Molecular pharmacology of endothelin converting enzymes

Biochemical Pharmacology

Volumn 51, Issue 2, 1996, Pages 91-102

  Turner, Anthony J ^a   Murphy, Leonard J ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

en dothelium; endopeptidase 24.11; endothelin; endothelin converting enzyme; metallopeptidase; phosphoramidon; thiorphan

Indexed keywords

BIG ENDOTHELIN 1; BIG ENDOTHELIN 2; BIG ENDOTHELIN 3; ENDOTHELIN; ENDOTHELIN 1; ENDOTHELIN CONVERTING ENZYME; ENZYME INHIBITOR; ISOENZYME; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; PHOSPHORAMIDON; THIORPHAN;

BIOSYNTHESIS; CARDIOVASCULAR SYSTEM; ENDOTHELIUM CELL; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; ENZYME STRUCTURE; ENZYME SUBUNIT; HUMAN; IMMUNOCYTOCHEMISTRY; KIDNEY; MOLECULAR CLONING; NONHUMAN; PH; PRIORITY JOURNAL; REVIEW;

EID: 0030032386     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(95)02036-5     Document Type: Note

References (127)

1. Roques BP, Zinc metallopeptidases: Active site structure and design of selective and mixed inhibitors: New approaches in the search for analgesics and anti-hypertensives. Biochem Soc Trans 21: 678-685, 1993.
2. Roques BP, Noble F, Dauge V, Fournié-Zaluski M-C and Beaumont A, Neutral endopeptidase 24-11: Structure, inhibition and experimental and clinical pharmacology. Pharmacol Rev 45: 87-146, 1993.
3. Masaki T and Yanagisawa M, Endothelins. Essays Biochem 271 79-89, 1992.
4. Kennedy RL, Haynes WG and Webb DJ, Endothelins as regulators of growth and function in endocrine tissues. Clin Endocrinol (Oxf) 39: 259-265, 1993.
5. Yanagisawa M, Kurihara H, Kimura S, Tomobe Y, Kobayishi Y, Mitsui Y, Yazaki Y, Goto K and Masaki T, A novel potent, vasoconstrictor peptide produced by vascular endothelial cells. Nature 332: 411-415, 1988.
6. Inoue A, Yanagisawa M, Kimura S, Kasuya Y, Miyauchi T, Goto K and Masaki T, The human endothelin family: Three structurally and pharmacologically distinct isopeptides predicted by three separate genes. Proc Natl Acad Sci USA 86: 2863-2867, 1989.
7. Shubeita HE, McDonough PM, Harris AN, Knowlton KU, Glembotski CC, Brown JH and Chien KR, Endothelin induction of inositol phospholipid hydrolysis, sarcomere assembly, and cardiac gene expression in ventricular myocytes. A paracrine mechanism for myocardial cell hypertrophy. J Biol Chem 265: 20555-20562, 1990.
8. Gandhi CR, Stephenson K and Olson MS, Endothelin, a potent peptide agonist in the liver. J Biol Chem 265: 17432-17435, 1990.
9. Kurihara Y, Kurihara H, Suzuki H, Kodama T, Maemura K, Nagai R, Oda H, Kuwaki T, Cao W, Kamada N, Jishage K, Ouchi Y, Azuma S, Toyoda Y, Ishikawa T, Kumada M and Yazaki Y, Elevated blood pressure and craniofacial abnormalities in mice deficient in endothelin-1. Nature 368: 703-710, 1994.
10. Baynash AG, Hosoda K, Giaid A, Richardson JA, Emoto N, Hammer RE and Yanagisawa M, Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons. Cell 79: 1277-1285, 1994.
11. Hosoda K, Hammer RE, Richardson JA, Baynash AG, Cheung JC, Giaid A and Yanagisawa M, Targeted and natural (piebaldlethal) mutations of endothelin-B receptor gene produce megacolon associated with spotted coat color in mice. Cell 79: 1267-1276, 1994.
12. Puffenberger EG, Hosoda K, Washington SS, Nakao K, deWit D, Yanagisawa M and Chakravarti A, A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease. Cell 79: 1257-1266, 1994.
13. Turner AJ, Endothelin-converting enzyme and other families of metalloendopeptidases. Biochem Soc Trans 21: 697-701, 1993.
14. Shimada K, Takahashi M and Tanzawa K, Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J Biol Chem 269: 18275-18278, 1994.
