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Chemical Compound Review

Apstatin     (2S)-N-[(1S)-1- aminocarbonylethyl]-1- [(2S)...

Synonyms: CHEMBL311875, SureCN6667113, CHEBI:225749, AC1L9KOA, DB04092, ...
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Disease relevance of Apstatin


High impact information on Apstatin

  • Activity was potently inhibited by bestatin and apstatin in a slow binding competitive fashion, with K(i)* values of 3 and 44 nm, respectively [5].
  • We have developed an inhibitor of AP-P called apstatin (1) (N-[(2S, 3R)-3-amino-2-hydroxy-4-phenyl-butanoyl]-L-prolyl-L-prolyl-L-al aninam ide); IC50,human = 2.9 microM [6].
  • Transient expression of AP-P cDNA in COS-1 cells resulted in enzymic activity characteristic of AP-P, namely apstatin- and EDTA-sensitive hydrolysis of bradykinin and Gly-Pro-Hyp [7].
  • The low dose of GW796406 administered with apstatin, an APP inhibitor, did not increase plasma extravasation [8].
  • 5. Apstatin reduces IS in an in vivo model of acute myocardial ischaemia and reperfusion to the same extent than ramiprilat [1].

Chemical compound and disease context of Apstatin

  • In an isolated perfused rat heart preparation subjected to global ischemia and reperfusion, both apstatin and ramiprilat (an ACE inhibitor) significantly decreased creatine kinase (CK) and lactate dehydrogenase (LDH) release [3].

Biological context of Apstatin


Associations of Apstatin with other chemical compounds

  • To do this, we measured the wheal response to intradermal injection of bradykinin (0, 1, or 10 nicrog) in the presence or absence of intradermal administration of the specific aminopeptidase P inhibitor apstatin (5 or 10 microg) and oral administration of the ACE inhibitor quinapril (10 mg) in six healthy subjects [10].
  • N-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-prolyl-L-prolyl-L - alaninamide (apstatin) inhibited purified rat lung membrane-bound aminopeptidase P with a Ki value of 2.6 microM (linear mixed-type inhibition, alpha = 5.1, beta = 0) [11].


  1. Apstatin, a selective inhibitor of aminopeptidase P, reduces myocardial infarct size by a kinin-dependent pathway. Wolfrum, S., Richardt, G., Dominiak, P., Katus, H.A., Dendorfer, A. Br. J. Pharmacol. (2001) [Pubmed]
  2. Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin. Graham, S.C., Maher, M.J., Simmons, W.H., Freeman, H.C., Guss, J.M. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  3. Cardioprotective effects of the aminopeptidase P inhibitor apstatin: studies on ischemia/reperfusion injury in the isolated rat heart. Erşahin, C., Euler, D.E., Simmons, W.H. J. Cardiovasc. Pharmacol. (1999) [Pubmed]
  4. Effects of aminopeptidase P inhibition on kinin-mediated vasodepressor responses. Kitamura, S., Carbini, L.A., Simmons, W.H., Scicli, A.G. Am. J. Physiol. (1999) [Pubmed]
  5. Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species. Morty, R.E., Morehead, J. J. Biol. Chem. (2002) [Pubmed]
  6. Apstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme. Maggiora, L.L., Orawski, A.T., Simmons, W.H. J. Med. Chem. (1999) [Pubmed]
  7. Molecular cloning and expression in COS-1 cells of pig kidney aminopeptidase P. Hyde, R.J., Hooper, N.M., Turner, A.J. Biochem. J. (1996) [Pubmed]
  8. Mechanism of vasopeptidase inhibitor-induced plasma extravasation: comparison of omapatrilat and the novel neutral endopeptidase 24.11/angiotensin-converting enzyme inhibitor GW796406. Sulpizio, A.C., Pullen, M.A., Edwards, R.M., Louttit, J.B., West, R., Brooks, D.P. J. Pharmacol. Exp. Ther. (2005) [Pubmed]
  9. Potentiation by aminopeptidase P of blood pressure response to bradykinin. Kitamura, S., Carbini, L.A., Carretero, O.A., Simmons, W.H., Scicli, A.G. Br. J. Pharmacol. (1995) [Pubmed]
  10. Inhibition of aminopeptidase P potentiates wheal response to bradykinin in angiotensin-converting enzyme inhibitor-treated humans. Kim, K.S., Kumar, S., Simmons, W.H., Brown, N.J. J. Pharmacol. Exp. Ther. (2000) [Pubmed]
  11. Effect of a new aminopeptidase P inhibitor, apstatin, on bradykinin degradation in the rat lung. Prechel, M.M., Orawski, A.T., Maggiora, L.L., Simmons, W.H. J. Pharmacol. Exp. Ther. (1995) [Pubmed]
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