1995
DOI: 10.1016/0014-5793(95)00886-e
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Identification and characterization of two isoforms of an endothelin‐converting enzyme‐1

Abstract: . No significant difference was found in the specific activity and substrate specificity between the two isoforms. The expression level of ECE-I~ mRNA was higher than that of ECE-I~ in various rat cells and tissues, suggesting that the physiologically important isoform is ECE-la. The present findings verified the presence of two forms of ECE-1 over many species, which are created probably through alternative splicing.

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Cited by 118 publications
(79 citation statements)
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“…23 The present study confirms and extends previous investigations by demonstrating ECE-1 immunoreactivity in atherosclerotic vascular tissues and by determining the presence and distribution of the ␣ and ␤ isoforms of ECE-1. Shimada and colleagues 24,25 reported the expression of ECE-1 in rat ECs and human umbilical vein ECs and, later, isolated two isoforms of ECE-1 in humans. 26 This discovery led to the development of monoclonal ECE-1 antibodies.…”
Section: Discussionmentioning
confidence: 99%
“…23 The present study confirms and extends previous investigations by demonstrating ECE-1 immunoreactivity in atherosclerotic vascular tissues and by determining the presence and distribution of the ␣ and ␤ isoforms of ECE-1. Shimada and colleagues 24,25 reported the expression of ECE-1 in rat ECs and human umbilical vein ECs and, later, isolated two isoforms of ECE-1 in humans. 26 This discovery led to the development of monoclonal ECE-1 antibodies.…”
Section: Discussionmentioning
confidence: 99%
“…The reliability of internal branches was evaluated using bootstrap analysis (1000 replicas) and further supported by an analysis of the specific signature sequences of these enzymes. For Nep3 and LomECE the third zinc binding ligand ExxA/GD is located 61 residues downstream of the active site that corresponds to the 61 amino acid separation in human ECE-1 and ECE-2 (SHIMADA et al 1995). The characteristic ET binding site NAYY (SANSOM et al 1998) and the CEVW motif, critical for enzyme maturation and activity of ECE-1 and ECE-2 (MACLEOD et al 2001), are present in Nep3 and LomECE.…”
Section: Figure S1mentioning
confidence: 99%
“…Four isoforms of human ECE-1 differing only in the cytoplasmic tail are produced by a single gene located on chromosome 1 (1p36) through the use of alternate promoters (17,(21)(22)(23)(24)(25). The four isoforms cleave big ETs with equal efficiency but differ primarily in their subcellular localization and tissue distribution (24,25).…”
mentioning
confidence: 99%