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http://purl.uniprot.org/citations/12054617http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12054617http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12054617http://www.w3.org/2000/01/rdf-schema#comment"Endothelin-converting enzymes (ECEs) are the key enzymes in the endothelin (ET) biosynthesis that catalyze the conversion of big ET, the biologically inactive precursor of mature ET. Two enzymes, termed ECE-1 and ECE-2, have been molecularly identified. Here, we report novel four subisoforms of ECE-2 that differ in their N-terminal cytoplasmic tails, termed ECE-2a-1, ECE-2a-2, ECE-2b-1, and ECE-2b-2. RT-PCR analysis of these subisoforms in bovine tissues demonstrated that their tissue distribution was strikingly different. ECE-2a-1 and ECE-2a-2 are expressed in a variety of tissues including liver, kidney, adrenal gland, testis, and endothelial cells, while ECE-2b-1 and ECE-2b-2 are expressed abundantly in brain and adrenal gland. Furthermore, ECE-2a-1 and ECE-2b-2 were revealed to be predominant forms as compared to ECE-2a-2 and ECE-2b-1, respectively. Immunohistochemical analyses of CHO cells, stably expressing ECE-2a-1 or ECE-2b-2, revealed that both ECE-2a-1 and ECE-2b-2 were localized in intracellular compartments but not on the cell surface. Detailed analysis of ECE-2 subisoforms will provide crucial information to clarify the physiological function of ECE-2."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(02)00252-8"xsd:string
http://purl.uniprot.org/citations/12054617http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(02)00252-8"xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Matsuo M."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Matsuo M."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Yokoyama M."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Yokoyama M."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Ikeda S."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Ikeda S."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Emoto N."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Emoto N."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Alimsardjono H."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/author"Alimsardjono H."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/pages"421-426"xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/pages"421-426"xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/title"Molecular isolation and characterization of novel four subisoforms of ECE-2."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/title"Molecular isolation and characterization of novel four subisoforms of ECE-2."xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/volume"293"xsd:string
http://purl.uniprot.org/citations/12054617http://purl.uniprot.org/core/volume"293"xsd:string