Mohamed Rholam +33-1-57278886 +33-1-57277263 mohamed.rholam@univ-paris-diderot.fr Christine Fahy Interfaces, Traitements, Organisation et Dynamique des Systrèmes (ITODYS) Université Paris Diderot (Paris 7), CNRS UMR 7086 Bâtiment Lavoisier, 15 rue Jean-Antoine de Baïf 75205 Paris Cedex 13 France Abstract Many functionally important cellular peptides and proteins, including hormones, neuropeptides, and growth factors, are synthesized as inactive precursor polypeptides, which require post-translational proteolytic processing to become biologically active polypeptides. This is achieved by the action of a relatively small number of proteases that belong to a family of seven subtilisin-like proprotein convertases (PCs) including furin. In view of this, this review focuses on the importance of privileged secondary structures and of given amino acid residues around basic cleavage sites in substrate recognition by these endoproteases. In addition to their participation in normal cell functions, PCs are crucial for the initiation and progress of many important diseases. Hence, these proteases constitute potential drug targets in medicine. Accordingly, this review also discusses the approaches used to shed light on the cleavage preference and the substrate specificity of the PCs, a prerequisite to select which PCs are promising drug targets in each disease.
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Processing of peptide and hormone precursors at the dibasic cleavage sites
Mohamed, Rholam; Christine, Fahy
Follow Cellular and Molecular Life Sciences
, Volume 66 (13)
Springer Journals – Jul 1, 2009
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