Abstract

Human carbonic anhydrase VII (hCA VII) is a cytosolic isoform belonging to the α-CA family that shows high carbon dioxide hydration activity. Recently, S-glutathionylation of two cysteine residues (i.e., Cys183 and Cys217) of this protein was observed, suggesting that hCA VII could act as an oxygen radical scavenger, in addition to its well-established role in pH regulation. hCA VII has also been reported to be involved in the initial postnatal phases of brain development, as well as in the generation of neuronal excitation and febrile seizures; thus, its inhibition could represent a promising approach in designing new pharmacological agents useful for controlling such pathological conditions. The resolution of hCA VII crystal structure, together with the availability of inhibition data on different inhibitor classes, provide important perspectives in the drug design of CA-selective inhibitors.

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