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Human Polyclonal SLC26A5 Primary Antibody for ELISA - ABIN449905
Dallos, Wu, Cheatham, Gao, Zheng, Anderson, Jia, Wang, Cheng, Sengupta, He, Zuo: Prestin-based outer hair cell motility is necessary for mammalian cochlear amplification. in Neuron 2008
Motor function is an innovation of therian prestin and is concurrent with diminished transporter capabilities.
Compared with mammalian prestin, charge movements mediated by zprestin display a weaker voltage dependence and slower kinetics; they occur at more positive membrane voltages, and are not associated with electromotile responses.
sequence conservation between mammalian and nonmammalian prestin together with a common pharmacology of electromotility and divalent antiport
Prestin expression imparts susceptibility to 2-hydroxypropyl-beta-cyclodextrin-induced hearing loss.
I hypothesize that serum assays of OHC specific protein, prestin, will allow detection and quantification of OHC damage before audiometric testing can identify presence of hearing loss.
anion-pi interaction is the mechanism for the voltage-dependent response of prestin
The findings suggest that CASK (show CASK Antibodies) and the truncated prestin splice isoform contribute to confinement of prestin to the basolateral region of the plasma membrane.
The effects of fast temperature jumps induced by an infrared (IR) laser in control and prestin (SLC26a5)-transfected human embryonic kidney (HEK (show EPHA3 Antibodies)) cells, are reproted.
Calmodulin-prestin interaction may be involved in the medial olivocochlear-mediated modulation of cochlear amplification
COCH (show COCH Antibodies) and SLC26A5 mRNA are expressed in specific structures and cells of the inner ear in archival human temporal bone
prestin subunits are individually functional within a given multimer
This result implies that in cell membranes prestin oligomerizes to a tetramer.
Four mutations (C124A, C192A, C260A, and C415A), all in nonconserved cysteinyl residues, significantly differed in their nonlinear capacitance properties compared with wild-type prestin.
The IVS2-2A>G mutation in the Slc26a5 gene is insufficient to cause hearing loss in mice.
Prestin missense mutations reduce outer hair cell survival in knockin mice.
demonstrate that OHC lateral wall structure constrains the mobility of plasma membrane proteins and that the integrity of such membrane-associated structures are critical for Slc26a5's active and structural roles
SPAG6 (show SPAG6 Antibodies) is indispensible for the stability of outer hair cells by maintaining the normal expression of prestin
prestin is up-regulated by 32-58% in residual outer hair cell after noise exposure and that the prestin is functional.
calmodulin-prestin interaction may be involved in the medial olivocochlear-mediated modulation of cochlear amplification
Prestin has a role in harnessing the basilar membrane as the source of cochlear frequency tuning.
This gene encodes a member of the SLC26A/SulP transporter family. The protein functions as a molecular motor in motile outer hair cells (OHCs) of the cochlea, inducing changes in cell length that act to amplify sound levels. The transmembrane protein is an incomplete anion transporter, and does not allow anions to cross the cell membrane but instead undergoes a conformational change in response to changes in intracellular Cl- levels that results in a change in cell length. The protein functions at microsecond rates, which is several orders of magnitude faster than conventional molecular motor proteins. Mutations in this gene are potential candidates for causing neurosensory deafness. Multiple transcript variants encoding different isoforms have been found for this gene.
, solute carrier family 26, member 5 (prestin)
, prestin (motor protein)
, solute carrier family 26 member 5
, outer hair cell motor protein
, solute carrier family 26, member 5 (prestin) isoform 1
, solute carrier family 26, member 5 (prestin) isoform 2