Bioinformatic analysis of the neprilysin (M13) family of peptidases reveals complex evolutionary and functional relationships |
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Authors: | Nicholas D Bland John W Pinney Josie E Thomas Anthony J Turner R Elwyn Isaac |
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Institution: | (1) Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK;(2) Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK;(3) INSERM U609, Wellcome Centre for Molecular Parasitology, Glasgow Biomedical Research Facility, 120 University Place, University of Glasgow, Glasgow, G12 8TA, UK |
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Abstract: | Background The neprilysin (M13) family of endopeptidases are zinc-metalloenzymes, the majority of which are type II integral membrane
proteins. The best characterised of this family is neprilysin, which has important roles in inactivating signalling peptides
involved in modulating neuronal activity, blood pressure and the immune system. Other family members include the endothelin
converting enzymes (ECE-1 and ECE-2), which are responsible for the final step in the synthesis of potent vasoconstrictor
endothelins. The ECEs, as well as neprilysin, are considered valuable therapeutic targets for treating cardiovascular disease.
Other members of the M13 family have not been functionally characterised, but are also likely to have biological roles regulating
peptide signalling. The recent sequencing of animal genomes has greatly increased the number of M13 family members in protein
databases, information which can be used to reveal evolutionary relationships and to gain insight into conserved biological
roles. |
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