Molecular isolation and characterization of novel four subisoforms of ECE-2
Copyright policy )Molecular isolation and characterization of novel four subisoforms of ECE-2
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.
- Kobe University Japan
Male, Sequence Homology, Amino Acid, Molecular Sequence Data, Brain, Metalloendopeptidases, CHO Cells, Endothelin-Converting Enzymes, Rats, Isoenzymes, Mice, Liver, Cricetinae, Adrenal Glands, Animals, Aspartic Acid Endopeptidases, Humans, Cattle, Amino Acid Sequence, Endothelium, Vascular, Sequence Alignment
Male, Sequence Homology, Amino Acid, Molecular Sequence Data, Brain, Metalloendopeptidases, CHO Cells, Endothelin-Converting Enzymes, Rats, Isoenzymes, Mice, Liver, Cricetinae, Adrenal Glands, Animals, Aspartic Acid Endopeptidases, Humans, Cattle, Amino Acid Sequence, Endothelium, Vascular, Sequence Alignment
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