Disease relevance of Slc26a5

• Results from F3-F5 generation mice suggest that one copy of the prestin gene is capable of compensating for the deleted copy and that heterozygous mice do not suffer peripheral hearing impairment [1].

High impact information on Slc26a5

• Prestin, a member of the solute carrier family 26, is expressed in the basolateral membrane of outer hair cells [2].
• We investigated possible quaternary structures of prestin by lithium dodecyl sulfate-PAGE, perfluoro-octanoate-PAGE, a membrane-based yeast two-hybrid system, and chemical cross-linking experiments [2].
• Chemical cross-linking experiments, perfluoro-octanoate-PAGE/Western blot, and affinity purification experiments all indicate that prestin exists as a higher order oligomer, such as a tetramer, in prestin-expressing yeast, mammalian cell lines and native outer hair cells [2].
• In addition, both immunocytochemistry and western blot analysis in young adult mice suggest that prestin protein in heterozygotes is near normal [1].
• Although the cochlear microphonic in knockout mice remains approximately 12 dB below that in wild-type mice even at the highest levels, this deficit is thought to reflect hair cell losses in mice lacking prestin [3].

Biological context of Slc26a5

• The prestin open reading frames are 91% identical at the nucleotide level [4].
• Gross-potential recordings in mice lacking the Prestin gene indicate that compound action potential (CAP) thresholds are shifted by approximately 45 dB at 5 kHz and by approximately 60 dB at 33 kHz [3].
• Experiments were designed to determine if the deletion in the reeler mouse affects the coding and/or regulatory regions for the expression of prestin, the outer hair cell motor protein [5].
• We report here that in prestin-/- mice, no significant hair-cell loss occurred before postnatal day 28 (P28); apoptosis of hair cells began at P28; and the loss of inner hair cells lagged behind that of OHCs [6].
• Because reelin and prestin genes are located close together on mouse chromosome 5, reelin homozygous mutant mice were compared with littermate controls [5].

Anatomical context of Slc26a5

• Genomic characterization and expression of mouse prestin, the motor protein of outer hair cells [4].
• Using an antibody raised against the N-terminus of gerbil Prestin, we observed mPrestin expression by immunofluorescence in the lateral membrane of mouse OHCs and found no detectable expression elsewhere in the organ of Corti [4].
• Prestin expression in the cochlea of the reeler mouse [5].
• However, in the VHCs, staining of varying intensity with anti-prestin antibodies was observed in the cytoplasm, but not in the lateral plasma membrane or in the stereociliary membrane [7].
• In situ hybridization and immunolocalization studies confirmed the presence of prestin in OHCs as well as in vestibular hair cells (VHCs) of rodent saccule, utricle and crista ampullaris [7].

Physical interactions of Slc26a5

• Promyelocytic leukemia zinc finger protein localizes to the cochlear outer hair cells and interacts with prestin, the outer hair cell motor protein [8].

Analytical, diagnostic and therapeutic context of Slc26a5

• The interaction between endogenous prestin and PLZF proteins in the cochlea was confirmed by co-immunoprecipitation using organ of Corti lysates [8].
• Creation of a transgenic mouse for hair-cell gene targeting by using a modified bacterial artificial chromosome containing Prestin [9].
• In this experiment, the distribution of prestin in adult mouse, rat, and guinea pig OHCs was re-examined by use of immunofluorescent staining and confocal microscopy [10].

References