Endothelin-converting enzyme-like I (ECEL1; ‘XCE’): a putative metallopeptidase crucially involved in the nervous control of respiration

2000 ◽  
Vol 28 (4) ◽  
pp. 426-430 ◽  
Author(s):  
O. Valdenaire ◽  
A. Schweizer
Keyword(s):  
Physiological Function ◽  
Control Of Respiration ◽  
Converting Enzyme ◽  
Specific Expression ◽  
Nervous Control ◽  
Zinc Metalloprotease ◽  
Neonatal Lethality ◽  
Its Gene ◽  
Endothelin Converting Enzyme ◽  
The Central Nervous System

Endothelin-converting enzyme-like 1 (ECEL1) is a putative zinc metalloprotease that was recently identified on the basis of its strong similarity to endothelin-converting enzyme 1. The physiological function of ECEL1 remains unknown so far; the failure to identify a substrate for ECEL1 could be related to the endoplasmic reticulum subcellular localization found by immunofluorescence in recombinant systems. However, clues to the function of ECEL1 were provided by the in-activation of its gene in mice, which resulted in neonatal lethality. The phenotype of homozygous ECEL1− mice, together with the very specific expression profile of its mRNA in the central nervous system, suggests that ECEL1 is crucially involved in the nervous control of respiration.

scholarly journals Organization and chromosomal localization of the human ECEL1 (XCE) gene encoding a zinc metallopeptidase involved in the nervous control of respiration

2000 ◽  
Vol 346 (3) ◽  
pp. 611-616 ◽  
Author(s):  
Olivier VALDENAIRE ◽  
Elisabeth ROHRBACHER ◽  
An LANGEVELD ◽  
Anja SCHWEIZER ◽  
Carel MEIJERS
Keyword(s):  
Critical Role ◽  
Phylogenetic Study ◽  
Control Of Respiration ◽  
Chromosome 2 ◽  
Converting Enzyme ◽  
Gene Encoding ◽  
Nervous Control ◽  
Zinc Metalloprotease ◽  
Endothelin Converting Enzyme

ECEL1 (endothelin-converting enzyme-like 1; previously known as XCE) is a putative zinc metalloprotease that was identified recently on the basis of its strong identity with endothelin-converting enzyme. Although the physiological function of ECEL1 is unknown, inactivation of the corresponding gene in mice points to a critical role of this protein in the nervous control of respiration. In the present study we have characterized the human ECEL1 gene. It was located to region q36-q37 of chromosome 2 and shown to be composed of 18 exons spanning approx. 8 kb. The structure of the ECEL1 gene displays some striking similarities with those of genes of related metallopeptidases, supporting the hypothesis that they are all derived from a common ancestor. A short phylogenetic study describing the relationship between the various members of this gene family is also presented.

Evidence of alternative promoters directing isoform-specific expression of human endothelin-converting enzyme-1 mRNA in cultured endothelial cells

1997 ◽  
Vol 75 (7) ◽  
pp. 512-521 ◽  
Author(s):  
Hans-Dieter Orzechowski ◽  
Claus-Michael Richter ◽  
Heiko Funke-Kaiser ◽  
Burkhard Kröger ◽  
Martin Schmidt ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Alternative Promoters ◽  
Converting Enzyme ◽  
Specific Expression ◽  
Cultured Endothelial Cells ◽  
Endothelin Converting Enzyme

scholarly journals Neonatal Lethality in Mice Deficient in XCE, a Novel Member of the Endothelin-converting Enzyme and Neutral Endopeptidase Family

1999 ◽  
Vol 274 (29) ◽  
pp. 20450-20456 ◽  
Author(s):  
Anja Schweizer ◽  
Olivier Valdenaire ◽  
Anja Köster ◽  
Yolande Lang ◽  
Georg Schmitt ◽  
...  
Keyword(s):  
Neutral Endopeptidase ◽  
Converting Enzyme ◽  
Neonatal Lethality ◽  
Endothelin Converting Enzyme

Transcriptional Mechanism of Protein Kinase C-Induced Isoform-Specific Expression of the Gene for Endothelin-Converting Enzyme-1in Human Endothelial Cells

2001 ◽  
Vol 60 (6) ◽  
pp. 1332-1342 ◽  
Author(s):  
Hans-Dieter Orzechowski ◽  
Astrid Günther ◽  
Stefan Menzel ◽  
Andreas Zimmermann ◽  
Heiko Funke-Kaiser ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Converting Enzyme ◽  
Human Endothelial Cells ◽  
Specific Expression ◽  
Kinase C ◽  
Endothelin Converting Enzyme

Expression of human endothelin-converting enzyme isoforms: role of angiotensin IIThis article is one of a selection of papers published in the special issue (part 1 of 2) on Forefronts in Endothelin.

2008 ◽  
Vol 86 (6) ◽  
pp. 299-309 ◽  
Author(s):  
W. Goettsch ◽  
A. Schubert ◽  
H. Morawietz
Keyword(s):  
Endothelial Cells ◽  
Mrna Expression ◽  
Umbilical Vein ◽  
Artery Bypass ◽  
Control Group ◽  
Ang Ii ◽  
Converting Enzyme ◽  
Mammary Arteries ◽  
Endothelin Converting Enzyme ◽  
Internal Mammary

A key step in endothelin-1 (ET-1) synthesis is the proteolytic cleavage of big ET-1 by the endothelin-converting enzyme-1 (ECE-1). Four alternatively spliced isoforms, ECE-1a to ECE-1d, have been discovered; however, regulation of the expression of specific ECE-1 isoforms is not well understood. Therefore, we stimulated primary human umbilical vein endothelial cells (HUVECs) with angiotensin II (Ang II). Furthermore, expression of ECE-1 isoforms was determined in internal mammary arteries of patients undergoing coronary artery bypass grafting surgery. Patients had received one of 4 therapies: angiotensin-converting enzyme inhibitors (ACE-I), Ang II type 1 receptor blockers (ARB), HMG-CoA reductase inhibitors (statins), and a control group that had received neither ACE-I, ARB (that is, treatment not interfering in the renin–angiotensin system), nor statins. Under control conditions, ECE-1a is the dominant isoform in HUVECs (4.5 ± 2.8 amol/μg RNA), followed by ECE-1c (2.7 ± 1.0 amol/μg), ECE-1d (0.49 ± 0.17 amol/μg), and ECE-1b (0.17 ± 0.04 amol/μg). Stimulation with Ang II did not change the ECE-1 expression pattern or the ET-1 release. We found that ECE-1 mRNA expression was higher in patients treated with statins than in patients treated with ARB therapy (5.8 ± 0.76 RU versus 3.0 ± 0.4 RU), mainly attributed to ECE-1a. In addition, ECE-1a mRNA expression was higher in patients receiving ACE-I therapy than in patients receiving ARB therapy (1.68 ± 0.27 RU versus 0.83 ± 0.07 RU). We conclude that ECE-1a is the major ECE-1 isoform in primary human endothelial cells. Its expression in internal mammary arteries can be regulated by statin therapy and differs between patients with ACE-I and ARB therapy.

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