15. Xu D, Emoto N, Giaid A, Slaughter C, Kaw S, deWit D and Yanagisawa M, ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 78: 473-485, 1994.
16. Ikura T, Sawamura T, Shiraki T, Hosokawa H, Kido T, Hoshikawa H, Shimada K, Tanzawa K, Kobayashi S, Miwa S and Masaki T, cDNA cloning and expression of bovine endothelin converting enzyme. Biochem Biophys Res Commun 203: 1417-1422, 1994.
17. Schmidt M, Kröger B, Jacob E, Seulberger H, Subkowski T, Otter R, Meyer T, Schmalzing G and Hillen H, Molecular characterization of human and bovine endothelin converting enzyme (ECE-1). FEBS Lett 356: 238-243, 1994.
18. Simonson MS and Dunn MJ, The molecular mechanisms of cardiovascular and renal regulation by endothelin peptides. J Lab Clin Med 119: 622-639, 1992.
19. Kohan DE, Endothelins in the kidney: Physiology and pathophysiology. Am J Kidney Dis 22: 493-510, 1993.
20. Warner TD, Battistini D, Doherty AM and Corder R, Endothelin receptor antagonists: Actions and rationale for their development. Biochem Pharmacol 48: 625-635, 1994.
21. Laporte S, Denault J-B, D'Orléans-Juste P and Leduc R, Presence of furin mRNA in cultured bovine endothelial cells and possible involvement of furin in the processing of the endothelin precursor. J Cardiovasc Pharmacol 22 (Suppl 8): S7-S10, 1993.
22. Corder R, Harrison VJ, Khan N, Änggård EE and Vane JR, Effects of phosphoramidon in endothelial cell cultures on the endogenous synthesis of endothelin-1 and on conversion of exogenous big endothelin-1 to endothelin-1. J Cardiovasc Pharmacol 22 (Suppl 8): S73-S76, 1993.
23. Gui G, Xu D, Emoto N and Yanagisawa M, Intracellular localization of membrane-bound endothelin-converting enzyme from rat lung. J Cardiovasc Pharmacol 22 (Suppl 8): S53-S56, 1993.
24. Waxman L, Doshi KP, Gaul SL, Wang S, Bednar RA and Stern AM, Identification and characterization of endothelin converting activity from EAHY 926 cells: Evidence for the physiologically relevant human enzyme. Arch Biochem Biophys 308: 240-253, 1994.
25. Blache P, Kervran A, Le-Nguyen D and Bataille D, Miniglucagon production from glucagon: An extracellular processing of a hormone used as a prohormone, Biochimie 76: 295-299, 1994.
26. Medeiros MS and Turner AJ, Processing and metabolism of peptide-YY: Pivotal roles of dipeptidylpeptidase-IV, aminopeptidase-P and endopeptidase-24.11. Endocrinology 134: 2088-2094, 1994.
27. Medeiros MS and Turner AJ, Post-secretory processing of regulatory peptides: The pancreatic polypeptide family as a model example. Biochimie 76: 283-287, 1994.
28. Takaoka M, Miyata Y, Takenobu Y, Ikegawa R, Matsumura Y and Morimoto S, Mode of cleavage of pig big endothelin-1 by chymotrypsin. Production and degradation of mature endothelin-1. Biochem J 270: 541-544, 1990.
29. Wypij DM, Nichols JS, Novak PJ, Stacy DL, Berman J and Wiseman JS, Role of mast cell chymase in the extracellular processing of big endothelin-1 to endothelin-1 in the perfused rat lung. Biochem Pharmacol 43: 845-853, 1992.
30. Takaoka M, Takenobu Y, Miyata Y, Ikegawa R, Matsumura Y and Morimoto S, Pepsin, an aspartic protease, converts porcine big endothelin-1 to 21-residue endothelin. Biochem Biophys Res Commun 166: 436-442, 1990.
31. Matsumura Y, Ikegawa R, Takaoka M and Morimoto S, Conversion of porcine big endothelin to endothelin by an extract from the porcine aortic endothelial cells. Biochem Biophys Res Commun 167: 203-210, 1990.
32. Ikegawa R, Matsumura Y, Takaoka M and Morimoto S, Evidence for pepstatin-sensitive conversion of porcine big endothelin-1 to endothelin-1 by the endothelial cell extract. Biochem Biophys Res Commun 167: 860-866, 1990.
