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Gene Review

Anpep  -  alanyl (membrane) aminopeptidase

Mus musculus

Synonyms: AP-M, AP-N, Alanyl aminopeptidase, Aminopeptidase M, Aminopeptidase N, ...
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Disease relevance of Anpep


High impact information on Anpep


Chemical compound and disease context of Anpep


Biological context of Anpep

  • The predicted amino acid sequence of the cDNA encoding the murine B-lymphocyte differentiation antigen BP-1/6C3 suggested that it is a member of the zinc-dependent metalloprotease family, possibly an aminopeptidase related to aminopeptidase N [microsomal aminopeptidase; alpha-aminoacyl-peptide hydrolase (microsomal), EC] [14].
  • The position of the Thy-1 (theta cell surface antigen) locus on chromosome 9 of the mouse was determined relative to the biochemical markers Lap-1 (leucine arylaminopeptidase) and Mpi-1 (mannosephosphate isomerase) [15].
  • This is corroborated by the fact that the selective APN inhibitor PC18 administered alone via the i.c.v. route increased arterial blood pressure [16].
  • Backcross data produced the following gene order and map distances: Lap-1 (31.6 +/- 7.5 cM) Es-13 (2.6 +/- 2.6 cM) Mod-1 [17].
  • Rab3 GAP consists of two subunits: the catalytic subunit p130 and the noncatalytic subunit p150 [18].

Anatomical context of Anpep


Associations of Anpep with chemical compounds

  • This pressor response was blocked by prior treatment with the angiotensin type 1 receptor antagonist losartan, showing that blocking the action of APN on AngIII metabolism leads to an increase in endogenous AngIII levels, resulting in arterial blood pressure increase through an interaction with angiotensin type 1 receptors [16].
  • These results demonstrate for the first time that (i) APA and APN are involved in vivo in the metabolism of brain Ang II and Ang III, respectively, and that (ii) the action of Ang II on vasopressin release depends upon the prior conversion of Ang II to Ang III [21].
  • Mice received [3H]Ang II intracerebroventricularly (i.c.v.) in the presence or absence of the APN inhibitor, EC33 (3-amino-4-thio-butyl sulfonate) of the APN inhibitor, EC27 (2-amino-pentan-1,5-dithiol) [21].
  • Recently, a potent APN inhibitor, PC18 (2-amino-4-methylsulfonyl butane thiol, methionine thiol), has been developed [22].
  • This pressor response was blocked by prior treatment with the angiotensin type 1 (AT(1)) receptor antagonist, losartan, showing that blocking the action of APN on AngIII metabolism leads to an increase in endogenous AngIII levels, resulting in BP increase, through interaction with AT(1) receptors [23].

Regulatory relationships of Anpep


Other interactions of Anpep

  • Secondly, we developed a specific and selective APA inhibitor, compound EC33 [(S)-3-amino-4-mercaptobutylsulphonic acid], as well as a potent and selective APN inhibitor, PC18 (2-amino-4-methylsulphonylbutane thiol) [16].
  • By observing the segregation of alleles at the Mod-1 (cytoplasmic malic enzyme) locus, which is known to lie distal to these three markers, it was possible to show that Lap-1 is at the centromeric end of this gene group [15].
  • Jejunal ApN and DPPIV activities were lower for obese mice before resection; ileal ApN activity was unaltered after resection for both strains [25].
  • The results of our experiments show that in all brain parenchyma vessels of all sizes, pericytes and periendothelial cells are immunoreactive for aminopeptidase N, essentially at the plasma membrane level, and are also labeled by nestin specific antibodies, which decorate typical intermediate filaments [26].
  • A small reduction in [Leu(5)]enkephalin degradation was detected in striatal membrane preparations of NEP-/- mice, if aminopeptidase N was additionally blocked by bestatin or amastatin [27].

