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Séminaire Chimie ED459

Carbonic anhydrase IX as a target for rational design of antitumoral drugs

Dr. Giuseppina De Simone (Sr. Researcher, Instituto di Biostrutture e Bioimmmagini – CNR, Napoli, Italy)

publié le

Le Jeudi 27 Septembre 2012 à 13h45
UM2, salle de cours SC-16.01

Carbonic anhydrases (CAs) are ubiquitous enzymes, which catalyze the simplest physiological reaction, the inter-conversion of the carbon dioxide in bicarbonate ions. In humans fifteen CA isoforms have been described with very different sub-cellular localizations and tissue distributions. These isoforms have different physiological functions and their absence or their malfunctioning can cause several pathologies. As a consequence, in the last years CA isozymes have become interesting targets for pharmaceutical research. However, most of the available CA-directed pharmacological agents are still far from being optimal drugs. They present various non-desired side-effects, mainly because of their lack of selectivity for the different CA isozymes. Thus, developing isozyme-specific CA inhibitors should be highly beneficial in obtaining novel classes of drugs.

hCA IX is a membrane-associated member of this enzyme family. It has recently been demonstrated that an aberrant increase in its expression in chronic hypoxia and during development of various carcinomas contributes to tumorigenesis through at least two mechanisms : pH regulation and cell adhesion control. In this lecture the molecular and catalytic features of this enzyme, the role of its different domains in tumor physiology, and its three dimensional structure, which has recently been solved, will be described together with recent advances in the rational drug design of CA IX-specific inhibitors.

Contact local IBMM : Dr. Jean-Yves Winum


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