33. Sawamura T, Kimura S, Shinmi O, Sugita Y, Kobayashi M, Mitsui Y, Yanagisawa M, Goto K and Masaki T, Characterization of endothelin converting enzyme activities in soluble fraction of bovine cultured endothelial cells. Biochem Biophys Res Commun 169: 1138-1144, 1990.
34. Sawamura T, Kimura S, Shinmi O, Sugita Y, Yanagisawa M, Goto K and Masaki T, Purification and characterization of putative endothelin converting enzyme in bovine adrenal medulla: Evidence for a cathepsin D-like enzyme. Biochem Biophys Res Commun 168: 1230-1236, 1990.
35. Wu-Wong JR, Budzik GP, Devine EM and Opgenorth TJ, Characterization of endothelin converting enzyme in rat lung. Biochem Biophys Res Commun 171: 1291-1296, 1990.
36. Knap AK, Soriano A, Savage P, Del Grande D and Shetty SS, Identification of a novel aspartyl endothelin converting enzyme in porcine aortic endothelial cells. Biochem Mol Biol Int 29: 739-745, 1993.
37. Sawamura T, Shinmi O, Kishi N, Sugita Y, Yanagisawa M, Goto K, Masaki T and Kimura S, Analysis of big endothelin-1 digestion by cathepsin D. Biochem Biophys Res Commun 172: 883-889, 1990,
38. Takaoka M, Hukumori Y, Shiragami K, Ikegawa R, Matsumura Y and Morimoto S, Proteolytic processing of porcine big endothelin-1 catalyzed by cathepsin D. Biochem Biophys Res Commun 173: 1218-1223, 1990.
39. Lees WE, Kalinka S, Meech J, Capper SJ, Cook ND and Kay J, Generation of human endothelin by cathepsin E. FEBS Lett 273: 99-102, 1990.
40. Robinson PS, Lees WE, Kay J and Cook ND, Kinetic parameters for the generation of endothelin-1, -2 and -3 by human cathepsin E. Biochem J 284: 407-409, 1992.
41. Bird JE, Waldron TL, Little DK, Asaad MM, Dorso CR, DiDonato G and Norman JA, The effects of novel cathepsin E inhibitors on the big endothelin pressor response in conscious rats. Biochem Biophys Res Commun 182: 224-231, 1992.
42. Shields PP, Gonzales TA, Charles D, Gilligan JP and Stern W, Accumulation of pepstatin in cultured endothelial cells and its effect on endothelial processing. Biochem Biophys Res Commun 177: 1006-1012, 1991.
43. Deng Y, Savage P, Shetty SS, Martin LL and Jeng AY, Identification and partial purification of a thiol endothelin-converting enzyme from porcine aortic endothelial cells. J Biochem (Tokyo) 111: 346-351, 1992.
44. Knap AK and Wigg AM, A comparison of endothelin-converting enzyme activity from primary aortic endothelial cells with activities in cultured human cell lines. J Cardiovasc Pharmacol 22 (Suppl 8): S90-S93, 1993.
45. Suda H, Aoyagi T, Takeuchi T and Umezawa H, A thermolysin inhibitor produced by actinomycetes: Phosphoramidon. J Antibiotics (Tokyo) 26: 621-623, 1973.
46. Kenny AJ, Proteinases associated with cell membranes. In: Proteinases in Mammalian Cells and Tissues (Ed. Barrett AJ), pp. 393-444. Elsevier/North-Holland Biomedical Press, Amsterdam, 1977.
47. Roques BP, Fournié-Zaluski MC, Soroca E, Lecomte JM, Malfroy B, Llorens C and Schwartz JC, The enkephalinase inhibitor thiorphan shows anti-nociceptive activity in mice. Nature 288: 286-288, 1980.
48. Ikegawa R, Matsumura Y, Tsukahara Y, Takaoka M and Morimoto S, Phosphoramidon, a metalloproteinase inhibitor, suppresses the secretion of endothelin-1 from cultured endothelial cells by inhibiting a big endothelin-1 converting enzyme. Biochem Biophys Res Commun 171: 669-675, 1990.
49. Sawamura T, Kasuya Y, Matsushita Y, Suzuki N, Shinmi O, Kishi N, Sugita Y, Yanagisawa M, Goto K, Masaki T and Kimura S, Phosphoramidon inhibits the intracellular conversion of big endothelin-1 to endothelin-1 in cultured endothelial cells. Biochem Biophys Res Commun 174: 779-784, 1991.
