K. Yorimitsu et al., CLONING AND SEQUENCING OF A HUMAN ENDOTHELIN-CONVERTING ENZYME IN RENAL ADENOCARCINOMA (ACHN) CELLS PRODUCING ENDOTHELIN-2, Biochemical and biophysical research communications, 208(2), 1995, pp. 721-727
Endothelin (ET)-2 is a 21 residue vasoactive peptide which is biosynth
esized from big ET-2(1-38) by a specific cleavage at Trp(21)-Val(22) w
ith an ET converting enzyme (ECE). To identify an ECE in ACHN (human r
enal adenocarcinoma) cells which produce ET-2, we have cloned and sequ
enced a novel cDNA encoding a human ECE in ACHN (hAECE). It encodes a
770 amino acid protein with a zinc-binding motif and a single membrane
spanning region. The sequences of nucleic acids and amino acids from
Leu(45) to Trp(770) of hAECE are identical to those from Leu(33) to Tr
p(758) Of a human ECE in HUVEC (hHECE). The sequences in the amino-ter
minal moiety are divergent between hAECE and hHECE. Based on the diffe
rence of the amino-terminal amino acid sequences, ECEs reported so far
, can be classified into two isoforms. These results strongly suggest
that an alternative splicing might occur in the 5'-terminal region of
the ECE pre-mRNA. (C) 1995 Academic Press, Inc.