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The Endothelin System and Endothelin-Converting Enzyme in the Brain: Molecular and Cellular Studies

Barnes, Kay, Turner, Anthony J.·1997·Neurochemical Research
DOI 10.1023/a:1022435111928
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Abstract

The biologically active vasoactive peptides, the endothelins (ETs), are generated from inactive intermediates, the big endothelins, by a unique processing event catalysed by the zinc metalloprotease, endothelin converting enzyme (ECE). In this overview we examine the actions of endothelins in the brain, and focus on the structure and cellular locations of ECE. The heterogeneous distribution in the brain of ET-1, ET-2, and ET-3 is discussed in relation to their hemodynamic, mitogenic and proliferative properties as well as their possible roles as neurotransmitters. The cellular and subcellular localization of ECE in neuronal and in glial cells is compared with that of other brain membrane metalloproteases, neutral endopeptidase-24.11 (neprilysin), angiotensin converting enzyme and aminopeptidase N, which all function in neuropeptide processing and metabolism Unlike these ectoenzymes, ECE exhibits a dual localisation in the cell, being present on the plasma membrane and also, in some instances, being concentrated in a perinuclear region. This differential localization may reflect distinct targeting of different ECE isoforms, ECE-1 alpha, ECE-1 beta, and ECE-2.

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  1. Yanagisawa, M., Kurihara, H., Kimura, S., Tomobe, Y., Kobayashi, Y., Mitsui, Y., Yazaki, Y., Goto, K., and Masaki, T. 1988. A novel potent, vasoconstrictor peptide produced by vascular endothelial cells. Nature. 332:411–415. · DOI
  2. Inoue, A., Yanagisawa, M., Kimura, S., Kasuya, Y., Miyauchi, T., Goto, K., and Masaki, T. 1989. The human endothelin family: Three structurally and pharmacologically distinct isopeptides predicted by three separate genes. Proc. Natl. Acad. Sci. USA. 86: 2863–2867. · DOI
  3. Warner, T. D., Battisti, B., Doherty, A. M., and Corder, R. 1994. Endothelin receptor antagonists: actions and rationale for their development. Biochem. Pharmacol. 48:625–35. · DOI
  4. Pollock, D. M., Keith, T. L., and Highsmith, R. F. 1995. Endothelin receptors and calcium signalling. FASEB J. 9:1196–1204. · DOI
  5. Kloog, Y., Ambar, I., Sokolovsky, M., Kochva, E., Wollberg, Z., and Bdolah, A. 1988. Sarafotoxin, a novel vasoconstrictor peptide: phosphoinositide hydrolysis in rat heart and brain. Science. 242: 268–70. · DOI
  6. Marsault, R., Vigne, P., and Frelin, C. 1990. The effect of extracellular calcium on the contractile action of endothelin. Biochem. Biophys. Res. Commun. 171:301–305. · DOI
  7. 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. 1994. Elevated blood pressure and craniofacial abnormalities in mice deficient in endothelin-1. Nature. 368:703–710. · DOI
  8. Baynash, A. G., Hosoda, K., Giaid, A., Richardson, J. A., Emoto, N., Hammer, R. E., and Yanagisawa, M. 1994. Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons. Cell. 79:1277–1285. · DOI
  9. Puffenberger, E. G., Hosoda, K., Washington, S. S., Nakao, K., de Wit, D., Yanagisawa, M., and Chakravarti, A. 1994. A missence mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease. Cell. 79:1257–1266. · DOI
