Organization and Chromosomal Localization of the Human ECEL1 (XCE) Gene Encoding a Zinc Metallopeptidase Involved in the Nervous Control of Respiration

Overview

Journal Biochem J

Specialty Biochemistry

Date 2000 Mar 4

PMID 10698686

Citations 7

Authors

O Valdenaire

E Rohrbacher

A Langeveld

A Schweizer

C Meijers

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

Brachial Plexus Root Avulsion Injury-Induced Endothelin-Converting Enzyme-Like 1 Overexpression Is Associated with Injured Motor Neurons Survival.

Huang Y, Mai Y, Ye W, Lv S, Zhou Y, Wu P Mol Neurobiol. 2024; 61(8):5194-5205.

PMID: 38170441 DOI: 10.1007/s12035-023-03887-7.

ECEL1 novel mutation in arthrogryposis type 5D: A molecular dynamic simulation study.

Ahangari N, Gholampour-Faroji N, Doosti M, Ghayour Mobarhan M, Shahrokhzadeh S, Karimiani E Mol Genet Genomic Med. 2023; 11(6):e2153.

PMID: 36794879 PMC: 10265054. DOI: 10.1002/mgg3.2153.

New Insights of a Neuronal Peptidase DINE/ECEL1: Nerve Development, Nerve Regeneration and Neurogenic Pathogenesis.

Kiryu-Seo S, Nagata K, Saido T, Kiyama H Neurochem Res. 2018; 44(6):1279-1288.

PMID: 30357652 DOI: 10.1007/s11064-018-2665-x.

Dynamic changes in the secondary structure of ECE-1 and XCE account for their different substrate specificities.

Ul-Haq Z, Iqbal S, Moin S BMC Bioinformatics. 2012; 13:285.

PMID: 23113990 PMC: 3558449. DOI: 10.1186/1471-2105-13-285.

The wrickkened pathways of FGF23, MEPE and PHEX.

Rowe P Crit Rev Oral Biol Med. 2004; 15(5):264-81.

PMID: 15470265 PMC: 3361894. DOI: 10.1177/154411130401500503.

References

DeVault A, Lazure C, Nault C, Le Moual H, Seidah N, Chretien M . Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA. EMBO J. 1987; 6(5):1317-22. PMC: 553935. DOI: 10.1002/j.1460-2075.1987.tb02370.x. View

Valdenaire O, Egidy G, Thouard A, Barret A, Vranckx R, Tougard C . A fourth isoform of endothelin-converting enzyme (ECE-1) is generated from an additional promoter molecular cloning and characterization. Eur J Biochem. 1999; 264(2):341-9. DOI: 10.1046/j.1432-1327.1999.00602.x. View

Shipp M, Richardson N, Sayre P, Brown N, Masteller E, Clayton L . Molecular cloning of the common acute lymphoblastic leukemia antigen (CALLA) identifies a type II integral membrane protein. Proc Natl Acad Sci U S A. 1988; 85(13):4819-23. PMC: 280527. DOI: 10.1073/pnas.85.13.4819. View

Letarte M, Vera S, Tran R, Addis J, Onizuka R, Quackenbush E . Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. J Exp Med. 1988; 168(4):1247-53. PMC: 2189092. DOI: 10.1084/jem.168.4.1247. View

DAdamio L, Shipp M, Masteller E, Reinherz E . Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5' untranslated regions. Proc Natl Acad Sci U S A. 1989; 86(18):7103-7. PMC: 298003. DOI: 10.1073/pnas.86.18.7103. View

Lee S, Zambas E, Marsh W, Redman C . Molecular cloning and primary structure of Kell blood group protein. Proc Natl Acad Sci U S A. 1991; 88(14):6353-7. PMC: 52081. DOI: 10.1073/pnas.88.14.6353. View

Roques B, Noble F, Dauge V, Fournie-Zaluski M, Beaumont A . Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. Pharmacol Rev. 1993; 45(1):87-146. View

Shimada K, Takahashi M, Tanzawa K . Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J Biol Chem. 1994; 269(28):18275-8. View

Xu D, Emoto N, Giaid A, Slaughter C, Kaw S, Dewit D . ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell. 1994; 78(3):473-85. DOI: 10.1016/0092-8674(94)90425-1. View

10.

Hooper N . Families of zinc metalloproteases. FEBS Lett. 1994; 354(1):1-6. DOI: 10.1016/0014-5793(94)01079-x. View

11.

Lee S, Zambas E, Green E, Redman C . Organization of the gene encoding the human Kell blood group protein. Blood. 1995; 85(5):1364-70. View

12.

Emoto N, Yanagisawa M . Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J Biol Chem. 1995; 270(25):15262-8. DOI: 10.1074/jbc.270.25.15262. View

13.

Mulder M, Wilke M, Langeveld A, Wilming L, Hagemeijer A, van Drunen E . Positional mapping of loci in the DiGeorge critical region at chromosome 22q11 using a new marker (D22S183). Hum Genet. 1995; 96(2):133-41. DOI: 10.1007/BF00207368. View

14.

Li C, Chen G, Gerard N, Gerard C, Bozic C, Hersh L . Comparison of the structure and expression of the human and rat neprilysin (endopeptidase 24.11)-encoding genes. Gene. 1995; 164(2):363-6. DOI: 10.1016/0378-1119(95)00464-h. View

15.

Breathnach R, Chambon P . Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981; 50:349-83. DOI: 10.1146/annurev.bi.50.070181.002025. View

16.

Valdenaire O, Rohrbacher E, Mattei M . Organization of the gene encoding the human endothelin-converting enzyme (ECE-1). J Biol Chem. 1995; 270(50):29794-8. DOI: 10.1074/jbc.270.50.29794. View

17.

Kondrakhin Y, Kel A, Kolchanov N, Romashchenko A, Milanesi L . Eukaryotic promoter recognition by binding sites for transcription factors. Comput Appl Biosci. 1995; 11(5):477-88. DOI: 10.1093/bioinformatics/11.5.477. View

18.

Holm I, Huang X, Kunkel L . Mutational analysis of the PEX gene in patients with X-linked hypophosphatemic rickets. Am J Hum Genet. 1997; 60(4):790-7. PMC: 1712471. View

19.

Francis F, Strom T, Hennig S, Boddrich A, Lorenz B, Brandau O . Genomic organization of the human PEX gene mutated in X-linked dominant hypophosphatemic rickets. Genome Res. 1997; 7(6):573-85. DOI: 10.1101/gr.7.6.573. View

20.

Orzechowski H, Richter C, Funke-Kaiser H, Kroger B, Schmidt M, Menzel S . Evidence of alternative promoters directing isoform-specific expression of human endothelin-converting enzyme-1 mRNA in cultured endothelial cells. J Mol Med (Berl). 1997; 75(7):512-21. DOI: 10.1007/s001090050136. View