50. Takada J, Okada K, Ikenaga T, Matsuyama K and Yano M, Phosphoramidon-sensitive endothelin converting enzyme in the cytosol of cultured bovine endothelial cells. Biochem Biophys Res Commun 176: 860-865, 1991.
51. Takaoka M, Shiragami K, Fujino K, Miki K, Miyake Y, Yasuda M, Wang GF, Hisaki K, Matsumura Y and Morimoto S, Phosphoramidon-sensitive endothelin converting enzyme in rat lung. Biochem Int 25: 697-704, 1991.
52. Shinyama H, Uchida T, Kido H, Hayashi K, Watanabe M, Matsumura Y, Ikegawa R, Takaoka M and Morimoto S, Phosphoramidon inhibits the conversion of intracisternally administered big endothelin-1 to endothelin-1. Biochem Biophys Res Commun 178: 24-30, 1991.
53. McMahon EG, Palomo MA, Moore WM, McDonald JF and Stern MK, Phosphoramidon blocks the presser activity of porcine big endothelin-1-(1-39) in vivo and conversion of big endothelin-1-(1-39) to endothelin-1-(1-21) in vitro. Proc Natl Acad Sci USA 88: 703-707, 1991.
54. Matsumura Y, Hisaki K, Takaoka M and Morimoto S, Phosphoramidon, a metalloproteinase inhibitor, suppresses the hypertensive effect of big endothelin-1. Eur J Pharmacol 185: 103-106, 1990.
55. Pollock DM and Opgenorth TJ, Evidence for metalloprotease involvement in the in vivo effects of big endothelin-1. Am J Physiol 261: R257-R263, 1991.
56. Kenny AJ, Stephenson SL and Turner AJ, Cell surface peptidases. In: Mammalian Ectoenzymes (Eds. Kenny AJ and Turner AJ), pp. 169-210. Elsevier, Amsterdam, 1987.
57. Turner AJ, Endopeptidase-24.11 and neuropeptide metabolism. In: Neuropeptides and Their Peptidases (Ed. Turner AJ), pp. 183-201. Ellis Horwood, Chichester, 1987.
58. Matsas R, Fulcher IS, Kenny AJ and Turner AJ, Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli. Proc Natl Acad Sci USA 80: 3111-3115, 1983.
59. Sokolovsky M, Galron R, Kloog Y, Bdolah A, Indig FE, Blumberg S and Fleminger G, Endothelins are more sensitive than sarafotoxins to neutral endopeptidase: Possible physiological significance. Proc Natl Acad Sci USA 87: 4702-4706, 1990.
60. Vijayaraghavan J, Scicli AG, Carretero OA, Slaughter C, Moomaw C and Hersh LB, The hydrolysis of endothelins by neutral endopeptidase 24.11 (enkephalinase). J Biol Chem 265: 14150-14155, 1990.
61. Abassi ZA, Golomb E, Bridenbaugh R and Keiser HR, Metabolism of endothelin-1 and big endothelin-1 by recombinant neutral endopeptidase EC 3.4.24.11. Br J Pharmacol 109: 1024-1028, 1993.
62. Murphy LJ, Corder R, Mallet AI and Turner AJ, Generation by the phosphoramidon-sensitive peptidases, endopeptidase-24.11 and thermolysin, of endothelin-1 and C-terminal fragment from big endothelin-1. Br J Pharmacol 113: 137-142, 1994.
63. Weaver LH, Kester WR and Matthews BW, A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substrates. J Mol Biol 114: 119-132, 1977.
64. Monzingo AF and Matthews BW, Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: A novel class of transition state analogues for zinc peptidases. Biochemistry 23: 5724-5729, 1984.
65. Murphy LJ, Greenhough KJ and Turner AJ, Processing and metabolism of endothelin peptides by porcine lung membranes. J Cardiovasc Pharmacol 22 (Suppl 8): S94-S97, 1993.
66. Corder R, Khan N and Harrison VJ, A simple method for isolating human endothelin converting enzyme free from contamination by neutral endopeptidase 24-11. Biochem Biophys Res Commun 207: 355-362, 1995.
67. Ohnaka K, Takayanagi R, Yamauchi T, Okazaki H, Ohashi M, Umeda F and Nawata H, Identification and characterization of endothelin converting activity in cultured bovine endothelial cells. Biochem Biophys Res Commun 168: 1128-1136, 1990.