  10. Siren, A. L., and Feuerstein, G. 1989. Hemodynamic effect of endothelin after systemic and central nervous system administration in the conscious rat. Neuropeptides. 14:231–236. · DOI
  11. Kobayashi, H., Hayushi, M., Kobayashi, S., Kabuto, M., Handa, Y., Kawano, H., and Ide. H. 1991. Cerebral vasospasm and vasoconstriction caused by endothelin. Neurosurgery. 28:673–679. · DOI
  12. MacCumber, M. W., Ross, C. A., and Snyder, S. H. 1990. Endothelin in brain: receptors, mitogenesis, and biosynthesis in glial cells. Proc. Natl. Acad. Sci. USA. 87:2359–2363. · DOI
  13. Fuxe, K., Tinner, B., Staines, W., Hemsen, A., Hersh, L., and Lundberg, J. M. 1991. Demonstration and nature of endothelin-3-like immunoreactivity in somatostatin and choline acetyltransferase-immunoreactive nerve cells of the neostriatum of the rat. Neurosci. Lett. 123:107–111. · DOI
  14. Giaid, A., Gibson, S. J., Herrero, M. T., Gentleman, S., Legon, S., Yanagisawa, M., Masaki, T., Ibrahim, N. B. N., Roberts, G. W., Rossi, M. L., and Polak, J. M. 1991. Topographical localisation of endothelin mRNA and peptide immunoreactivity in neurones of the human brain. Histochemistry. 95:303–314. · DOI
  15. Stanimirovic, D. B., Yamamoto, T., Uematsu, S., and Spatz, M. 1994. Endothelin-1 receptor binding and cellular signal transduction in cultured human brain endothelial cells. J. Neurochem. 62: 592–601. · DOI
  16. Ehrenreich, H., Kehrl, J. H., Anderson, R. W., Rieckmann, P., Vitkovic, L., Coligan, J. E., and Fauci, A. S. 1991. A vasoactive peptide, endothelin-3 is produced by and specifically binds to primary astrocytes. Brain Res. 538:54–58. · DOI
  17. Armstead, W. M., Mirro, R., Leffler, C. W., and Busija, D. W. 1989. Influence of endothelin on piglet cerebral microcirculation. Am. J. Physiol. 257:H707–H710.
  18. Shubeita, H. E., McDonough, P. M., Harris, A. N., Knowlton, K. U., Glembotski, C. C., Brown, J. H., and Chien, K. R. 1990. Endothelin induction of inositol phospholipid hydrolysis, sarcomare assembly, and cardiac gene expression in ventricular myocytes. A paracrine mechanism for myocardial cell hypertrophy. J. Biol. Chem. 265:20555–20562. · DOI
  19. Masaki, T., Kimura, S., Yanagisawa, M., and Goto, K. 1991. Molecular and cellular mechanisms of endothelin regulation. Implications for vascular function. Circulation. 84:1457–1468. · DOI
  20. Vanhoutte, P. M. 1994. A matter of life and breath. Nature. 368: 693–694. · DOI
  21. Zhang, M., and Olsson, Y. 1995. Reactions of astrocytes and microglial cells around hematogenous metastases of the human brain. Expression of endothelin-like immunoreactivity in reactive astrocytes and activation of microglial cells. J. Neurol. Sci. 134:26–32. · DOI
  22. Zhang, W. W., Badonic, T., Hoog, A., Jiang, M. H., Ma, K. C., Nie, X. J., and Olsson, Y. 1994. Astrocytes in Alzheimer's disease express immunoreactivity to the vaso-constrictor endothelin 1. J. Neurol. Sci. 122:90–96. · DOI
  23. Giaid, A., Gibson, S. J., Ibrahim, N. B. N., Legon, S., Bloom, S. R., Yanagisawa, M., Masaki, T., Varndell, I. M., and Polak, J. M. 1989. Endothelin 1, an endothelin-derived peptide, is expressed in neurons of the human spinal cord and dorsal root ganglia. Proc. Natl. Acad. Sci. USA. 86:7634–7638. · DOI
  24. Yoshizawa, T., Kimura, S., Kamazawa, I., Uchiyama, Y., Yanagisawa, M., and Masaki, T. 1989. Endothelin localizes in the dorsal horn and acts on the spinal neurones: possible involvement of dihydropyridine-sensitive calcium channels and substance P release. Neurosci. Lett. 102:179–184. · DOI
