Anti-peptide antibodies specific to rat endothelin-converting enzyme-1 isoforms reveal isoform localisation and expression

FEBS Letters
C D BrownA J Turner

Abstract

Endothelin-converting enzyme-1 (ECE-1) is a critical enzyme in the biosynthesis of the potent vasoconstrictor peptide endothelin and exists in several isoforms. Anti-peptide antibodies raised against epitopes in the distinct N-terminal cytoplasmic tails of the rat ECE-1 isoforms have been obtained. By using these antibodies in Western blot analysis and immunofluorescence studies, we have shown that cultures of transformed rat lung vascular endothelial cells treated with the metalloprotease inhibitor phosphoramidon and untreated cells express ECE-1alpha only, whereas human umbilical vein endothelial cells express ECE-1alpha and ECE-1beta. The ECE-1 isoforms expressed in CHO-K1 cells transfected with rat cDNA to ECE-1alpha and ECE-1beta could be immunoprecipitated by using the appropriate isospecific antibody.

References

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Citations

May 4, 2001·International Journal for Parasitology·S B PetkovaH B Tanowitz
Jan 1, 1999·Trends in Pharmacological Sciences·A J TurnerO Valdenaire
Nov 7, 2000·Cardiovascular Pathology : the Official Journal of the Society for Cardiovascular Pathology·S B PetkovaH Huang
Jun 9, 1999·The Biochemical Journal·A SchweizerJ Rohrer
Jun 12, 1999·Endothelium : Journal of Endothelial Cell Research·H B TanowitzG J Christ
Oct 12, 2005·International Journal of Cancer. Journal International Du Cancer·Shuji AwanoBadar A Usmani
Jun 27, 2003·Journal of Cardiovascular Pharmacology·Daiji IsakaMasafumi Matsuo
Oct 16, 2010·International Journal of Cancer. Journal International Du Cancer·Yue HongBadar A Usmani
Dec 26, 2003·American Journal of Physiology. Lung Cellular and Molecular Physiology·Lisa K KellyStephen M Black

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