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Journal articles on the topic 'Endothelin converting enzyme 1'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Cottrell, Graeme S., Benjamin E. Padilla, Silvia Amadesi, Daniel P. Poole, Jane E. Murphy, Markus Hardt, Dirk Roosterman, Martin Steinhoff, and Nigel W. Bunnett. "Endosomal Endothelin-converting Enzyme-1." Journal of Biological Chemistry 284, no. 33 (June 16, 2009): 22411–25. http://dx.doi.org/10.1074/jbc.m109.026674.

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2

Barnes, K., K. Shimada, M. Takahashi, K. Tanzawa, and A. J. Turner. "Metallopeptidase inhibitors induce an up-regulation of endothelin-converting enzyme levels and its redistribution from the plasma membrane to an intracellular compartment." Journal of Cell Science 109, no. 5 (May 1, 1996): 919–28. http://dx.doi.org/10.1242/jcs.109.5.919.

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Endothelin-converting enzyme is a phosphoramidon-sensitive membrane metallopeptidase that catalyses the final step in biosynthesis of the potent vasoactive endothelin peptides. Immunomagnetic separation technology and immunohistochemistry have been used to demonstrate the co-localisation of endothelin-converting enzyme with the established ectoenzyme, aminopeptidase N, on the surface of endothelial cells. Unlike aminopeptidase N, however, endothelin-converting enzyme is seen to associate in clusters on the plasma membrane which can be distinguished from caveolae both biochemically and immunologically. Pre-treatment of endothelial cells with the metallopeptidase inhibitors phosphoramidon or thiorphan in the range 0.01-100 microM produced a dose-dependent increase in the levels of endothelin-converting enzyme protein and its accumulation in an intracellular compartment. No corresponding change in the levels of endothelin-converting enzyme-1 mRNA was detected under these conditions, nor in the levels of the closely related metalloenzyme, endopeptidase-24.11. The phosphoramidon and thiorphan-dependent increase is not due to direct inhibition of endothelin-converting enzyme not endopeptidase-24.11 but, rather, to an inhibition of the selective turnover of endothelin-converting enzyme protein.

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3

Wu, Ching-Fang, Ching-Tai Lee, Yao-Hung Kuo, Tzu-Haw Chen, Chi-Yang Chang, I.-Wei Chang, and Wen-Lun Wang. "High endothelin-converting enzyme-1 expression independently predicts poor survival of patients with esophageal squamous cell carcinoma." Tumor Biology 39, no. 9 (September 2017): 101042831772592. http://dx.doi.org/10.1177/1010428317725922.

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Patients with esophageal squamous cell carcinoma have poor survival and high recurrence rate, thus an effective prognostic biomarker is needed. Endothelin-converting enzyme-1 is responsible for biosynthesis of endothelin-1, which promotes growth and invasion of human cancers. The role of endothelin-converting enzyme-1 in esophageal squamous cell carcinoma is still unknown. Therefore, this study investigated the significance of endothelin-converting enzyme-1 expression in esophageal squamous cell carcinoma clinically. We enrolled patients with esophageal squamous cell carcinoma who provided pretreated tumor tissues. Tumor endothelin-converting enzyme-1 expression was evaluated by immunohistochemistry and was defined as either low or high expression. Then we evaluated whether tumor endothelin-converting enzyme-1 expression had any association with clinicopathological findings or predicted survival of patients with esophageal squamous cell carcinoma. Overall, 54 of 99 patients with esophageal squamous cell carcinoma had high tumor endothelin-converting enzyme-1 expression, which was significantly associated with lymph node metastasis ( p = 0.04). In addition, tumor endothelin-converting enzyme-1 expression independently predicted survival of patients with esophageal squamous cell carcinoma, and the 5-year survival was poorer in patients with high tumor endothelin-converting enzyme-1 expression ( p = 0.016). Among patients with locally advanced and potentially resectable esophageal squamous cell carcinoma (stage II and III), 5-year survival was poorer with high tumor endothelin-converting enzyme-1 expression ( p = 0.003). High tumor endothelin-converting enzyme-1 expression also significantly predicted poorer survival of patients in this population. In patients with esophageal squamous cell carcinoma, high tumor endothelin-converting enzyme-1 expression might indicate high tumor invasive property. Therefore, tumor endothelin-converting enzyme-1 expression could be a good biomarker to identify patients with worse survival and higher risks of recurrence, who might benefit from the treatment by endothelin-converting enzyme-1 inhibitor.

