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Parvalbumin (PV) is a cytosolic Ca 2+ -binding protein acting as a slow-onset Ca 2+  buffer modulating the shape of Ca 2+  transients in fast-twitch muscles and a subpopulation of neurons. PV is also expressed in non-excitable cells including distal convoluted tubule (DCT) cells of the kidney, where it might act as an intracellular Ca 2+  shuttle facilitating transcellular Ca 2+  resorption. In excitable cells, upregulation of mitochondria in “PV-ergic” cells in PV-/- mice appears to be a general hallmark, evidenced in fast-twitch muscles and cerebellar Purkinje cells. Using Gene Chip Arrays and qRT-PCR, we identified differentially expressed genes in the DCT of PV-/- mice. With a focus on genes implicated in mitochondrial Ca 2+  transport and membrane potential, uncoupling protein 2 ( Ucp2 ), mitocalcin ( Efhd1 ), mitochondrial calcium uptake 1 ( Micu1 ), mitochondrial calcium uniporter ( Mcu ), mitochondrial calcium uniporter regulator 1 ( Mcur1 ), cytochrome c oxidase subunit 1 ( COX1 ), and ATP synthase subunit β ( Atp5b ) were found to be up-upregulated. At the protein level, COX1 was increased by 31 ± 7%, while ATP-synthase subunit β was unchanged. This suggested that these mitochondria were better suited to uphold the electrochemical potential across the mitochondrial membrane, necessary for mitochondrial Ca 2+  uptake. Ectopic expression of PV in PV-negative Madin-Darby canine kidney (MDCK) cells decreased COX1 and concomitantly mitochondrial volume, while ATP synthase subunit β levels remained unaffected. Suppression of PV by shRNA in PV-expressing MDCK cells led subsequently to an increase in COX1 expression. The collapsing of the mitochondrial membrane potential by the uncoupler CCCP occurred at lower concentrations in PV-expressing MDCK cells than in control cells. In support, a reduction of the relative mitochondrial mass was observed in PV-expressing MDCK cells. Deregulation of the cytoplasmic Ca 2+  buffer PV in kidney cells was counterbalanced  in vivo  and  in vitro  by adjusting the relative mitochondrial volume and modifying the mitochondrial protein composition conceivably to increase their Ca 2+ -buffering/sequestration capacity.

Antagonistic Regulation of Parvalbumin Expression and Mitochondrial Calcium Handling Capacity in Renal Epithelial Cells