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Dipeptidyl Aminopeptidases: Basic Science and Clinical Applications (Advances in Experimental Medicine and Biology)

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DPP IV has been attributed a large array of functions, some of which are mediated by its exopeptidase activity. Although it only removes two amino acid residues at the N-terminus of the peptide, this cleavage can inactivate or modify the activity of regulatory peptides, peptide hormones, chemokines and neuropeptides. Several excellent DPP IV substrates with high specificity constants were identified by the in vitro kinetic study of the truncation of bioactive peptides by DPP IV. In vivo studies e.g. with DPP IV negative animals and in vivo inhibition experiments could enlighten us on the physiological relevance of these truncations.

The DPP IV mediated truncation of bioactive peptides has been reviewed on several occasions (Mentlein et al 1999, Lambeir et al 2003, De Meester et al 2000 and 2003). Here we want (1) to present some data on a novel DPP IV substrate, (2) to review some of the recent literature on known substrates and (3) to discuss the possible truncation of known DPP IV substrates by related dipeptidyl peptidases.

This is the first comprehensive volume on Dipeptidyl Aminopeptidases that can be marketed to a wide variety of disciplines, as well as to a variety of clinicians. Leading experts in the field contribute to this state-of-the-art view on these enzymes. This book comes at a time when our understanding of their function is growing ever more rapidly and therapeutic options have become imminent.

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