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4

D'Orléans-Juste, P., M. Plante, J. C. Honoré, E. Carrier, and J. Labonté. "Synthesis and degradation of endothelin-1." Canadian Journal of Physiology and Pharmacology 81, no. 6 (June 1, 2003): 503–10. http://dx.doi.org/10.1139/y03-032.

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The endothelin-converting enzyme (ECE) is the main enzyme responsible for the genesis of the potent pressor peptide endothelin-1 (ET-1). It is suggested that the ECE is pivotal in the genesis of ET-1, considering that the knockout of both genes generates the same lethal developments during the embryonic stage. Several isoforms of the ECE have been disclosed, namely ECE-1, ECE-2, and ECE-3. Within each of the first two groups, several sub-isoforms derived through splicing of single genes have also been identified. In this review, the characteristics of each sub-isoform for ECE-1 and 2 will be discussed. It is important to mention that the ECE is, however, not the sole enzyme involved in the genesis of endothelins. Indeed, other moieties, such as chymase and matrix metalloproteinase II, have been suggested to be involved in the production of ET intermediates, such as ET-1 (131) and ET-1 (132), respectively. Other enzymes, such as the neutral endopeptidase 2411, is curiously not only involved in the degradation and inactivation of ET-1, but is also responsible for the final production of the peptide via the hydrolysis of ET-1 (131). In this review, we will attempt to summarize, through the above-mentioned characteristics, the current wisdom on the role of these different enzymes in the genesis and termination of effect of the most potent pressor peptide reported to date.Key words: endothelin converting enzyme, endothelin-1, isoforms, human, inhibitors, chymase, ET-1 (131).

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5

Pupilli, C., P. Romagnani, L. Lasagni, F. Bellini, N. Misciglia, N. Emoto, M. Yanagisawa, M. Rizzo, M. Mannelli, and M. Serio. "Localization of endothelin-converting enzyme-1 in human kidney." American Journal of Physiology-Renal Physiology 273, no. 5 (November 1, 1997): F749—F756. http://dx.doi.org/10.1152/ajprenal.1997.273.5.f749.

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The distribution of endothelin-converting enzyme-1 (ECE-1) mRNA and protein was investigated in human kidney excised because of renal tumors. ECE-1 immunoreactivity was detected by immunohistochemistry throughout the different areas of the kidney in the vascular and tubular structures. In the cortex, ECE-1 immunostaining was present in the endothelial surface of arcuate and interlobular arteries and in arterioles. Weak specific immunoreactivity was present over some proximal and distal tubules. Few endothelial glomerular cells contained ECE-1 protein. In the medulla, ECE-1 immunoreactivity was observed in the vasa recta bundles and capillaries. ECE-1 immunostaining was also detected in the outer and inner medullary collecting ducts and thin limbs of Henle’s loops. Immunohistochemical detection of the von Willebrand factor on adjacent sections confirmed the endothelial nature of the vascular cells that exhibited ECE-1 immunostaining. The distribution patterns of ECE-1 mRNA, investigated by in situ hybridization, appeared similar to that obtained by immunohistochemistry in the cortical and medullary vasculature and in different portions of the nephron. Northern blot and densitometric analyses demonstrated that ECE-1 mRNA levels were quantitatively similar in both the renal cortex and medulla. These results demonstrate that vascular endothelial and tubular epithelial cells in the cortex and medulla of the human kidney synthesize ECE-1, which, in turn, may play an important role in regulating endothelin production in physiological and pathological conditions.

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6

Jafri, Farahdiba, and Adviye Ergul. "Nuclear Localization of Endothelin-Converting Enzyme-1." Arteriosclerosis, Thrombosis, and Vascular Biology 23, no. 12 (December 2003): 2192–96. http://dx.doi.org/10.1161/01.atv.0000099787.21778.55.

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7

Tapia, Julio C., and Ignacio Niechi. "Endothelin-converting enzyme-1 in cancer aggressiveness." Cancer Letters 452 (June 2019): 152–57. http://dx.doi.org/10.1016/j.canlet.2019.03.033.

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8

Kuruppu, Sanjaya, and A. Ian Smith. "Endothelin Converting Enzyme-1 phosphorylation and trafficking." FEBS Letters 586, no. 16 (June 21, 2012): 2212–17. http://dx.doi.org/10.1016/j.febslet.2012.06.020.

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9

Lin, J., and C. Wei. "Enhancement of Endothelin Converting Enzyme and Endothelin Receptor Subtypes in Human Myocardium with Congestive Heart Failure." Microscopy and Microanalysis 6, S2 (August 2000): 608–9. http://dx.doi.org/10.1017/s1431927600035534.