Analytical, diagnostic and therapeutic context of Anpep


  1. A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules. Hansen, A.S., Norén, O., Sjöström, H., Werdelin, O. Eur. J. Immunol. (1993) [Pubmed]
  2. H-2M3 presents a Listeria monocytogenes peptide to cytotoxic T lymphocytes. Pamer, E.G., Wang, C.R., Flaherty, L., Lindahl, K.F., Bevan, M.J. Cell (1992) [Pubmed]
  3. Aminopeptidase N is involved in cell motility and angiogenesis: its clinical significance in human colon cancer. Hashida, H., Takabayashi, A., Kanai, M., Adachi, M., Kondo, K., Kohno, N., Yamaoka, Y., Miyake, M. Gastroenterology (2002) [Pubmed]
  4. Expression of interferon-inducible RNA adenosine deaminase ADAR1 during pathogen infection and mouse embryo development involves tissue-selective promoter utilization and alternative splicing. George, C.X., Wagner, M.V., Samuel, C.E. J. Biol. Chem. (2005) [Pubmed]
  5. Expression and different polarity of aminopeptidase N in normal human colonic mucosa and colonic tumors. Quaroni, A., Nichols, B.L., Quaroni, E., Hurst, K., Herrera, L., Weiser, M.M., Hamilton, S.R. Int. J. Cancer (1992) [Pubmed]
  6. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Lioubin, M.N., Algate, P.A., Tsai, S., Carlberg, K., Aebersold, A., Rohrschneider, L.R. Genes Dev. (1996) [Pubmed]
  7. T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides. Larsen, S.L., Pedersen, L.O., Buus, S., Stryhn, A. J. Exp. Med. (1996) [Pubmed]
  8. Mast cells lacking the high affinity immunoglobulin E receptor are deficient in Fc epsilon RI gamma messenger RNA. Ryan, J.J., Kinzer, C.A., Paul, W.E. J. Exp. Med. (1995) [Pubmed]
  9. Transcytosis of immunoglobulin A in the mouse enterocyte occurs through glycolipid raft- and rab17-containing compartments. Hansen, G.H., Niels-Christiansen, L.L., Immerdal, L., Hunziker, W., Kenny, A.J., Danielsen, E.M. Gastroenterology (1999) [Pubmed]
  10. Activation and cytotoxicity of 2-alpha-aminoacyl prodrugs of methotrexate. Smal, M.A., Dong, Z., Cheung, H.T., Asano, Y., Escoffier, L., Costello, M., Tattersall, M.H. Biochem. Pharmacol. (1995) [Pubmed]
  11. Anti-tumor angiogenesis effect of aminopeptidase inhibitor bestatin against B16-BL6 melanoma cells orthotopically implanted into syngeneic mice. Aozuka, Y., Koizumi, K., Saitoh, Y., Ueda, Y., Sakurai, H., Saiki, I. Cancer Lett. (2004) [Pubmed]
  12. Production of actinonin, an inhibitor of aminopeptidase M, by actinomycetes. Umezawa, H., Aoyagi, T., Tanaka, T., Suda, H., Okuyama, A., Naganawa, H., Hamada, M., Takeuchi, T. J. Antibiot. (1985) [Pubmed]
  13. Probestin, a new inhibitor of aminopeptidase M, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties and biological activities. Aoyagi, T., Yoshida, S., Nakamura, Y., Shigihara, Y., Hamada, M., Takeuchi, T. J. Antibiot. (1990) [Pubmed]
  14. Aminopeptidase A activity of the murine B-lymphocyte differentiation antigen BP-1/6C3. Wu, Q., Li, L., Cooper, M.D., Pierres, M., Gorvel, J.P. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  15. Location of the gene for theta antigen in the mouse. III. The position of Thy-1 relative to Lap-1 and Mpi-1. Douglas, T.C., Dawson, P.E. J. Hered. (1979) [Pubmed]
  16. Aminopeptidase A, which generates one of the main effector peptides of the brain renin-angiotensin system, angiotensin III, has a key role in central control of arterial blood pressure. Reaux, A., Iturrioz, X., Vazeux, G., Fournie-Zaluski, M.C., David, C., Roques, B.P., Corvol, P., Llorens-Cortes, C. Biochem. Soc. Trans. (2000) [Pubmed]
