CA VII

Carbonic Anhydrase VII (CA VII) is a cytosolic zinc metalloenzyme of the α-carbonic anhydrase family that catalyzes the reversible hydration of carbon dioxide to bicarbonate and protons, thereby contributing to intracellular pH regulation and neuronal acid-base homeostasis^[1][2]. CA VII is highly relevant in the nervous system, where neuronal expression supports bicarbonate-dependent signaling mechanisms and influences GABAergic neurotransmission through regulation of intracellular bicarbonate availability^[3]. Mechanistically, CA VII facilitates the generation of bicarbonate ions that can enhance depolarizing GABA responses under conditions of elevated neuronal activity, linking carbon dioxide metabolism to neuronal excitability and network function^[3]. In experimental models, neuronal CA VII expression has been associated with susceptibility to febrile seizures, supporting its relevance to epilepsy-related research and studies of neuronal hyperexcitability^[3]. Compared with related cytosolic isoforms such as CA II, CA VII exhibits a more restricted neuronal expression pattern, making it particularly valuable for investigating brain-specific carbonic anhydrase functions and disease mechanisms^[3][4]. This isoform distinction has stimulated efforts to develop selective CA VII inhibitors because nonselective inhibition of multiple carbonic anhydrase isoforms may produce unwanted off-target effects^[5][6]. Accordingly, structure-based drug discovery and crystallographic studies have identified CA VII as a promising target for the development of isoform-selective inhibitors for neurological disorders, particularly epilepsy and other central nervous system diseases^[5][6].