34
Views
4
CrossRef citations to date
0
Altmetric
Review

Aminopeptidase A inhibitors

, &
Pages 431-444 | Published online: 25 Feb 2005

Bibliography

  • WILK S, HEALY DP: Glutamyl aminopeptidase (aminopeptidase A), the BP-1/6C3 antigen. Adv. Neuroimmunol. (1993) 3:195–207.
  • ••This is the first review of APA describing the purification, thephysical properties, the substrate specificity, the effect of metal ions (Ca2+ and Zn2+), the localisation of the enzyme, its biological role, the identity BP-1/6C3 antigen with the regulation of APA and its inhibition.
  • WANG J, COOPER MD: Ilistidine residue in the zinc binding motif of aminopeptidase A is critical for enzymatic activity. Proc. Natl. Acad. Sci. USA (1993) 90:1222–1226.
  • RAWLING ND, BARRETT AJ: Evolutionary families ofmetallopeptidases. Methods Enzymol. (1 9 9 5) 248:183–228.
  • ZINI S, FOURNIE-ZALUSKI MC, CHAUVEL EN et al.: Identi- fication of metabolic pathways of brain angiotensin II and III using specific aminopeptidase inhibitors: predominant role of angiotensin III in the control of vasopressin release. Proc. Natl. Acad. Sci. USA (1996) 93:11968–11973.
  • ••Demonstration of the metabolic pathway of angiotensins inbrain by means of selective APA and APN inhibitors.
  • CHANSEL D, CZEKALSKI S, VANDERMEERSCH S, et al: Characterization of angiotenin IV degrading enzymes and receptors on rat mesangial cells. Am. J. Physiol (1998) 275:535–542.
  • THORSETT ED, WYVRATT MJ: Inhibition of zinc peptidases that hydrolyse neuropep tides. In: Neuropep-tides and their peptidases. Turner AJ (Ed.), Ellis Horwood Ltd. Chinchester, England (1987):229–292.
  • REAUX A, FOURNIE-ZALUSKI M-C, ZINI S. et al.: Arninopeptidase A inhibitors as potential central antihypertensive agents. Proc. Natl. Acad. Sci. USA (1999) 96 (23) :13415–13420.
  • ••Demonstration of the decrease in blood pressure ensured byinhibition of the tonic release of angiotensin III.
  • MIGAUD M, DURIEUX C, CHAUVEL EN et al.: The in vivo metabolism of cholecystokinin (CCK8) is essentially ensured by aminopeptidase A. Peptides (1996) 17 (0601–607.
  • NOBLE F, ROQUES BP: CCK-B receptor: chemistry, molecular biology biochemistry and pharmacology. Progress Neurobiol. (1999) 58:349–379.
  • •Review on brain CCK8, its metabolism and pharmacology.
  • ROQUES BP, NOBLE F, DAUGE V, FOURNIE-ZALUSKI M-C, BEAUMONT A: Neutral endopeptidase 24.11: structure, inhibition and experimental and clinical pharma-cology. Pharmacol. Rev. (1993) 45:87–146.
  • •Molecular mechanism of peptide bond hydrolysis by zinc metallopeptidases and strategies used in designing inhibitors.
  • ROQUES BP: Novel approaches to targeting neuropep-tide systems. Trends Pharmacol Sci. (2000) 21:475–483.
  • LOJDA Z, GOSSRAU R: Study on aminopeptidase A. Histochemistry (1980) 67:267–290.
  • ••This is a complete and systematic comparative biochemicaland histochemical investigation of the localisation of the enzyme in the cardiovascular, the digestive, the respiratory, the urogenital systems, the liver and lung, the endocrine, the central and peripheral nervous systems.
  • ZINI S, MASDEHORS P, LENKEI Z et al.: Arninopeptidase A: distribution in rat brain nuclei and increased activity in spontaneously hypertensive rat. Neurosci-ence (1997) 78 (4) :1187–1193.
  • ••This is a more precise distribution of APA in rat brain nucleiusing microdissection.
  • RAMIREZ MJ, MARTINEZ JM, PRIETO I, ALBA F, RAMIREZ M: Lateralization of aminopeptidase A activity in substantia nigra, striatum and frontal cortex of rats. Neuropeptides (1999) 33 (2) :155–158.
  • WU Q, LI L, COOPER MD, PIERUS M, GORVEL JP: Aminopeptidase A activity in the murine B-lymphocytes differentiation antigen BP-1 /6 C3. Proc. Natl. Acad. Sci. USA (1991) 88:676–680.
  • •Molecular identity between APA and BP-1/6C3.
  • LI, L, WANG, J, COOPER, M.D. cDNA cloning and expres- sion of human glutamyl aminopeptidase (aminopepti-dase A). Genomics (1993) 17:657–664.
  • •Sequence of APA.