68. Okada K, Miyazaki Y, Takada J, Matsuyama K, Yamaki T and Yano M, Conversion of big endothelin-1 by membrane-bound metalloendopeptidase in cultured bovine endothelial cells. Biochem Biophys Res Commun 171: 1192-1198, 1990.
69. Matsumura Y, Ikegawa R, Tsukahara Y, Takaoka M and Morimoto S, Conversion of big endothelin-1 to endothelin-1 by two types of metalloproteinases derived from porcine aortic endothelial cells. FEBS Lett 272: 166-170, 1990.
70. Matsumura Y, Ikegawa R, Tsukahara Y, Takaoka M and Morimoto S, N-Ethylmaleimide differentiates endothelin converting activity by two types of metalloproteinases derived from vascular endothelial cells. Biochem Biophys Res Commun 178: 531-538, 1991.
71. Devine EM, Marselle CA, Pederson TM, Wu-Wong JR, Budzik GP, Dillon TP and Opgenorth TJ, Identification of a neutral metalloendopeptidase endothelin converting enzyme from various cultured endothelial cell lines. FASEB J 5: A1417, 1991.
72. Hioki Y, Okada K, Ito H, Matsuyama K and Yano M, Endothelin converting enzyme of bovine carotid artery smooth muscle cells. Biochem Biophys Res Commun 174: 446-451, 1991.
73. Fukuroda T, Noguchi K, Tsuchida S, Nishikibe M, Ikemoto F, Okada K and Yano M, Inhibition of biological actions of big endothelin-1 by phosphoramidon. Biochem Biophys Res Commun 172: 390-395, 1990.
74. Sessa WC, Kaw S, Hecker M and Vane JR, The biosynthesis of endothelin-1 by human polymorphonuclear leukocytes. Biochem Biophys Res Commun 174: 613-618, 1991.
75. Takahashi M, Matsushita Y, Iijima Y and Tanzawa K, Purification and characterization of endothelin-converting enzyme from rat lung. J Biol Chem 268: 21394-21398, 1993.
76. Ohnaka K, Takayanagi R, Nishikawa M, Haji M and Nawata H, Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. J Biol Chem 268: 26759-26766, 1993.
77. Bordier C, Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 256: 1604-1607, 1981.
78. Turner AJ, Purification of membrane-associated proteins. Methods Mol Cell Biol 4: 205-211, 1994.
79. Hooper NM and Turner AJ, Ectoenzymes of the kidney microvillar membrane: Aminopeptidase P is anchored by a glycosylphosphatidylinositol moiety. FEBS Lett 229: 340-344, 1988.
80. Hooper NM, Low MG and Turner AJ, Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C. Biochem J 244: 465-469, 1987.
81. Edgell C-JS, McDonald CC and Graham JB, Permanent cell line expressing human factor VIII-related antigen established by hybridization. Proc Natl Acad Sci USA 80: 3734-3737, 1983.
82. Greenhough K, Walkden BJ, Murphy LJ, McLaren HE, Barnes K and Turner AJ, Membrane peptidase activity of a human endothelial cell line (EA.hy926). Biochem Soc Trans 22: 454S, 1994.
83. Saijonmaa O, Nyman T, Hohenthal U and Fyhrquist F, Endothelin-1 is expressed and released by a human endothelial hybrid line (EA.hy926). Biochem Biophys Res Commun 181: 529-536, 1991.
84. Takahashi M, Fukuda K, Shimada K, Barnes K, Turner AJ, Ikeda M, Koike H, Yamamoto Y and Tanzawa K, Localization of rat endothelin-converting enzyme to vascular endothelial cells and some secretory cells. Biochem J 311: 657-665, 1995.
85. Marchand P, Tang J and Bond JS, Membrane association and oligomeric organization of the α and β subunits of mouse meprin A. J Biol Chem 269: 15388-15393, 1994.
86. Gorbea CM, Beynon RJ and Bond JS, Meprins: Activation, subunit interactions, and anchoring. In: Mammalian Brush Border Membrane Proteins II (Eds. Lentze MJ, Naim HY and Grand RJ), pp. 89-97. Georg Thieme Verlag, Stuttgart, 1994.
87. Littlewood GM, Hooper NM and Turner AJ, Ectoenzymes of the kidney microvillar membrane. Affinity purification, characterization and localization of the phospholipase C-solubilized form of renal dipeptidase. Biochem J 257: 361-367, 1989.