  25. Koyama, Y., and Baba, A. 1994. Endothelins are extracellular signals modulating cytoskeletal actin organisation in rat cultured astrocytes. Neuroscience. 61:1007–1016. · DOI
  26. Laporte, S., Denault, J.-B., D'Orleans-Juste, P., and Leduc, R. 1993. Presence of furin in 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. · DOI
  27. Turner, A. J., and Murphy, L. J. 1996. Molecular pharmacology of endothelin-converting enzymes. Biochem. Pharmacol. 51:91–102. · DOI
  28. Takahashi, M., Matsushita, Y., Iijima, Y., and Tanzawa, K. 1993. Purification and characterization of endothelin-converting enzyme from rat lung. J. Biol. Chem. 268:21394–21398. · DOI
  29. Ohnaka, K., Takayanagi, R., Nishikawa, M., Haji, M., and Nawata, H. 1993. Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. J. Biol. Chem. 268:26759–26766. · DOI
  30. Xu, D., Emoto, N., Giaid, A., Slaughter, C., Kaw, S., deWit, D., and Yanagisawa, M. 1994. ECE-1: a membrane-bound metallo-protease that catalyzes the proteolytic activation of big endothelin-1. Cell. 78:473–485. · DOI
  31. Shimada, K., Takahashi, M., and Tanzawa, K. 1994. Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J. Biol. Chem. 269:18275–18278. · DOI
  32. Schmidt, M., Kroger, B., Jacob, E., Seulberger, H., Subkowski, T., Otter, R., Meyer, T., Schmalzing, G., and Hillen, H. 1994. Molecular characterization of human and bovine endothelin-converting enzyme (ECE-1). FEBS Lett. 356:238–243. · DOI
  33. Valdenaire, O., Rohrbacher, E., and Mattei, M.-G. 1995. Organisation of the gene encoding the human endothelin-converting enzyme (ECE-1). J. Biol. Chem. 270:29794–29798. · DOI
  34. Albertin, G., Rossi, G. P., Majone, F., Tiso, N., Mattara, A., Danieli, G. A., Pessina, A. C., and Paku, G. 1996. Fine mapping of the human endothelin-converting enzyme gene by fluorescent in situ hybridisation and radiation hybrids. Biochem. Biophys. Res. Commun. 221:682–687. · DOI
  35. Shimada, K., Takahashi, M., Ikeda, M., and Tanzawa, K. 1995. Identification and characterisation of two isoforms of an endothelin-converting enzyme-1. FEBS Lett. 371:140–144. · DOI
  36. Emoto, N., Xie, J., and Yanagisawa, M. 1996. Intracellular and cell surface isoforms of endothelin-converting enzyme-1 generated by tissue specific alternative splicing. Circulation 94:586.
  37. Shimada, K., Takahashi, M., Turner, A. J., and Tanzawa, K. 1996. Rat endothelin-converting enzyme-1 forms a dimer through Cys412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11. Biochem. J. 315:863–867. · DOI
  38. Emoto, N., and Yanagisawa, M. 1995. Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J. Biol. Chem. 250:15262–15268. · DOI
  39. Turner, A. J., and Barnes, K. 1994. Neuropeptidases: candidate enzymes and techniques for study. Biochem. Soc. Trans. 22:122–126. · DOI
  40. Turner, A. J., and Barnes, K. 1995. in Peptidases and Neuropeptide Processing, vol. 23, pp. 344–362, Academic Press. · DOI
  41. Roques, B. P., Noble, F., Dauge, V., Fournie-Zaluski, M.-C., and Beaumont, A. 1993. Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. Pharmacol. Rev. 45:87–146. · DOI
  42. Turner, A. J., Hooper, N. M., and Kenny, A. J. 1987. In Mammalian Ectoenzymes, vol. 14 (Kenny, A. J. and Turner., A. J., eds.), pp. 211–248, Elsevier, Amsterdam.