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Endothelin-1 (ET-1) is a potent endothelial cell-drived vasoconstrictive peptide which is increased in congestive heart failure (CHF). ET-1 is converted from its precursor big ET-1 by activation of endothelin converting enzyme (ECE). ET-1 binding to ET-A receptor in vascular smooth muscle cells stimulates vasoconstriction and binding to ET-B receptor in vascular endothelial cells mediates vasodilation. In previous studies, we and others demonstrated that plasma ET-1 was significantly increased in congestive heart failure. However, the presentation and localization of endothelin converting enzyme and endothelin receptors (ET-A and ET-B) in human cardiac tissue with and without heart failure remain unclear. Therefore, the current study was designed to investigate the expression and localization of endothelin receptors and endothelin converting enzyme in human myocardium in the absence or presence of congestive heart failure.Human atrial tissues (n=6) were obtained from normal subjects and end-stage CHF patients during cardiac transplantation. The expression of ECE, ET-A and ET-B were determined by immunohistochemical staining (IHCS).

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10

Kido-Nakahara, Makiko, Jörg Buddenkotte, Cordula Kempkes, Akihiko Ikoma, Ferda Cevikbas, Tasuku Akiyama, Frank Nunes, et al. "Neural peptidase endothelin-converting enzyme 1 regulates endothelin 1–induced pruritus." Journal of Clinical Investigation 124, no. 6 (May 8, 2014): 2683–95. http://dx.doi.org/10.1172/jci67323.

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11

Naomi, Shojiro, Taisuke Iwaoka, Tumba Disashi, Junnosuke Inoue, Yoshie Kanesaka, Hiroshi Tokunaga, and Kimio Tomita. "Endothelin-1 Inhibits Endothelin-Converting Enzyme-1 Expression in Cultured Rat Pulmonary Endothelial Cells." Circulation 97, no. 3 (January 27, 1998): 234–36. http://dx.doi.org/10.1161/01.cir.97.3.234.

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12

Kuruppu, Sanjaya, Shane Reeve, and A. Ian Smith. "Characterisation of endothelin converting enzyme-1 shedding from endothelial cells." FEBS Letters 581, no. 23 (August 22, 2007): 4501–6. http://dx.doi.org/10.1016/j.febslet.2007.08.028.

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13

Zorrilla, L. M., R. Sriperumbudur, and J. E. Gadsby. "Endothelin-1, endothelin converting enzyme-1 and endothelin receptors in the porcine corpus luteum." Domestic Animal Endocrinology 38, no. 2 (February 2010): 75–85. http://dx.doi.org/10.1016/j.domaniend.2009.08.006.

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14

Subkowski, Thomas, Heinz Hillen, Burkhard Kröger, and Martin Schmidt. "Monoclonal Antibodies Against Human Endothelin-Converting Enzyme-1." Journal of Immunoassay 19, no. 2-3 (May 1998): 75–93. http://dx.doi.org/10.1080/01971529808005474.

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15

Roosterman, Dirk, Cordula Kempkes, Graeme S. Cottrell, Benjamin E. Padilla, Nigel W. Bunnett, Christoph W. Turck, and Martin Steinhoff. "Endothelin-Converting Enzyme-1 Degrades Internalized Somatostatin-14." Endocrinology 149, no. 5 (February 14, 2008): 2200–2207. http://dx.doi.org/10.1210/en.2007-1628.

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Agonist-induced internalization of somatostatin receptors (ssts) determines subsequent cellular responsiveness to peptide agonists and influences sst receptor scintigraphy. To investigate sst2A trafficking, rat sst2A tagged with epitope was expressed in human embryonic kidney cells and tracked by antibody labeling. Confocal microscopical analysis revealed that stimulation with sst and octreotide induced internalization of sst2A. Internalized sst2A remained sequestrated within early endosomes, and 60 min after stimulation, internalized sst2A still colocalized with β-arrestin1-enhanced green fluorescence protein (EGFP), endothelin-converting enzyme-1 (ECE-1), and rab5a. Internalized 125I-Tyr11-SST-14 was rapidly hydrolyzed by endosomal endopeptidases, with radioactive metabolites being released from the cell. Internalized 125I-Tyr1-octreotide accumulated as an intact peptide and was released from the cell as an intact peptide ligand. We have identified ECE-1 as one of the endopeptidases responsible for inactivation of internalized SST-14. ECE-1-mediated cleavage of SST-14 was inhibited by the specific ECE-1 inhibitor, SM-19712, and by preventing acidification of endosomes using bafilomycin A1. ECE-1 cleaved SST-14 but not octreotide in an acidic environment. The metallopeptidases angiotensin-1 converting enzyme and ECE-2 did not hydrolyze SST-14 or octreotide. Our results show for the first time that stimulation with SST-14 and octreotide induced sequestration of sst2A into early endosomes and that endocytosed SST-14 is degraded by endopeptidases located in early endosomes. Furthermore, octreotide was not degraded by endosomal peptidases and was released as an intact peptide. This mechanism may explain functional differences between octreotide and SST-14 after sst2A stimulation. Moreover, further investigation of endopeptidase-regulated trafficking of neuropeptides may result in novel concepts of neuropeptide receptor inactivation in cancer diagnosis.