88. Fulcher IS and Kenny AJ, Proteins of the kidney microvillar membrane. The amphipathic forms of endopeptidase purified from pig kidneys. Biochem J 211: 743-753, 1983.
89. Kenny AJ and Maroux S, Topology of microvillar membrane hydrolases of kidney and intestine. Physiol Rev 62: 91-128, 1982.
90. Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear G and Corvol P, Two putative active centers in human angiotensin-I converting enzyme revealed by molecular cloning. Proc Natl Acad Sci USA 85: 9386-9390, 1988.
91. Danielsen EM, Dimeric assembly of brush border enzymes. In: Mammalian Brush Border Membrane Proteins II (Eds. Lentze MJ, Naim HY and Grand RJ), pp. 236-239. Georg Thieme Verlag, Stuttgart, 1994.
92. Jongeneel CV, Bouvier J and Bairoch A, A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett 242: 211-214, 1989.
93. Jiang W and Bond JS, Families of metalloendopeptidases and their relationships. FEBS Lett 312: 110-114, 1992.
94. Rawlings ND and Barrett AJ, Evolutionary families of peptidases. Biochem J 290: 205-218, 1993.
95. Lee S, Zambas ED, Marsh WL and Redman CM, Molecular cloning and primary structure of Kell blood group protein. Proc Natl Acad Sci USA 88: 6353-6357, 1991.
96. King M-J, Blood group antigens on human erythrocytes - distribution, structure and possible functions. Biochim Biophys Acta 1197: 15-44, 1994.
97. Hunziker W, Spiess M, Semenza G and Lodish HF, The sucrase - isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell 46: 227-234, 1986.
98. Laperche Y, Bulle F, Aissani T, Chobert M-N, Aggerbeck M, Hanoune J and Guellaen G, Molecular cloning and nucleotide sequence of rat kidney γ-glutamyl transpeptidase cDNA. Proc Natl Acad Sci USA 83: 937-941, 1986.
99. Bateman RC Jr, Jackson D, Slaughter CA, Unnithan S, Chai YG, Moomaw C and Hersh LB, Identification of the active-site arginine in rat neutral endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of a glutamine 102 mutant. J Biol Chem 264: 6151-6157, 1989.
100. Beaumont A, Le Moual H, Boileau G, Crine P and Roques BP, Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4-24-11). J Biol Chem 266: 214-220, 1991.
101. Le Moual H, Devault A, Roques BP, Crine P and Boileau G, Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase 24.11. J Biol Chem 266: 15670-15674, 1991.
102. Connelly JC, Skidgel RA, Schulz WW, Johnson AR and Erdös EG, Neutral endopeptidase 24.11 in human neutrophils: Cleavage of chemotactic peptide. Proc Natl Acad Sci USA 82: 8737-8741, 1985.
103. LeTarte M, Vera S, Tran R, Addis JB, Omizuka RJ, Quackenbush EJ, Jongeneel CV and McInnis RR, Common acute lymphoblastic leukemia antigen is identical to neutral endopeptidase. J Exp Med 168: 1247-1253, 1988.
104. Shipp MA, Vijayaraghavan J, Schmidt EV, Masteller EL, D'Adamio L, Hersh LB and Reinherz EL, Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): Direct evidence by cDNA transfection analysis. Proc Natl Acad Sci USA 86: 297-301, 1989.
105. Turner AJ, Membrane peptidases of the nervous and immune systems. Adv Neuroimmunol 3: 163-170, 1993.
106. Howell S, Murray H, Scott CS, Turner AJ and Kenny AJ, A highly sensitive e.l.i.s.a. for endopeptidase-24.11, the common acute-lymphoblastic-leukaemia antigen (CALLA, CD-10), applicable to material of porcine and human origin. Biochem J 278: 417-421, 1991.
107. Okada K, Arai Y, Hata M, Matsuyama K and Yano M, Big endothelin-1 structure important for specific processing by endothelin-converting enzyme of bovine endothelial cells. Eur J Biochem 218: 493-498, 1993.
108. Fabbrini MS, Vitale A, Pedrazzini E, Nitti G, Zamai M, Tamburin M, Caiolfa VR, Patrono C and Benatti L, In vivo expression of mutant preproendothelins: Hierarchy of processing events but no strict requirement of Trp-Val at the processing site. Proc Natl Acad Sci USA 90: 3923-3927, 1993.
