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Enpep  -  glutamyl aminopeptidase

Mus musculus

Synonyms: 6030431M22Rik, AP-A, APA, Aminopeptidase A, BP-1/6C3 antigen, ...
 
 
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Disease relevance of Enpep

 

Psychiatry related information on Enpep

 

High impact information on Enpep

  • We previously reported that in the murine brain, aminopeptidase A (APA) is involved in the conversion of angiotensin II (AngII) to AngIII and that AngIII is one of the main effector peptides of the brain RAS in the control of vasopressin release [7].
  • A single dose of systemic RB150 (15 mg/kg, i.v.) in conscious DOCA-salt rats inhibited brain APA activity and markedly reduced blood pressure for up to 24 h [7].
  • Brain renin-angiotensin system blockade by systemically active aminopeptidase A inhibitors: a potential treatment of salt-dependent hypertension [7].
  • RB150 given i.v. is able to cross the blood-brain barrier, to inhibit brain APA, and to block the formation of central AngIII [7].
  • 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 [8].
 

Chemical compound and disease context of Enpep

  • There was no clear relation between the inhibition of glomerular APA activity and albuminuria, yet it was evident that intrarenal Ang II levels were significantly increased in albuminuric mice and not in nonalbuminuric mice [9].
  • We have investigated the effects of glucose concentration on the bioenergetic status and on the metabolic and secretory functions exhibited by mouse insulinoma betaTC3 cells entrapped in calcium alginate/poly-L-lysine/alginate (APA) beads [10].
  • Both enalapril and losartan treatment reduced the acute albuminuria, measured 1 day after injection of a monoclonal antibody against aminopeptidase A, by 91% and 83%, respectively [11].
  • The effects of alginate composition on cell growth as well as the metabolic and secretory profile of transformed beta-cells entrapped in alginate/poly-L-lysine/alginate (APA) solid beads were investigated following entrapment of beta TC3 mouse insulinoma cells in alginate composed of either high mannuronic acid or high guluronic acid residues [12].
  • Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes [13].
 

Biological context of Enpep

 

Anatomical context of Enpep

  • Aminopeptidase A activity of the murine B-lymphocyte differentiation antigen BP-1/6C3 [17].
  • From brush border preparations of the small intestine, a rich source of many endopeptidases and exopeptidases, the BP-1 antibody selectively removed aminopeptidase A [APA; L-alpha-aspartyl(L-alpha-glutamyl)-peptide hydrolase, EC 3.4.11.7] activity [17].
  • The APA activity of a panel of cell lines correlated in linear fashion with cell-surface levels of the BP-1/6C3 antigen [17].
  • Thus APA, the enzyme responsible for the formation of brain AngIII, represents a potential central therapeutic target that justifies the development of APA inhibitors, crossing the blood-brain barrier, as central anti-hypertensive agents [14].
  • Activity of APM and APA was found mostly in the fibrocytes which adhered to the basal membrane of the epithelium and glands [18].
 

Associations of Enpep with chemical compounds

  • This activity was enhanced by alkaline earth metals such as Ca2+ and was abrogated by amastatin and angiotensin, which are known competitive inhibitors of APA [17].
  • The data indicate that the murine BP-1/6C3 antigen is active APA, an enzyme that catalyzes specifically the removal of unsubstituted, N-terminal glutamic acid and aspartic acid residues from peptides [17].
  • Contribution of molecular modeling and site-directed mutagenesis to the identification of a new residue, glutamate 215, involved in the exopeptidase specificity of aminopeptidase A [19].
  • In female mice, cholesterol-enriched diet produced a significant increase in soluble aspartyl- and membrane-bound aspartyl- and glutamyl-aminopeptidase activities, and a significant decrease in membrane-bound alanyl-, arginyl- and cystinyl-aminopeptidase activities [20].
  • BP-1/6C3/APA expression by early B lineage cells is up-regulated by IL-7, an important growth factor for pre-B cells and T cells [21].
 

Other interactions of Enpep

 

