Identification and characterization of two isoforms of an endothelin-converting enzyme-1.
We report the cloning and sequencing of 5'-terminal region of a beta form of rat ECE-1 cDNA which is different only in its N-terminal amino-acid sequence to the cDNA we have cloned previously (alpha form [K. Shimada et al. (1994) J. Biol. Chem. 269, 18275-18278]). No significant difference was found in the specific activity and substrate specificity between the two isoforms. The expression level of ECE-1 alpha mRNA was higher than that of ECE-1 beta in various rat cells and tissues, suggesting that the physiologically important isoform is ECE-1 alpha. The present findings verified the presence of two forms of ECE-1 over many species, which are created probably through alternative splicing.
Shimada
K
K
Biological Research Laboratories, Sankyo Co. Ltd., Tokyo, Japan.
Takahashi
M
M
Ikeda
M
M
Tanzawa
K
K
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D001483:Base Sequence; D002460:Cell Line; D002461:Cell Line, Transformed; D003001:Cloning, Molecular; D000072396:Endothelin-Converting Enzymes; D004730:Endothelium, Vascular / Q000201:enzymology; D015870:Gene Expression; D006801:Humans; D007527:Isoenzymes / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D008168:Lung / Q000201:enzymology; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000378:metabolism; D013379:Substrate Specificity; D014471:Umbilical Veins
D007527:Isoenzymes; D012333:RNA, Messenger; D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; C000606923:ECE1 protein, human; D000072396:Endothelin-Converting Enzymes