  • NANUS DM, ENGELSTEIN D, GASTL GA et al.: Molecular cloning of the human kidney differentiation antigen gp160: human aminopeptidase A. Proc. Natl. Acad. Sci. USA (1993) 90:7069–7073.
  • •Sequence of human APA and comparison with other zinc peptidases.
  • WANG J, WALKER H, LIN Q et al.: The mouse BP-1 gene: structure, chromosomal localization and regulation of expression by Type I interferons and interleukin-7. Genomics (1996) 33:167–176.
  • VAZEUX G, WILK S, WILK E, CORVOL P, LLORENS-CORTES C: Production and properties of a recombi-nant soluble form of aminopeptidase A. Eur.J. Biochem. (1998) 254:671–678.
  • •Removal of the transmembraneous sequence of APA. The soluble form has the same enzymatic properties that the WT enzyme.
  • CHEUNG HS, CUSHMAN, DW: A soluble aspartate aminopeptidase from dog kidney. Biochem. Biophys. Acta (1971) 242:190–193.
  • KELLY JA, NEIDLE EL, NEIDLE A: An aminopeptidase from mouse brain cytosol that cleaves N-terminal amino acid residues. J. Neurochem. (1983) 40:1727–1734.
  • WILK S, WILK E, MAGNUSSON RP: Purification, charac-terization and cloning of a cytosolic aspartyl aminopeptidase. J. Biol. Chem. (1998) 273 (26):15961–15970.
  • VAZEUX G, WANG J, COOPER M, CORVOL P, LLORENS-CORTES C: Identification of glutamate residues essential for catalytic activity and zinc coordination in aminopeptidase A. J. Biol. Chem. (1996) 271 (15)9069–9074.
  • VAZEUX, G, ITURRIOZ, X, CORVOL, P, LLORENS-CORTES, C. A tyrosine residue essential for catalytic activity in aminopeptidase A. Biochem. J (1997) 327 (3):883–889.
  • LUCIANI N, MARIE-CLAIRE C, RUFFET E et al: Characteri-zation of G1u35° as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC.3.4.11.2): insights into its mechanism of action. Biochemistry (1998) 37(2):686–692.
  • VAZEUX G, ITURRIOZ X, CORVOL P, LLORENS-CORTES C: A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A. Biochem. J (1998) 334:407–413.
  • MATTHEWS BW: Structural basis of the action ofthermolysin and related zinc peptidases. Acc. Chem. Res. (1988) 21 :333–340.
  • MARIE-CLAIRE C, RUFFET E, TIRABOSCHI G, FOURNIE-ZALUSKI MC: Differences in transition state stabiliza-tion between thermolysin (EC 3.4.2 4.27) and neprilysin (EC 3.4.24.11). FEBSLett. (1998) 438:215–219.
  • DANIELSON EM, NOREN 0, SJOSTROM TT, INGRAM J, KENNY AJ: Proteins of the kidney microvillar membrane. Aspar tate aminopeptidase: purification by immunoabsorbent chromatography and properties of the detergent- and proteinase-solubilized forms. Biochem. J. (1980) 189:591–603.
  • ITURRIOZ X, VAZEUX G, CELERIER J, CORVOL P, LLORENS-CORTES C: Ilistidine 450 plays a critical role in catalysis and, with Ca2+, contributes to the substrate specificity of aminopeptidase A. Biochemistry (2000) 39(103061–3068.
  • TOBE H, MORISHIMA H, NAGANAWA H et al: Structure and chemical synthesis of amastatin. Agrk. Biol. Chem. (1979) 43(3):591–596.
  • TOBE H, MORISHIMA T, AOYAGI T et al.: Synthesis and structure-activity relationships of amastatin analogues, inhibitors of aminopeptidase A. Agrk. Biol. Chem. (1982) 46(7):1865–1872.
  • TIEKU S, HOOPER NM; Inhibition of aminopeptidases N, A and W. A re-evaluation of the actions of bestatin and inhibitors of angiotensin converting enzyme. Biochem. Pharmacol. (1992) 44:1725–1730.
  • YOSHIDA S, NAKAMURA Y, NAGANAWA H, AOYAGI T, TAKEUCHI T:Probestin, a new inhibitor of aminopepti-dase M, produced by Streptomyces azureus MH663-2F6. II. Structure determination of probestin. Antibiol (1990) 43 (2) :149–153.
  • NAGAI M, KOJIMA F, NAGANAWA H. et al: Phebestin, a new inhibitor of aminopeptidase N, produced by Streptomyces sp. MJ71 6-m3. J. Antibiot. (1997) 50 (1):82–84.© Ashley Publications Ltd. All rights reserved.Exp. Opin. Ther. Patents (2001) 11(3)
  • AOYAGI T, YOSHIDA S, MATSUDA N et al: lzuhistin, a new inhibitor of aminopeptidase M, produced by Bacillus laterosporus BMI156-14 F1 . I. Taxonomy, production, isolation, physico-chemical properties and biological activities. j Antibiol (1991) 44 (6):573–578.