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16

Arun, Banu, Gokhan Kilic, Raheela Ashfaq, Hossein M. Saboorian, and Tunc Gokaslan. "Endothelin Converting Enzyme-1 Expression in Endometrial Adenocarcinomas." Cancer Investigation 19, no. 8 (January 2001): 779–82. http://dx.doi.org/10.1081/cnv-100107738.

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17

Kinjo, M., J. Papadimitriou, C. Drachenberg, M. R. Weir, and C. Wei. "Expression and Localization of Renal Endothelin-1, Endotehlin Receptors and Endothelin Converting Enzyme in Human Renal Biopsy with Rejection after Kidney Transplantation." Microscopy and Microanalysis 6, S2 (August 2000): 610–11. http://dx.doi.org/10.1017/s1431927600035546.

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Endothelin (ET-1) is a potent renal and systemic vasoconstrictor and sodium regulating peptide. Endothelin synthesis in the kidney have been reported in glomerulus endothelial, epithelial and mesangial cells as well as in inner medullary collecting duct. Factors stimulating the production of endothelin include shear stress, hypoxia, vasoactive agents and cytokines. Endothelin binding to ET-A receptor in vascular smooth muscle cells stimulates vasoconstriction.Renal graft rejection is a major problem after kidney transplantation with severe renal damage and renal vasoconstriction. We hypothesized that renal tissue level of endothelin-1, endothelin receptors and endothelin converting enzyme (ECE) may increase in renal tissue with rejection after kidney transplantation. Therefore, the current study was designed to determine the endothelin-1 and endothelin receptors (ET-A and ET-B) as well as endothelin converting enzyme level by immunohistochemical staining (IHCS) in human renal tissue with rejection after kidney transplantation.

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18

Nakagomi, Saya, Sumiko Kiryu-Seo, and Hiroshi Kiyama. "Endothelins, endothelin converting enzyme and endothelin receptors mRNA localizations in the rat brain." Neuroscience Research 31 (January 1998): S315. http://dx.doi.org/10.1016/s0168-0102(98)82437-1.

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19

Takayanagi, Ryoichi, Wei Liu, Takeshi Ito, Keizo Ohnaka, and Hajime Nawata. "Big Endothelin Analogues with Inhibitory Activity on Endothelin-Converting Enzyme-1." Journal of Cardiovascular Pharmacology 31 (1998): S62—S63. http://dx.doi.org/10.1097/00005344-199800001-00020.

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20

Corder, Roger, Noorafza Q. Khan, Vanessa J. Harrison, Elizabeth G. Wood, Delphine M. Lees, and Stewart Barker. "Relationship Between Soluble Intracellular Endothelin-Converting Enzyme and Endothelin-1 Synthesis." Journal of Cardiovascular Pharmacology 36 (2000): S19—S21. http://dx.doi.org/10.1097/00005344-200036001-00008.

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21

Corder, Roger, Noorafza Q. Khan, Vanessa J. Harrison, Elizabeth G. Wood, Delphine M. Lees, and Stewart Barker. "Relationship Between Soluble Intracellular Endothelin-Converting Enzyme and Endothelin-1 Synthesis." Journal of Cardiovascular Pharmacology 36, Supplement 1 (2000): S19—S21. http://dx.doi.org/10.1097/00005344-200036051-00008.

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22

SCHWEIZER, Anja, Olivier VALDENAIRE, Peter NELBÖCK, Ulrich DEUSCHLE, Jean-Baptiste DUMAS MILNE EDWARDS, Jürgen G. STUMPF, and Bernd-Michael LÖFFLER. "Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations." Biochemical Journal 328, no. 3 (December 15, 1997): 871–77. http://dx.doi.org/10.1042/bj3280871.