109. Fukami T, Hayama T, Amano Y, Nakamura Y, Arai Y, Matsuyama K, Yano M and Ishikawa K, Aminophosphonate endothelin converting enzyme inhibitors: Potency enhancing and selectivity improving modifications of phosphoramidon. Bioorg Med Chem Lett 4: 1257-1262, 1994.
110. De Lombaert S, Ghai RD, Jeng AY, Trapani AJ and Webb RL, Pharmacological profile of a non-peptidic dual inhibitor of neutral endopeptidase 24.11 and endothelin-converting enzyme. Biochem Biophys Res Commun 204: 407-412, 1994.
111. Corder R and Vane JR, Radioimmunoassay evidence that the presser effect of big endothelin-1 is due to local conversion to endothelin-1. Biochem Pharmacol 49: 375-380, 1995.
112. Hisaki K, Matsumura Y, Nishiguchi S, Fujita K, Takaoka M and Morimoto S, Endothelium independent pressor effect of big endothelin-1 and its inhibition by phosphoramidon in rat mesenteric artery. Eur J Pharmacol 241: 75-81, 1993.
113. Harrison VJ, Barnes K, Turner AJ, Wood E, Corder R and Vane JR, Identification of endothelin 1 and big endothelin 1 in secretory vesicles isolated from bovine aortic endothelial cells. Proc Natl Acad Sci USA 92: 6344-6348, 1995.
114. Emoto N and Yanagisawa M, Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J Biol Chem 270: 15262-15268, 1995.
115. Rothberg KG, Heuser JE, Donzell WC, Ying Y-S, Glenney JR and Anderson ROW, Caveolin, a protein component of caveolae membrane coats. Cell 68: 673-682, 1992.
116. Anderson RGW, Potocytosis of small molecules and ions by caveolae. Trends Cell Biol 3: 69-71, 1993.
117. Turner AJ, PIG-tailed membrane proteins. Essays Biochem 28: 113-127, 1994.
118. Ryan JW, Day AR, Schulz DR, Ryan US, Chung A, Marlborough DI and Dorer FE, Localization of angiotensin converting enzyme (kininase II). I. Preparation of antibody hemeoctapeptide conjugates. Tissue Cell 8: 111-124, 1976.
119. Chun M, Liyanage UK, Lisanti MP and Lodish HF, Signal transduction of a G protein-coupled receptor in caveolae: Co-localization of endothelin and its receptor with caveolin. Proc Natl Acad Sci USA 91: 11728-11732, 1994.
120. Chang W-J, Ying Y-s, Rothberg KG, Hooper NM, Turner AJ, Gambliel HA, De Gunzburg J, Mumby SM, Gilman AG and Anderson RGW, Purification and characterization of smooth muscle cell caveolae. J Cell Biol 126: 127-138, 1994.
121. Lisanti MP, Scherer PE, Vidugiriene J, Tang Z, Hermanowski-Vosatka A, Tu YH, Cook RF and Sargiacomo M, Characterization of caveolin-rich domains isolated from an endothelial rich source: Implications for human disease. J Cell Biol 126: 111-126, 1994.
122. Abassi ZA, Tate J, Golomb E and Keiser H, Role of neutral endopeptidase in the metabolism of endothelin. Hypertension 20: 89-95, 1992.
123. Isaac RE, Neuropeptide-degrading endopeptidase activity of locust (Schistocerca gregaria) synaptic membranes. Biochem J 255: 843-847, 1988.
124. Lamango NS and Isaac RE, Identification of an insect neuropeptide-degrading endopeptidase. Insect Biochem Mol Biol 22: 777-783, 1993.
125. Bawab W, Aloyz RS, Crine P, Roques BP and DesGroseillers L, Identification and characterization of a neutral endopeptidase activity in Aplysia californica. Biochem J 296: 459-465, 1993.
126. Shipp MA, Stefano GB, D'Adamio L, Switzer SN, Howard FD, Sinisterra J, Scharrer B and Reinherz EL, Down-regulation of enkephalin-mediated inflammatory responses by CD10/neutral endopeptidase 24.11. Nature 347: 394-396, 1990.
127. Clozel M, Breu V, Burri K, Cassal J-M, Fischli W, Gray GA, Hirth G, Löffler B-M, Müller M, Neidhart W and Ramuz H, Pathophysiological role of endothelin revealed by the first orally active endothelin receptor antagonist. Nature 365: 759-761, 1993.