbilical vein endothelial cells which is highly sensitive to the Kunitz inhibitor domain peptide of Alzheimer's disease amyloid protein precursor. Kido, H., Takeda, M., Wakabayashi, H., Tanaka, S., Nishimura, N., Takenaka, M., Okada, M. Gerontology. (1993) [Pubmed]
  8. HDL3-signalling in HepG2 cells involves glycosyl-phosphatidylinositol-anchored proteins. Nazih-Sanderson, F., Pinchon, G., Nion, S., Fruchart, J.C., Delbart, C. Biochim. Biophys. Acta (1997) [Pubmed]
  9. Pharmacological dissociation of memory: anisomycin, a protein synthesis inhibitor, and leupeptin, a protease inhibitor, block different learning tasks. Stäubli, U., Faraday, R., Lynch, G. Behavioral and neural biology. (1985) [Pubmed]
  10. Proteolytic processing activates a viral superantigen. Mix, D., Winslow, G.M. J. Exp. Med. (1996) [Pubmed]
  11. Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles. Amigorena, S., Webster, P., Drake, J., Newcomb, J., Cresswell, P., Mellman, I. J. Exp. Med. (1995) [Pubmed]
  12. Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases. Walz, A., Baggiolini, M. J. Exp. Med. (1990) [Pubmed]
  13. Time-dependent changes in protein kinase C distribution and disappearance in phorbol ester-treated human osteosarcoma cells. Krug, E., Tashjian, A.H. Cancer Res. (1987) [Pubmed]
  14. Effects of the protease inhibitor leupeptin on proteolytic activities and regeneration of mouse skeletal muscles after exercise injuries. Salminen, A. Am. J. Pathol. (1984) [Pubmed]
  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]
  16. Role of cellular proteinases in acute myocardial infarction. I. Proteolysis in nonischemic and ischemic rat myocardium and the effects of antipain, leupeptin, pepstatin and chymostatin administered in vivo. Bolli, R., Cannon, R.O., Speir, E., Goldstein, R.E., Epstein, S.E. J. Am. Coll. Cardiol. (1983) [Pubmed]
  17. Effects of heparin on osteoclast activity. Chowdhury, M.H., Hamada, C., Dempster, D.W. J. Bone Miner. Res. (1992) [Pubmed]
  18. Mast cell tryptase stimulates the synthesis of type I collagen in human lung fibroblasts. Cairns, J.A., Walls, A.F. J. Clin. Invest. (1997) [Pubmed]
  19. Intestinal epithelial cells use two distinct pathways for HLA class II antigen processing. Hershberg, R.M., Framson, P.E., Cho, D.H., Lee, L.Y., Kovats, S., Beitz, J., Blum, J.S., Nepom, G.T. J. Clin. Invest. (1997) [Pubmed]
  20. Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes. Kopitz, J., Kisen, G.O., Gordon, P.B., Bohley, P., Seglen, P.O. J. Cell Biol. (1990) [Pubmed]
  21. Transcriptional and post-transcriptional regulation of tyrosine hydroxylase gene by protein kinase C. Vyas, S., Faucon Biguet, N., Mallet, J. EMBO J. (1990) [Pubmed]
  22. Inhibition of fusion of embryonic muscle cells in culture by tunicamycin is prevented by leupeptin. Olden, K., Law, J., Hunter, V.A., Romain, R., Parent, J.B. J. Cell Biol. (1981) [Pubmed]
  23. Inhibition of autophagic-lysosomal delivery and autophagic lactolysis by asparagine. Høyvik, H., Gordon, P.B., Berg, T.O., Strømhaug, P.E., Seglen, P.O. J. Cell Biol. (1991) [Pubmed]
  24. Ii chain controls the transport of major histocompatibility complex class II molecules to and from lysosomes. Brachet, V., Raposo, G., Amigorena, S., Mellman, I. J. Cell Biol. (1997) [Pubmed]
  25. Receptor-mediated endocytosis of epidermal growth factor by rat hepatocytes: receptor pathway. Dunn, W.A., Connolly, T.P., Hubbard, A.L. J. Cell Biol. (1986) [Pubmed]
  26. Cytochrome P-450 and NADPH-cytochrome P-450 reductase are degraded in the autolysosomes in rat liver. Masaki, R., Yamamoto, A., Tashiro, Y. J. Cell Biol. (1987) [Pubmed]
  27. Exposure of K562 cells to anti-receptor monoclonal antibody OKT9 results in rapid redistribution and enhanced degradation of the transferrin receptor. Weissman, A.M., Klausner, R.D., Rao, K., Harford, J.B. J. Cell Biol. (1986) [Pubmed]
  28. Further studies on the effect of leupeptin, a protease inhibitor, on induction of bladder tumors in rats by N-butyl-N-(4-hydroxybutyl)nitrosamine. Kakizoe, T., Esumi, H., Kawachi, T., Sugimura, T., Takeuchi, T., Umezawa, H. J. Natl. Cancer Inst. (1977) [Pubmed]
  29. Proteinase activities of Entamoeba histolytica cytotoxin. Lushbaugh, W.B., Hofbauer, A.F., Pittman, F.E. Gastroenterology (1984) [Pubmed]
  30. Adhesion of cells to polystyrene surfaces. Curtis, A.S., Forrester, J.V., McInnes, C., Lawrie, F. J. Cell Biol. (1983) [Pubmed]
  31. Estrogen-induced membrane alterations and growth associated with proteinase activity in endometrial cells. Pietras, R.J., Szego, C.M. J. Cell Biol. (1979) [Pubmed]
  32. Calpain-2 as a target for limiting prostate cancer invasion. Mamoune, A., Luo, J.H., Lauffenburger, D.A., Wells, A. Cancer Res. (2003) [Pubmed]
  33. Saposin C is required for normal resistance of acid beta-glucosidase to proteolytic degradation. Sun, Y., Qi, X., Grabowski, G.A. J. Biol. Chem. (2003) [Pubmed]
  34. Human airway trypsin-like protease increases mucin gene expression in airway epithelial cells. Chokki, M., Yamamura, S., Eguchi, H., Masegi, T., Horiuchi, H., Tanabe, H., Kamimura, T., Yasuoka, S. Am. J. Respir. Cell Mol. Biol. (2004) [Pubmed]
  35. Clinical and laboratory studies of a new immunoradiometric assay of parathyroid hormone-related protein. Fraser, W.D., Robinson, J., Lawton, R., Durham, B., Gallacher, S.J., Boyle, I.T., Beastall, G.H., Logue, F.C. Clin. Chem. (1993) [Pubmed]
  36. Differential DNA synthesis in response to activation of protease-activated receptors on cultured guinea-pig tracheal smooth muscle cells. Corteling, R., Bonneau, O., Ferretti, S., Ferretti, M., Trifilieff, A. Naunyn Schmiedebergs Arch. Pharmacol. (2003) [Pubmed]
  37. Successful treatment of murine muscular dystrophy with the proteinase inhibitor leupeptin. Sher, J.H., Stracher, A., Shafiq, S.A., Hardy-Stashin, J. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  38. The CD8+ cell noncytotoxic anti-HIV response can be blocked by protease inhibitors. Mackewicz, C.E., Craik, C.S., Levy, J.A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  39. Antipain and leupeptin restrict uterine DNA synthesis and function in mice. Katz, J., Troll, W., Adler, S.W., Levitz, M. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
WikiGenes - Universities