Carbonic anhydrases are enzymes that catalyze the reversible hydration of carbon dioxide according to the following reaction:

CO₂ + H₂O ↔ HCO₃^– + H⁺

The main function of this protein family is to regulate the acid-base balance, which is of considerable biological importance. In addition, they participate in several other physiological functions including CO2 and HCO3- transport, bone resorption, production of biological fluids, ureagenesis, gluconeogenesis, and lipogenesis. CAs are metalloenzymes containing a zinc-atom in their active site, whereas CARPs do not bind zinc because they lack some of the critical histidine residues which are critical for zinc binding.

The expanding alpha CA gene family includes 13 enzymatically active members with different structural and catalytic properties.  Each isoform has a characteristic distribution in tissues.

We have previously shown that CA II, VII, IX and XII are expressed in various malignant tissues. Based on the distribution and functional studies, they may play a role in neoplastic processes such as invasion and increased cell proliferation. We have also demonstrated that Car9 defect in mouse results in a gastric phenotype with significant hyperplasia in the gastric epithelium. More recently, we have produced a novel knockout mouse model for CA VI deficiency.

Recently our studies have extended to cover other gene families of carbonic anhydrase including, importantly, the beta carbonic anhydrases.  This family is present in a number of species while absent in mammals, providing a potential therapeutic target for certain diseases.