Analytical, diagnostic and therapeutic context of Enpep

References

  1. Hypertension and angiotensin II hypersensitivity in aminopeptidase A-deficient mice. Mitsui, T., Nomura, S., Okada, M., Ohno, Y., Kobayashi, H., Nakashima, Y., Murata, Y., Takeuchi, M., Kuno, N., Nagasaka, T., O-Wang, J., Cooper, M.D., Mizutani, S. Mol. Med. (2003) [Pubmed]
  2. Enhancement of myoblast microencapsulation for gene therapy. Li, A.A., Shen, F., Zhang, T., Cirone, P., Potter, M., Chang, P.L. Journal of biomedical materials research. Part B, Applied biomaterials. (2006) [Pubmed]
  3. A nephritogenic rat monoclonal antibody to mouse aminopeptidase A. Induction of massive albuminuria after a single intravenous injection. Assmann, K.J., van Son, J.P., Dijkman, H.B., Koene, R.A. J. Exp. Med. (1992) [Pubmed]
  4. Physiologic self antigens rapidly capacitate autoimmune disease-specific polyclonal CD4+ CD25+ regulatory T cells. Setiady, Y.Y., Ohno, K., Samy, E.T., Bagavant, H., Qiao, H., Sharp, C., She, J.X., Tung, K.S. Blood (2006) [Pubmed]
  5. Mouse glomerular epithelial cells in culture with features of podocytes in vivo express aminopeptidase A and angiotensinogen but not other components of the renin-angiotensin system. Mentzel, S., Van Son, J.P., De Jong, A.S., Dijkman, H.B., Koene, R.A., Wetzels, J.F., Assmann, K.J. J. Am. Soc. Nephrol. (1997) [Pubmed]
  6. Lack of angiotensin II conversion to angiotensin III increases water but not alcohol consumption in aminopeptidase A-deficient mice. Faber, F., Gembardt, F., Sun, X., Mizutani, S., Siems, W.E., Walther, T. Regul. Pept. (2006) [Pubmed]
  7. Brain renin-angiotensin system blockade by systemically active aminopeptidase A inhibitors: a potential treatment of salt-dependent hypertension. Fournie-Zaluski, M.C., Fassot, C., Valentin, B., Djordjijevic, D., Reaux-Le Goazigo, A., Corvol, P., Roques, B.P., Llorens-Cortes, C. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  8. 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]
  9. Albuminuria in mice after injection of antibodies against aminopeptidase A: role of angiotensin II. Gerlofs-Nijland, M.E., Assmann, K.J., Dijkman, H.B., Dieker, J.W., van Son, J.P., Mentzel, S., van Kats, J.P., Danser, A.H., Smithies, O., Groenen, P.J., Wetzels, J.F. J. Am. Soc. Nephrol. (2001) [Pubmed]
  10. Role of ATP and Pi in the mechanism of insulin secretion in the mouse insulinoma betaTC3 cell line. Papas, K.K., Long, R.C., Constantinidis, I., Sambanis, A. Biochem. J. (1997) [Pubmed]
  11. Inhibition of aminopeptidase A activity causes an acute albuminuria in mice: an angiotensin II-mediated effect? Mentzel, S., Assmann, K.J., Dijkman, H.B., de Jong, A.S., van Son, J.P., Wetzels, J.F., Koene, R.A. Nephrol. Dial. Transplant. (1996) [Pubmed]
  12. Effects of alginate composition on the metabolic, secretory, and growth characteristics of entrapped beta TC3 mouse insulinoma cells. Constantinidis, I., Rask, I., Long, R.C., Sambanis, A. Biomaterials (1999) [Pubmed]
  13. Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes. Aoyagi, T., Tobe, H., Kojima, F., Hamada, M., Takeuchi, T., Umezawa, H. J. Antibiot. (1978) [Pubmed]
  14. 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]
  15. A tyrosine residue essential for catalytic activity in aminopeptidase A. Vazeux, G., Iturrioz, X., Corvol, P., Llorens-Cortès, C. Biochem. J. (1997) [Pubmed]
  16. Molecular cloning and expression of aminopeptidase A isoforms from rat hippocampus. Lee, H.J., Tomioka, M., Takaki, Y., Masumoto, H., Saido, T.C. Biochim. Biophys. Acta (2000) [Pubmed]
  17. 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]
  18. 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]
  19. Contribution of molecular modeling and site-directed mutagenesis to the identification of a new residue, glutamate 215, involved in the exopeptidase specificity of aminopeptidase A. Rozenfeld, R., Iturrioz, X., Okada, M., Maigret, B., Llorens-Cortes, C. Biochemistry (2003) [Pubmed]
  20. Pituitary aminopeptidase activities involved in blood-pressure regulation are modified by dietary cholesterol: sex differences. Ramírez-Expósito, M.J., Mayas, M.D., García, M.J., Ramírez, M., Martínez-Martos, J.M. Regul. Pept. (2001) [Pubmed]
  21. T and B cell development in BP-1/6C3/aminopeptidase A-deficient mice. Lin, Q., Taniuchi, I., Kitamura, D., Wang, J., Kearney, J.F., Watanabe, T., Cooper, M.D. J. Immunol. (1998) [Pubmed]
  22. An aminopeptidase from mouse brain cytosol that cleaves N-terminal acidic amino acid residues. Kelly, J.A., Neidle, E.L., Neidle, A. J. Neurochem. (1983) [Pubmed]
  23. Enzyme cytochemistry combined with electron microscopy, pharmacokinetics, and clinical chemistry for the evaluation of the effects of steady-state valproic acid concentrations on the mouse. Graf, R., Gossrau, R., Merker, H.J., Schwabe, R., Stahlmann, R., Nau, H. Histochemistry (1985) [Pubmed]
  24. Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein. Parkin, E.T., Turner, A.J., Hooper, N.M. Biochem. J. (1999) [Pubmed]
  25. Organ distribution of aminopeptidase A and dipeptidyl peptidase IV in normal mice. Mentzel, S., Dijkman, H.B., Van Son, J.P., Koene, R.A., Assmann, K.J. J. Histochem. Cytochem. (1996) [Pubmed]
  26. The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of this monozinc aminopeptidase. Rozenfeld, R., Muller, L., Messari, S.E., Llorens-Cortes, C. J. Biol. Chem. (2004) [Pubmed]
  27. Glucose metabolism in vitro of cultured and transplanted mouse pancreatic islets microencapsulated by means of a high-voltage electrostatic field. King, A., Sandler, S., Andersson, A., Hellerström, C., Kulseng, B., Skjåk-Braek, G. Diabetes Care (1999) [Pubmed]
 
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