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Dipeptidyl peptidase IV and its implication in cancer

Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5), also known as CD26, is a serine aminopeptidase that preferentially cleaves Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of oligopeptides and processes regulatory peptides in vivo, leading to their biological activation or inactivation. The ezyme is a homodimer and each subunit is formed by a ab-hydrolase domain and a b-propeller domain, involved in the enzymatic activity and its interaction with other proteins. It has an important role in multiple physiological functions, including the regulation of glucose metabolism being one of the current targets for the treatment of type II diabetes mellitus. This enzyme also regulates immune system responses mediated by CD4+ T lymphocytes, and recently has been identified a high/low DPP-IV activity regarding physiological levels, in pathologies like thyroid, ovarian, lung, skin, prostate cancers and central nervous system tumors. For these reasons, this enzyme evolves as a new target of attention for the development of more efficient diagnostics being considering as molecular markers for some pathologies and a target for the development of new therapeutic assessments in cancer. Current research interests are focused on depth in the structure-function relation for this enzyme, as a key point for the development of new therapies in pathologies involving DPP-IV activity or its interaction with other proteins.