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Endothelin-converting enzyme 1 (ECE-1) is a membrane-bound metalloprotease that catalyses the conversion of inactive big endothelins into active endothelins. Two different isoforms (ECE-1a and ECE-1b) have previously been identified for human ECE-1. In the present study we have cloned a novel human ECE-1 isoform, termed ECE-1c, and have thus shown for the first time the existence of three distinct ECE-1 isoforms. The three isoforms differ only in their N-terminal regions and are derived from a single gene through the use of alternative promoters. Ribonuclease protection experiments revealed that, although the relative levels of the three isoform mRNA species vary between human tissues, ECE-1c mRNA is generally the predominant isoform messenger. Immunofluorescence microscopy analysis showed distinct subcellular localizations for the three isoforms: whereas ECE-1a and ECE-1c are localized at the cell surface, ECE-1b was found to be intracellular and showed significant co-localization with a marker protein for the trans-Golgi network. We determined that the three isoforms have similar kinetic rate constants (Km, kcat and Vmax) for the processing of big endothelin 1 and that the big endothelin isoforms 1, 2 and 3 are cleaved with similar relative velocities of 1.0:0.1:0.1 by the three isoenzymes.

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23

Muller, Laurent, Olivier Valdenaire, Alain Barret, Petra Korth, Florence Pinet, Pierre Corvol, and Claude Tougard. "Expression of the Endothelin-Converting Enzyme-1 Isoforms in Endothelial Cells." Journal of Cardiovascular Pharmacology 36 (2000): S15—S18. http://dx.doi.org/10.1097/00005344-200036001-00007.

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24

Muller, Laurent, Olivier Valdenaire, Alain Barret, Petra Korth, Florence Pinet, Pierre Corvol, and Claude Tougard. "Expression of the Endothelin-Converting Enzyme-1 Isoforms in Endothelial Cells." Journal of Cardiovascular Pharmacology 36, Supplement 1 (2000): S15—S18. http://dx.doi.org/10.1097/00005344-200036051-00007.

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25

Ikegawa, Ruriko, Yasuo Matsumura, Yaeko Tsukahara, Masanori Takaoka, and Shiro Morimoto. "Suppression of endothelin-1 release from endothelial cells by inhibiting an endothelin-converting enzyme." Japanese Journal of Pharmacology 55 (1991): 163. http://dx.doi.org/10.1016/s0021-5198(19)38500-2.

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26

Khamaisi, Mogher, Rachel Dahan, Saher Hamed, Zaid Abassi, Samuel N. Heyman, and Itamar Raz. "Role of Protein Kinase C in the Expression of Endothelin Converting Enzyme-1." Endocrinology 150, no. 3 (October 30, 2008): 1440–49. http://dx.doi.org/10.1210/en.2008-0524.

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Increased expression of endothelin converting enzyme-1 (ECE-1) is associated with diabetic nephropathy. The molecular mechanisms underlying this association, as yet unknown, possibly involve protein kinase C (PKC) pathways. In the present study, we examined the effects of high glucose and PKC activation on ECE-1 expression in primary human umbilical vein endothelial cells (HUVECs) and in HUVEC line (EA.hy926). Increasing glucose concentration, but not mannitol, from 5.5–22.2 mmol/liter for 3 d, enhanced prepro endothelin-1 (ET-1) mRNA expression, ET-1 levels, ECE-1 protein, and mRNA expressions by 7, 4, 20, and 2.6-fold, respectively. High glucose increased ECE-1 protein expression dose and time dependently. By Western blot analysis, PKC-β1, -β2, and -δ isoform levels were significantly increased relative to other isoforms when glucose level was increased. Treatment with Rottlerin, a PKC-δ isoform inhibitor, reduced significantly the glucose-induced ET-1 secretion, and ECE-1 protein expression, but (S)-13-[(dimethylamino)methyl]-10,11,14,15-tetrahydro-4,9:16,21-dimetheno 1H,13H-dibenzo[e,k]pyrrolo[3,4-h] (1, 4, 3) oxadiaza-cyclohexadecene-1,3(2H)-dione or Gö6976, specific PKC-β and -α inhibitors, respectively, did not. Overexpression of PKC-δ but not PKC-α or -β1 isoforms by adenovirus vector containing the respective cDNA in HUVECs incubated with 5.5 mmol/liter glucose, increased in parallel PKC proteins, and glucose-induced endothein-1 and ECE-1 protein expression by 4- to 6-fold. These results show that enhanced ECE-1 expression induced by hyperglycemia is partly due to activation of the PKC-δ isoform. Thus, inhibition of this PKC isoform may prevent diabetes-related increase in ET-1. Hyperglycemia-induced enhanced endothelin converting enzyme-1 expression is mediated by PKC-δ. Inhibition of this PKC isoform may prevent diabetes-related increase in endothelin-1.