  • UMEZAWA H, AOYAGI T, OHUCHI S eta].: Arphamenine A and B, new inhibitors of aminopeptidase B, produced by bacteria. J. Antibiot. (1983) 36(10:1572–1575.
  • CHUNG A, RYAN JW, BEIRYER P: Inhibition of theformation of angiotensin III. Adv. Exp. Med. Biol. (1983) 156:693–703.
  • WILK S, THURSTON LS: Inhibition of angiotensin III formation by thiol derivatives of acidic amino acids. Neuropeptides (1990) 16:163–168.
  • CHAUVEL EN, CORIC P, LLORENS-CORTES C et al: Investigation of the active-site of aminopeptidase A using a series of new thiol- containing inhibitors. J Med. Chem. (1994) 37(9):1339–1346.
  • CHAUVEL EN, LLORENS-CORTES C, CORIC P et al: Differ-ential inhibition of aminopeptidase A and aminopep-tidase N by new 13-amino thiols. J Med. Chem. (1994) 37 (18):2950–2957.
  • ••A complete structure-activity investigation of the Si subsiteof APA leading to the first specific inhibitor of APA versus APN with an affinity in the 106–10 7 M range.
  • KAZNADAR T, DAVID C, CRETE D et al : Arninopeptidase A involved in the inactivation of endogenous CCK8: a micro dialysis study. J. Neuropsychopharmacol. (1997) 11:A50.
  • ZINI S, DEMASSEY Y, FOURNIE-ZALUSKI M-C et al: Inhibition of vasopressinergic neurons by central injection of a specific aminopeptidase A inhibitor. Neuroreport (1998) 9:825–828.
  • •Demonstration of the role of angiotensin III on the regula-tion of plasma vasopressin release.
  • LEJCZAK B, POPIEL DE, CHOSZAK M, KAFARSKI P: Inhibi-tion of aminopeptidases by phosphonic acid analogues of aspartic and glutamic acids. J Enz. Inh. (1993) 7:97–103.
  • DAVID C, BISCHOFF L, MEUDAL H et al: Investigation of subsite preferences in aminopeptidase A (EC 3.4.11.7) led to the design of the first highly potent and selective inhibitors of this enzyme. J Med. Chem. (1999) 42 (25):5197–5211.
  • ••A complete characterisation of the three Si, Si' and Szt sub-sites of APA leading to the first nanomolar and subnano-molar inhibitors of the enzyme in the thiol series described to date.
  • DAVID-BASEI C, BISCHOFF L, FOURNIE-ZALUSKI M-C, ROQUES BP: Synthesis of [[(25:3R):3-amino-2-sulfhydry1-5-sulfonate]-pentanoyll-L-34125IFiodo- tyrosine-L-aspartic acid: a radiolabelled inhibitor of aminopeptidase A. J. Lab. Comp. Radiopharm. (2001) 44:89–98
  • •A compound for visualisation of APA.
  • CHEN H, NOBLE F, MOTHE A et al.: Phosphinic deriva-tives as new dual enkephalin degrading enzyme inhibitors: synthesis, biological properties and antinociceptive activities. J. Med. Chem. (2000) 43 (7):1398–1408.
  • GEORGIADIS D, VAZEUX G, LLORENS-CORTES C, YIOTAKIS A, DIVE V. Potent and selective inhibition of zinc aminopeptidase A (EC 3.4.11.7, APA) by glutamyl aminophosphinic peptides: importance of glutamyl aminophosphinic residue in the P1 position. Biochem-istry (2000) 39 (5):1152–1155.
  • •A study reporting nanomolar and subnanomolar inhibitors of APA in the phosphinic series
  • LIN Q, TANIUCHI I, KITAMURA D et al: T and B cell development in BP-1 /6C3 /Aminopeptidase A-deficient mice. j linmunoi. (1998) 160:4681–4687.
  • KUDA T, SHOJI M, ARAI H, KAWASHIMA S, SAIDO TC: Reduction of plasma glutamyl aminopeptidase activity in sporadic Alzheimer's disease. Biochem. Biophys. Res. Commun. (1997) 231:526–530.
  • FINSTAD CL, CORDON-CARDO C, BANDER NH et al: Specificity analysis of mouse monoclonal antibodies defining cell surface antigens of human renal cancer. Proc. Nat. Acad. Sci. USA (1985) 82:2955–2959.
  • BOGENRIEDER T, FINSTAD CL, FREEMAN RH et al: Expression and localization of aminopeptidase A, aminopeptidase N and dipeptidyl peptidase W in benign and malignant human prostate tissue. The Prostate (1997) 33:225–232.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.