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XPNPEP2  -  X-prolyl aminopeptidase (aminopeptidase P)...

Sus scrofa

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Disease relevance of XPNPEP2

  • Human cytosolic AP-P isozymes and Escherichia coli AP-P exhibited different inhibitor profiles than mammalian membrane-bound AP-P isozymes [1].

High impact information on XPNPEP2


Biological context of XPNPEP2

  • Aminopeptidase P (AP-P; X-Pro aminopeptidase; EC, a key enzyme in the metabolism of the vasodilator bradykinin, has been cloned from a pig kidney cortex cDNA library following the use of the PCR to identify sub-libraries enriched in AP-P clones [5].
  • In this study, we have determined structure-activity relationships for apstatin analogues as well as for other chemical classes of inhibitors using AP-P isozymes from different sources [1].
  • Purification and amino acid sequence of aminopeptidase P from pig kidney [6].
  • The racemic center at the Amp residue did not prevent total hydrolysis of the Lys derivative, suggesting that subsite specificity in AP-P does not extend as far as the P3' position [7].
  • Northern hybridization analysis and RT-PCR suggests that the soluble and membrane-bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences [8].

Anatomical context of XPNPEP2

  • Molecular cloning and expression in COS-1 cells of pig kidney aminopeptidase P [5].
  • Aminopeptidase P (EC was solubilized from pig kidney membranes with bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) and then purified by a combination of anion-exchange and hydrophobic-interaction chromatographies [9].
  • Pig kidney aminopeptidase P (AP-P; EC has been purified to homogeneity after its solubilisation from brush border membranes by phosphatidylinositol-specific phospholipase C. The effects of various activators and inhibitors of AP-P activity have been examined with a number of different substrates for the enzyme [10].
  • Similarly, Vmax/Km values of AmP in plasmas of cat, dog, rabbit, pig, calf (serum), human and rat were 0, 0.016, 0.025, 0.068, 0.191, 0.237 and 3.53 min-1 [11].
  • In culture, Vmax/Km of AmP was 3 to 10 x 10(-4) min-1 for human basal arterial and rabbit and bovine pulmonary arterial endothelial cell monolayers (2 x 10(5) cells) [11].

Associations of XPNPEP2 with chemical compounds

  • Several inhibitors of angiotensin converting enzyme were also found to inhibit aminopeptidase P, whereas inhibitors of other mammalian aminopeptidases were ineffective [3].
  • 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 [1].
  • Enzymic deglycosylation revealed that aminopeptidase P is a glycoprotein, with up to 25% by weight of the protein being due to the presence of N-linked sugars [9].
  • The activity of aminopeptidase P was inhibited by chelating agents and was stimulated by Mn2+ or Co2+ ions, confirming the metallo-enzyme nature of this peptidase [9].
  • The involvement of other peptidases known to be responsible for BK cleavage in other tissues and body fluids, namely carboxypeptidase N (EC, post proline cleaving enzyme (EC and aminopeptidase P (EC was excluded [12].

Other interactions of XPNPEP2

  • Two polyclonal antisera were raised in rabbits to the phospholipase C-solubilized forms of pig renal dipeptidase (EC and pig aminopeptidase P (EC [13].
  • Both of these detergent-insoluble complexes were enriched in the glycosyl-phosphatidylinositol (GPI)-anchored ectoenzymes alkaline phosphatase, aminopeptidase P and 5'-nucleotidase, and both complexes excluded the polypeptide-anchored ectoenzymes angiotensin-converting enzyme, dipeptidyl peptidase IV and aminopeptidases A and N [14].

Analytical, diagnostic and therapeutic context of XPNPEP2

  • Those antibodies recognising the cross-reacting determinant (CRD) were isolated by chromatography on a column of immobilized phospholipase C-solubilized porcine aminopeptidase P (EC, and the epitopes involved in the recognition were then characterized by immunoelectrophoretic blot analysis and by a competitive ELISA [15].


  1. Apstatin analogue inhibitors of aminopeptidase P, a bradykinin-degrading enzyme. Maggiora, L.L., Orawski, A.T., Simmons, W.H. J. Med. Chem. (1999) [Pubmed]
  2. Monocyte- and cytokine-induced downregulation of angiotensin-converting enzyme in cultured human and porcine endothelial cells. Papapetropoulos, A., Antonov, A., Virmani, R., Kolodgie, F.D., Munn, D.H., Marczin, N., Ryan, J.W., Gerrity, R.G., Catravas, J.D. Circ. Res. (1996) [Pubmed]
  3. Inhibition by converting enzyme inhibitors of pig kidney aminopeptidase P. Hooper, N.M., Hryszko, J., Oppong, S.Y., Turner, A.J. Hypertension (1992) [Pubmed]
  4. Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P. Cottrell, G.S., Hyde, R.J., Lim, J., Parsons, M.R., Hooper, N.M., Turner, A.J. Biochemistry (2000) [Pubmed]
  5. 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]
  6. Purification and amino acid sequence of aminopeptidase P from pig kidney. Vergas Romero, C., Neudorfer, I., Mann, K., Schäfer, W. Eur. J. Biochem. (1995) [Pubmed]
  7. Evaluation of some fluorogenic substrates for continuous assay of aminopeptidase P. Hawthorne, S.J., Harriott, P., Lim, J., Turner, A.J., Walker, B., Williams, C.H. Anal. Biochem. (1997) [Pubmed]
  8. Cloning and tissue distribution of human membrane-bound aminopeptidase P. Venema, R.C., Ju, H., Zou, R., Venema, V.J., Ryan, J.W. Biochim. Biophys. Acta (1997) [Pubmed]
  9. Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme. Hooper, N.M., Hryszko, J., Turner, A.J. Biochem. J. (1990) [Pubmed]
  10. Inhibition and metal ion activation of pig kidney aminopeptidase P. Dependence on nature of substrate. Lloyd, G.S., Hryszko, J., Hooper, N.M., Turner, A.J. Biochem. Pharmacol. (1996) [Pubmed]
  11. Species variation in pulmonary endothelial aminopeptidase P activity. Chen, X., Orfanos, S.E., Ryan, J.W., Chung, A.Y., Hess, D.C., Catravas, J.D. J. Pharmacol. Exp. Ther. (1991) [Pubmed]
  12. Degradation of bradykinin in semen of ram and boar. Boettger, A., Kertscher, U., Steinmann, C., Baeger, U., Siems, W.E., Heder, G. Biochem. Pharmacol. (1993) [Pubmed]
  13. Characterization of antibodies to the glycosyl-phosphatidylinositol membrane anchors of mammalian proteins. Hooper, N.M., Broomfield, S.J., Turner, A.J. Biochem. J. (1991) [Pubmed]
  14. Isolation and characterization of two distinct low-density, Triton-insoluble, complexes from porcine lung membranes. Parkin, E.T., Turner, A.J., Hooper, N.M. Biochem. J. (1996) [Pubmed]
  15. Characterization of an antibody to the cross-reacting determinant of the glycosyl-phosphatidylinositol anchor of human membrane dipeptidase. Broomfield, S.J., Hooper, N.M. Biochim. Biophys. Acta (1993) [Pubmed]
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