  43. Barnes, K., Doherty, S., and Turner, A. J. 1995. Endopeptidase-24.11 is the integral membrane peptidase initiating degradation of somatostatin in the hippocampus. J. Neurochem. 64:1826–1832. · DOI
  44. Matsas, R., Kenny, A. J., and Turner, A. J. 1986. An immunohistochemical study of endopeptidase-24.11 (enkephalinase) in the pig nervous system. Neuroscience. 18:991–1012. · DOI
  45. Waksman, G., Hamel, E., Delay-Goyet, P., and Roques, B. P. 1986. Neuronal localisation of the neutral endopeptidase ‘enkephalinase’ in rat brain revealed by lesions and auto radiography. EMBO J. 5:3163–3166. · DOI
  46. Marcel, D., Pollard, H., Verroust, P., Schwartz, J. C., and Beaudet, A. 1990. Electron microscopic localisation of immunoreactive enkephalinase (EC 3.4.24.11) in the neostriatum of the rat. J. Neurosci. 10:2804–2817. · DOI
  47. Barnes, K., Matsas, R., Hooper, N. M., Turner, A. J., and Kenny, A. J. 1988. Endopeptidase-24.11 is striosomally ordered in pig brain and, in contrast to aminopeptidase N and peptidyl dipeptidase A (‘angiotensin converting enzyme’), is a marker for a set of striatal efferent fibres. Neuroscience. 27:799–817. · DOI
  48. Barnes, K., Turner, A. J., and Kenny, A. J. 1988. Electronmi-croscopic immunocytochemistry of pig brain shows that endopeptidase-24.11 is localized in neuronal membranes. Neurosci. Lett. 94:64–69. · DOI
  49. Barnes, K., Turner, A. J., and Kenny, A. J. 1992. Membrane localisation of endopeptidase-24.11 and peptidyl dipeptidase A (angiotensin converting enzyme) in the pig brain: a study using sub-cellular fractionation and electron microscopic immunocytochemistry. J. Neurochem. 58:2088–2096. · DOI
  50. Barnes, K., Turner, A. J., and Kenny, A. J. 1993. An immunoelectron microscopic study of pig substantia nigra shows co-localization of endopeptidase-24.11 with substance P. Neuroscience. 53:1073–1082. · DOI
  51. Waksman, G., Hamel, E., Fournie-Zaluski, M.-C., and Roques, B. P. 1986. Autoradiographic comparison of the distribution of the neutral endopeptidase ‘enkephalinase’ and of m and d opioid receptors in rat brain. Proc. Natl. Acad. Sci. USA. 83:1523–1527. · DOI
  52. Defendini, R., Zimmerman, E. A., Weare, J. A., Alhenc-Gelas, F., and Erdos, E. G. 1983. Angiotensin converting enzyme in epithelial and neuroepithelial cells. Neuroendocrinol. 37:32–40. · DOI
  53. Strittmatter, S. M., Lo, M. M. S., Javitch, J. A., and Snyder, S. H. 1984. Autoradiographic visualisation of angiotensin converting enzyme in rat brain with [3H] captopril: localisation to a striatonigral pathway. Proc. Natl. Acad. Sci. USA. 81:1599–1603. · DOI
  54. Pickel, V. M., Chan, J., and Ganten, D. 1986. Dual peroxidase and colloidal gold-labelling study of angiotensin converting enzyme and angiotensin-like immunoreactivity in the rat subfornical organ. J. Neurosci. 6:2457–2469. · DOI
  55. Erdos, E. G., and Skidgel, R. A. 1987. The angiotensin I converting enzyme. Lab. Invest. 56:345–348.
  56. Brownfield, M. S., Reid, I. A., Ganten, D., and Ganong, W. F. 1982. Differential distribution of immunoreactive angiotensin and angiotensin-converting enzyme in rat brain. Neuroscience. 7: 1759–1769. · DOI
  57. Williams, T. A., Hooper, N. M., and Turner, A. J. 1991. Characterization of neuronal and endothelial forms of angiotensin converting enzyme in pig brain. J. Neurochem. 57:193–199. · DOI
  58. Solhonne, B., Gros, C., Pollard, H., and Schwartz, J.-C. 1987. Major localisation of aminopeptidases M in rat brain microvessels. Neuroscience. 22:225–232. · DOI
  59. Hersh, L. B., Aboukhair, N., and Watson, S. 1987. Immunohistochemical localisation of aminopeptidase M in rat brain and periphery: relationship of enzyme localisation and enkephalin metabolism. Peptides. 8:523–532. · DOI
  60. Schnabel, R., Bernstein, H.-G., Luppa, H., Lojda, Z., and Barth, A. 1992. Aminopeptidase in the circumventricular organs of the mouse brain: a histochemical study. Neuroscience 47:431–438. · DOI
  61. Barnes, K., Kenny, A. J., and Turner, A. J. 1994. Localization of aminopeptidase N and dipeptidyl peptidase IV in pig striatum and in neuronal and glial cell cultures. Eur. J. Neurosci. 6:531–537. · DOI
  62. Kunz, J., Krause, D., Kremer, M., and Dermietzel, R. 1994. The 140-kDa protein of blood-brain barrier-associated pericytes is identical to aminopeptidase. N. J. Neurochem. 62:2375–2386. · DOI
  63. Ikura, T., Sawamura, T., Shiraki, T., Hosokawa, H., Kido, T., Hoshikawa, H., Shimada, K., Tanzawa, K., Kobayashi, S., Miwa, S., and Masaki, T. 1994. cDNA cloning and expression of bovine endothelin-converting enzyme. Biochem. Biophys. Res. Commun. 203:1417–1422. · DOI
  64. Warner, T. D., Budzik, G. P., Matsumoto, T., Mitchell, J. A., Forstermann, U., and Murad, F. 1992. Regional differences in endothelin-converting enzyme activity in rat brain: inhibition by phosphoramidon and EDTA. B. J. Pharmacol. 106:968–952.