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27

Peri, A. "Gene Expression of Endothelin-1, Endothelin-Converting Enzyme-1, and Endothelin Receptors in Human Epididymis." Journal of Clinical Endocrinology & Metabolism 82, no. 11 (November 1, 1997): 3797–806. http://dx.doi.org/10.1210/jc.82.11.3797.

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28

Peri, Alessandro, Guido Fantoni, Simone Granchi, Gabriella B. Vannelli, Tullio Barni, Sandra Amerini, Cinzia Pupilli, et al. "Gene Expression of Endothelin-1, Endothelin-Converting Enzyme-1, and Endothelin Receptors in Human Epididymis1." Journal of Clinical Endocrinology & Metabolism 82, no. 11 (November 1997): 3797–806. http://dx.doi.org/10.1210/jcem.82.11.4395.

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29

Sluck, J. M., R. C. S. Lin, L. I. Katolik, A. Y. Jeng, and J. C. Lehmann. "Endothelin converting enzyme-1-, endothelin-1-, and endothelin-3-like immunoreactivity in the rat brain." Neuroscience 91, no. 4 (July 1999): 1483–97. http://dx.doi.org/10.1016/s0306-4522(98)00692-7.

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30

Molet, Sophie, Kanako Furukawa, Azzam Maghazechi, Qutayba Hamid, and Adel Giaid. "Chemokine- and cytokine-induced expression of endothelin 1 and endothelin-converting enzyme 1 in endothelial cells." Journal of Allergy and Clinical Immunology 105, no. 2 (February 2000): 333–38. http://dx.doi.org/10.1016/s0091-6749(00)90084-8.

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31

Herman, William H., Joseph Holcomb, Donald E. Hricik, and Michael S. Simonson. "INTERLEUKIN-1?? STIMULATES ENDOTHELIN-1 GENE TRANSCRIPTION AND ENDOTHELIN CONVERTING ENZYME ACTIVITY IN HUMAN ENDOTHELIAL CELLS." Transplantation 65, no. 12 (June 1998): S43. http://dx.doi.org/10.1097/00007890-199806270-00182.

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32

Magder, Sheldon, Danesh Javeshghani, Peter Cernacek, and Adel Giaid. "REGIONAL DISTRIBUTION OF ENDOTHELIN-1 AND ENDOTHELIN CONVERTING ENZYME-1 IN PORCINE ENDOTOXEMIA." Shock 16, no. 4 (October 2001): 320–25. http://dx.doi.org/10.1097/00024382-200116040-00015.

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33

Shao, Rong, Wei Yan, and Don C. Rockey. "Regulation of Endothelin-1 Synthesis by Endothelin-converting Enzyme-1 during Wound Healing." Journal of Biological Chemistry 274, no. 5 (January 29, 1999): 3228–34. http://dx.doi.org/10.1074/jbc.274.5.3228.

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34

Jullien, Nicolas, Anastasios Makritis, Dimitris Georgiadis, Fabrice Beau, Athanasios Yiotakis, and Vincent Dive. "Phosphinic Tripeptides as Dual Angiotensin-Converting Enzyme C-Domain and Endothelin-Converting Enzyme-1 Inhibitors." Journal of Medicinal Chemistry 53, no. 1 (January 14, 2010): 208–20. http://dx.doi.org/10.1021/jm9010803.

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35

SCHWEIZER, Anja, Bernd-Michael LÖFFLER, and Jack ROHRER. "Palmitoylation of the three isoforms of human endothelin-converting enzyme-1." Biochemical Journal 340, no. 3 (June 8, 1999): 649–56. http://dx.doi.org/10.1042/bj3400649.

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Endothelin-converting enzyme-1 (ECE-1) is a membrane-bound metalloprotease that catalyses the conversion of inactive big endothelins into active endothelins. Here we have examined whether the three isoforms of human ECE-1 (ECE-1a, ECE-1b and ECE-1c) are modified by the covalent attachment of the fatty acid palmitate and have evaluated a potential functional role of this modification. To do this, wild-type and mutant enzymes were expressed and analysed by metabolic labelling with [3H]palmitate, immunoprecipitation and SDS/PAGE. All three ECE-1 isoforms were found to be palmitoylated via hydroxylamine-sensitive thioester bonds. In addition, the isoforms showed similar levels of acylation. Cys46 in ECE-1a, Cys58 in ECE-1b and Cys42 in ECE-1c were identified as sites of palmitoylation and each of these cysteines accounted for all the palmitoylation that occured in the corresponding isoform. Immunofluorescence analysis demonstrated further that palmitoylated and non-palmitoylated ECE-1 isoforms had the same subcellular localizations. Moreover, complete solubility of the three isoforms in Triton X-100 revealed that palmitoylation does not target ECE-1 to cholesterol and sphingolipid-rich membrane domains or caveolae. The enzymic activities of ECE-1a, ECE-1b and ECE-1c were also not significantly affected by the absence of palmitoylation.

