Proline residues in the maturation and degradation of peptide hormones and neuropeptides

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Abstract
The proteases involved in the maturation of regulatory peptides like those of broader specificity normally fail to cleave peptide bonds linked to the cyclic amino acid proline. This generates several mature peptides with N‐terminal X‐Prosequences. However, in certain non‐mammalian tissues repetitive pre‐sequences of this type are removed by specialized dipeptidyl (amino)peptidases during maturation. In mammals, proline‐specific proteases are not involved in the biosynthesis of regulatory peptides, but due to their unique specificity they could play an important role in the degradation of them. Evidence exists that dipeptidyl (amino)peptidase IV at the cell surface of endothelial cells sequesters circulating peptide hormones which are then susceptible to broader aminopeptidase attack. The cleavage of several neuropeptides by prolyl endopeptidase has been demonstrated in vitro, but its role in the brain is questionable since the precise localization of the protease is not clarified.