  17. Esterase 13, a new mouse esterase locus with recessive expression and its genetic location on chromosome 9. Womack, J.E., Taylor, B.A., Barton, J.E. Biochem. Genet. (1978) [Pubmed]
  18. Rab3 GTPase-activating protein regulates synaptic transmission and plasticity through the inactivation of Rab3. Sakane, A., Manabe, S., Ishizaki, H., Tanaka-Okamoto, M., Kiyokage, E., Toida, K., Yoshida, T., Miyoshi, J., Kamiya, H., Takai, Y., Sasaki, T. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  19. Histochemical study of aminopeptidase M, aminopeptidase A, and gamma-glutamyltransferase in the nasal cavity of laboratory rodents andman. Kubisová, I., Pospísilová, B. Sborník vědeckých prací Lékařské fakulty Karlovy university v Hradci Králové. (1994) [Pubmed]
  20. p161, a murine membrane protein expressed on mast cells and some macrophages, is mouse CD13/aminopeptidase N. Chen, H., Kinzer, C.A., Paul, W.E. J. Immunol. (1996) [Pubmed]
  21. Identification of metabolic pathways of brain angiotensin II and III using specific aminopeptidase inhibitors: predominant role of angiotensin III in the control of vasopressin release. Zini, S., Fournie-Zaluski, M.C., Chauvel, E., Roques, B.P., Corvol, P., Llorens-Cortes, C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  22. PC18, a specific aminopeptidase N inhibitor, induces vasopressin release by increasing the half-life of brain angiotensin III. Réaux, A., de Mota, N., Zini, S., Cadel, S., Fournié-Zaluski, M.C., Roques, B.P., Corvol, P., Llorens-Cortès, C. Neuroendocrinology (1999) [Pubmed]
  23. Aminopeptidase A inhibitors as potential central antihypertensive agents. Reaux, A., Fournie-Zaluski, M.C., David, C., Zini, S., Roques, B.P., Corvol, P., Llorens-Cortes, C. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  24. Composite effects of actinonin when inhibiting enkephalin-degrading enzymes. Hachisu, M., Hiranuma, T., Shibazaki, Y., Uotani, K., Murata, S., Aoyagi, T., Umezawa, H. Eur. J. Pharmacol. (1987) [Pubmed]
  25. Altered small intestinal absorptive enzyme activities in leptin-deficient obese mice: influence of bowel resection. Kiely, J.M., Noh, J.H., Svatek, C.L., Pitt, H.A., Swartz-Basile, D.A. J. Pediatr. Surg. (2006) [Pubmed]
  26. Pericytes and periendothelial cells of brain parenchyma vessels co-express aminopeptidase N, aminopeptidase A, and nestin. Alliot, F., Rutin, J., Leenen, P.J., Pessac, B. J. Neurosci. Res. (1999) [Pubmed]
  27. Neutral endopeptidase and alcohol consumption, experiments in neutral endopeptidase-deficient mice. Siems, W., Maul, B., Krause, W., Gerard, C., Hauser, K.F., Hersh, L.B., Fischer, H.S., Zernig, G., Saria, A. Eur. J. Pharmacol. (2000) [Pubmed]
  28. A tyrosine residue essential for catalytic activity in aminopeptidase A. Vazeux, G., Iturrioz, X., Corvol, P., Llorens-Cortès, C. Biochem. J. (1997) [Pubmed]
  29. Aminophosphinic inhibitors as transition state analogues of enkephalin-degrading enzymes: a class of central analgesics. Chen, H., Noble, F., Coric, P., Fournie-Zaluski, M.C., Roques, B.P. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  30. Establishment of renal proximal tubule cell lines by targeted oncogenesis in transgenic mice using the L-pyruvate kinase-SV40 (T) antigen hybrid gene. Cartier, N., Lacave, R., Vallet, V., Hagege, J., Hellio, R., Robine, S., Pringault, E., Cluzeaud, F., Briand, P., Kahn, A. J. Cell. Sci. (1993) [Pubmed]
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