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36

López-Ongil, S., M. Saura, C. Zaragoza, L. Gónzalez-Santiago, M. Rodrı́guez-Puyol, C. J. Lowenstein, and D. Rodrı́guez-Puyol. "Hydrogen peroxide regulation of bovine endothelin-converting enzyme-1." Free Radical Biology and Medicine 32, no. 5 (March 2002): 406–13. http://dx.doi.org/10.1016/s0891-5849(01)00822-x.

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37

McCormick, Anna, Jasmin Kristianto, Xiaohu Wang, Jennifer McIntosh, Meredith Cruz, Judith U. Hibbard, and Robert D. Blank. "Placental endothelin-converting enzyme-1 is decreased in preeclampsia." Pregnancy Hypertension 20 (April 2020): 108–10. http://dx.doi.org/10.1016/j.preghy.2020.04.001.

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38

MacLeod, Kathryn J., Rhonda D. Husain, Douglas A. Gage, and Kyunghye Ahn. "Constitutive Phosphorylation of Human Endothelin-converting Enzyme-1 Isoforms." Journal of Biological Chemistry 277, no. 48 (September 18, 2002): 46355–63. http://dx.doi.org/10.1074/jbc.m207972200.

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39

Johnson, Gary D., Tracy Stevenson, and Kyunghye Ahn. "Hydrolysis of Peptide Hormones by Endothelin-converting Enzyme-1." Journal of Biological Chemistry 274, no. 7 (February 12, 1999): 4053–58. http://dx.doi.org/10.1074/jbc.274.7.4053.

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40

Ahn, Kyunghye, Andre M. Sisneros, Sarah B. Herman, Sharon M. Pan, Donald Hupe, Chitase Lee, Sham Nikam, et al. "Novel Selective Quinazoline Inhibitors of Endothelin Converting Enzyme-1." Biochemical and Biophysical Research Communications 243, no. 1 (February 1998): 184–90. http://dx.doi.org/10.1006/bbrc.1998.8081.

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41

Volpi, N., P. Carbotti, G. Greco, G. Bibbo, C. Alessandrini, and F. Giannini. "Endothelin and endothelin-converting-enzyme-1 in inflammatory neuropathies: an immunohistological study." Journal of the Peripheral Nervous System 9, no. 2 (June 2004): 118. http://dx.doi.org/10.1111/j.1085-9489.2004.009209au.x.

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42

Zolk, Oliver, Jessika Quattek, Gerhard Sitzler, Thomas Schrader, Georg Nickenig, Petra Schnabel, Kohei Shimada, Masaaki Takahashi, and Michael Böhm. "Expression of Endothelin-1, Endothelin-Converting Enzyme, and Endothelin Receptors in Chronic Heart Failure." Circulation 99, no. 16 (April 27, 1999): 2118–23. http://dx.doi.org/10.1161/01.cir.99.16.2118.

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43

McDermott, Colleen D., Hani Shennib, and Adel Giaid. "Immunohistochemical Localization of Endothelin-1 and Endothelin-Converting Enzyme-1 in Rat Lung Allografts." Journal of Cardiovascular Pharmacology 31 (1998): S27—S30. http://dx.doi.org/10.1097/00005344-199800001-00010.

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44

CARSON, Julie A., Toshihiro ANSAI, Shuji AWANO, Weixian YU, Tadamichi TAKEHARA, and Anthony J. TURNER. "Characterization of PgPepO, a bacterial homologue of endothelin-converting enzyme-1." Clinical Science 103, s2002 (September 1, 2002): 90S—93S. http://dx.doi.org/10.1042/cs103s090s.

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Abstract:

