CA XIV

Carbonic anhydrase XIV (CA XIV) is a membrane-bound carbonic anhydrase first isolated from mouse kidney, and human CA14 was cloned and mapped as a distinct gene^[1][2]. It supports CO₂/HCO₃⁻ conversion, linking extracellular acid-base regulation with bicarbonate handling in kidney, brain, retina, and skeletal muscle models^{[3][4][5][6][7][8][9]}. Mechanistically, CA XIV contributes to extracellular buffering in brain and interacts with the AE3 Cl⁻/HCO₃⁻ exchanger, connecting enzyme activity to bicarbonate homeostasis in excitable tissues^[5][8]. In disease-relevant models, CA XIV deficiency caused a functional defect in the retinal light response, while retinal studies localized CA XIV to retinal pigment epithelium, Müller cells, and astrocytes^[6][7]. Compared with related isoforms, CA XIV differs from CA IV in brain buffering roles and from CA XIII/XV by being a membrane-associated isoform with distinct characterization and inhibition profiles^[5][10]. For experimental applications, sulfonamides, natural polyphenols, and phenolic acids provide inhibitor classes for comparing CA XIV with mammalian isoforms I-XIV^[10][11].