Human endothelin converting enzyme-2 (ECE2): characterization of mRNA species and chromosomal localization

Generation of the functionally pleiotropic members of the endothelin vasoac tive peptide family is critically catalyzed by unique type II metalloprotea ses, termed endothelin converting enzymes (ECE). Isolation of human ECE-2 ( EC 3.4.24.71) cDNAs revealed deduced open reading frames of 787 and 765 ami no acids with approximately 60% identity with human ECE-1. Characterization of mRNA variants revealed mRNA structural diversity at the 5'-terminus. Tw o mRNA species exist containing distinct first and second exons. Furthermor e, in one of these species, an in-frame deletion of the intracytoplasmic do main removed 29 amino acids. Because of the previously reported human genet ic diseases ascribed to germline mutations of member genes of the endotheli n family, ECE2 was localized in human chromosomes with fluorescence in situ hybridization and radiation hybrid mapping to 3q28-q29 and SHGC-20171/D3S1 571, respectively. (C) 2001 Elsevier Science B.V. All rights reserved.