PgPepO is a homologue of endothelin-converting enzyme-1 (ECE-1), with which it shares 31% identity. PgPepO was isolated from the periodontal pathogen Porphyromonas gingivalis. Recent studies have suggested a link between periodontal and cardiovascular disease, and several groups have suggested that bacterial and viral infections may contribute to the latter. P. gingivalis possesses the ability to invade, and multiply within, aortic endothelial cells and has been localized to atherosclerotic plaques. PgPepO was expressed and purified to homogeneity and we have begun detailed functional analysis, in terms of substrate preference and inhibitor specificity, in order to provide active-site comparisons with other members of the neprilysin (NEP)/ECE family. PgPepO possesses similar substrate specificity to ECE-1 and has been shown to cleave big endothelin-1 (big ET-1), big ET-2 and big ET-3, converting the substrates into their respective mature endothelin peptides. Substance P, angiotensin I, angiotensin II and neurotensin are all cleaved at multiple sites by PgPepO and the kinetics of these reactions have been compared. The potent vasoconstrictor urotensin II is not hydrolysed by PgPepO. Cleavage of bradykinin by PgPepO occurs at the Pro7-Phe8 bond and is inhibited by the NEP and ECE-1 inhibitor phosphoramidon in a pH-dependent fashion (IC50 = 10µM at pH 7.0) but not by thiorphan, an NEP-specific inhibitor. PgPepO activity is completely inhibited by EDTA. Characterization of this enzyme is important in elucidating possible links between periodontal pathogens and cardiovascular disorders such as atherosclerosis, and provides an opportunity to gain structural information on a bacterial protein with striking similarity to human ECE-1.

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Barnes, Kay, Julie A. Carson, and Anthony J. Turner. "Regulation of the isoforms of brain and endothelial endothelin converting enzyme-1." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A81. http://dx.doi.org/10.1042/bst028a081a.

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46

Haynes, William G. "Endothelins as Regulators of Vascular Tone in Man." Clinical Science 88, no. 5 (May 1, 1995): 509–17. http://dx.doi.org/10.1042/cs0880509.

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1. The vascular pharmacology, physiological relevance and pathophysiological roles of the endothelium-derived vasoconstrictor peptide endothelin-1 have been unclear. These issues were investigated, in vivo in man, using infusion of drugs into the brachial artery or dorsal hand vein, with responses measured by forearm plethysmography and the hand vein displacement technique respectively. 2. Endothelin-1 is a potent and sustained constrictor of resistance and capacitance vessels in vivo in man, acting through both subtypes (ETA and ETB) of endothelin receptors. Endothelin-1 stimulates generation of vasodilator prostaglandins, but not of nitric oxide, that act to oppose its direct constrictor actions. Venoconstriction to endothelin-1 is blocked more effectively by K+-channel openers than by Ca2+-channel antagonists, suggesting a novel cellular mechanism of action for this peptide. 3. The forearm vasculature is able to convert the precursor big endothelin-1 to the mature peptide, endothelin-1, thus demonstrating the local presence of ‘endothelin-converting enzyme’ in man. Local inhibition of this enzyme, or blockade of ETA receptors, causes slow-onset forearm vasodilatation, suggesting that endogenously generated endothelin-1 contributes to basal resistance vessel tone in man. 4. Venoconstriction to endothelin-1 is selectively enhanced in patients with untreated essential hypertension. Endothelin-1 also potentiates sympathetically mediated vasoconstriction, but only in hypertensive subjects. 5. Endogenous generation of endothelin-1 plays a fundamental physiological role in the maintenance of basal vascular tone. Endothlin-converting enzyme inhibitors and endothelin receptor antagonists possess novel vasodilator properties and should represent a major therapeutic advance in cardiovascular disease.

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Morawietz, H., W. Goettsch, M. Szibor, M. Barton, S. Shaw, K. Hakim, H. R. Zerkowski, and J. Holtz. "Angiotensin-converting enzyme inhibitor therapy prevents upregulation of endothelin-converting enzyme-1 in failing human myocardium." Biochemical and Biophysical Research Communications 295, no. 5 (August 2002): 1057–61. http://dx.doi.org/10.1016/s0006-291x(02)00799-4.

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48

Gokhale, Nikhil H., and J. A. Cowan. "Metallopeptide-promoted inactivation of angiotensin-converting enzyme and endothelin-converting enzyme 1: toward dual-action therapeutics." JBIC Journal of Biological Inorganic Chemistry 11, no. 7 (July 28, 2006): 937–47. http://dx.doi.org/10.1007/s00775-006-0145-2.

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49

Davenport, Anthony P., and Rhoda E. Kuc. "Cellular Expression of Isoforms of Endothelin-Converting Enzyme-1 (ECE-1c, ECE-1b and ECE-1a) and Endothelin-Converting Enzyme-2." Journal of Cardiovascular Pharmacology 36 (2000): S12—S14. http://dx.doi.org/10.1097/00005344-200036001-00006.

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50

Davenport, Anthony P., and Rhoda E. Kuc. "Cellular Expression of Isoforms of Endothelin-Converting Enzyme-1 (ECE-1c, ECE-1b and ECE-1a) and Endothelin-Converting Enzyme-2." Journal of Cardiovascular Pharmacology 36, Supplement 1 (2000): S12—S14. http://dx.doi.org/10.1097/00005344-200036051-00006.

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