Also, although internal Ca 2+ levels modulate motility, the ions themselves do not participate in this activity. OHC electromotility has several salient features, and obtains its energy supply via changing membrane potential instead of ATP hydrolysis. SLC26A5 inactivation in mammals resulted in a loss of OHC somatic motility in vitro and a 40–60 dB loss of cochlear sensitivity in vivo. This mechanical activity is believed to feed back into the vibration of the cochlear partition, thereby enhancing the mechanical stimulus of IHCs.
Electromotility as a central mechanism in the mammalian inner ear is unique to the OHCs and absent in the inner hair cells (IHCs).
Prestin is localized in the lateral wall of outer hair cells (OHCs) and is a membrane-based motor protein that powers electromotility. While comparing to its orthologs, the amphibian prestin has been evolutionarily changing its function and becomes more advanced than avian and teleost prestin. This new coding gene could encode a functionally active protein conferring NLC to both frog HCs and the mammalian cell line. The Rana SLC26A5 cDNA was 2292 bp long, encoding a polypeptide of 763 amino acid residues, with 40% identity to mammals. We mapped and sequenced the SLC26A5 of the Rana catesbeiana from its inner ear cDNA using RNA-Seq. Ancient frog’s prestin was functionally different from Rana. Comparative studies of zebrafish, chick, Rana and an ancient frog species showed that chick and zebrafish prestin lacked NLC. HEK293T cells expressing Rana prestin showed electrophysiological features similar to that of hair cells from its inner ear. We measured the nonlinear capacitance (NLC) of prestin both in the hair cells of Rana’s inner ear and HEK293T cells transfected with this new coding gene. In our study, the SLC26A5 gene of Rana has been mapped, sequenced and cloned successively using RNA-Seq. Here we report a new coding sequence of SLC26A5 for a frog species, Rana catesbeiana (the American bullfrog). Frog prestin is the only representative in amphibian lineage and the studies of it were quite rare with only one species identified. Limited knowledge of prestin is from experiments using site-directed mutagenesis or domain-swapping techniques after the amino acid residues were identified by comparing the sequence of prestin to those of its paralogs and orthologs. So if you’re looking to engage in rewarding research that’s having a positive global impact – apply for a PhD with Monash IT today.Prestin (SLC26A5) is responsible for acute sensitivity and frequency selectivity in the vertebrate auditory system.
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