  65. Warner, T. D., Mitchell, J. A., D'Orleans-Juste, P., Ishii, K., Forstermann, U., and Murad, F. 1992. Characterisation of endothelin-converting enzyme from endothelial cells and rat brain: detection of the formation of biologically active endothelin-1 by rapid bioassay. Mol. Pharmacol. 41:399–403. · DOI
  66. Deschepper, C. F., Houweling, A. D., and Picard, S. 1995. The membranes of cultured rat brain astrocytes contain endothelin-converting enzyme activity. Eur. J. Pharmacol. 275:61–66. · DOI
  67. Barnes, K., Walkden, B. J., Wilkinson, T. C., and Turner, A. J. 1997. Expression of endothelin-converting enzyme in both neuroblastoma and glial cell lines and its localisation in rat hippocampus. J. Neurochem. 68: In press. · DOI
  68. Takahashi, M., Fukuda, K., Shimada, K., Barnes, K., Turner, A. J., Ikeda, M., Koike, H., Yamamoto, Y., and Tanzawa, K. 1995. Localization of rat endothelin-converting enzyme to vascular endothelial cells and some secretory cells. Biochem. J. 311:657–665. · DOI
  69. Barnes, K., Shimada, K., Takahashi, M., Tanzawa, K., and Turner, A. J. 1996. Metallopeptidase inhibitors induce an up-regulation of endothelin-converting enzyme levels and its redistribution from the plasma membrane to an intracellular compartment. J. Cell Sci. 109:919–928. · DOI
  70. Waxman, L., Doshi, K. P., Gaul, S. L., Wang, S., Bednar, R. A., and Stern, A. M. 1994. Identification and characterisation of endothelin-converting activity from EAHY 926 cells: evidence for the physiologically relevant human enzyme. Arch. Biochem. Biophys. 308:240–253. · DOI
  71. Corder, R., Khan, N., and Harrison, V. J. 1995. A simple method for isolating human endothelin converting enzyme free from contamination by neutral endopeptidase-24.11. Biochem. Biophys. Res. Commun. 207:377–362. · DOI
  72. Gautam, M., Noakes, P. G., Mudd, J., Nichol, M., Chu, G. C., Sanes, J. R., and Merlie, J. P. 1995. Failure of postsynaptic specialisation to develop at neuromuscular junctions of rapsyn-deficient mice. Nature 377:232–236. · DOI
  73. Gui, G., Xu, D., Emoto, N., and Yanagisawa, M. 1993. Intracellular localisation of membrane-bound endothelin-converting enzymes from rat lung. J. Cardiovasc. Pharmacol. 22(Suppl. 8): S53–56. · DOI
  74. Harrison, V. J., Barnes, K., Turner, A. J., Wood, E., Corder, R., and Vane, J. R. 1995. 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. · DOI

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Authors
Barnes, K., & Turner, A. J.
Venue
Neurochemical Research
Publisher
Springer Science and Business Media LLC
Published
1997-08
Volume
22
Issue
8
Pages
1033-1040
ISSN
  • 0364-3190
  • 1573-6903
DOI
10.1023/a:1022435111928
Cited by
45
References
0
Language
en
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