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Polyclonal SLC26A5 Primary Antibody for ELISA - ABIN539856
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
results show, for the first time, that the substitution of a span of 11 amino acid residues confers the electrogenic anion transporters of zebrafish and chicken prestins with motor-like function
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
extracellular loop of pendrin and prestin modulates their voltage-sensing property
Our study thus provides experimental evidence that supports a causal relationship between the R130S mutation in the prestin gene and hearing loss found in patients with this missense mutation.
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 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) cells, are reproted.
Calmodulin-prestin interaction may be involved in the medial olivocochlear-mediated modulation of cochlear amplification
COCH 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.
These data reveal that the STAS (sulfate transporters and anti-sigma factor antagonist) domain starts immediately after the last transmembrane segment and lies beneath the lipid bilayer.
Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin
an essential function of prestin in human auditory processing
KCNQ4 phosphorylation via PKA and coupling to a complex that may include prestin can lead to the negative activation and the negative resting potential found in adult outer hair cells.
Because mammals possess differentiated outer hair cells (OHC), they also benefit from a novel electromotile process, powered by the motor protein, prestin.
Packing of helices and interactions between residues surrounding the sulfate transporter motif is essential for normal prestin activity.
This is the first genetic and electrophysiological analysis of a human mutation in a coding exon of the pres gene by 47 patients with non-syndromic, sensorineural, mild-to-moderate hearing impairment.
Cholesterol levels modulate the distribution of prestin within plasma membrane microdomains and affect prestin self-association
response of endogenously expressed prestin in HEI-OC1 cells is different from the response of prestin expressed exogenously in non-auditory cells
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 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.
prestin knockout mice had increased auditory threshold but no changes in spine density or morphological characteristics on apical dendrites of auditory cortical layer 5 pyramidal neurons.
A previously unexpected role of prestin, in mediating antibiotic-induced apoptosis, the effect of which is associated with its anion-transporting capacity.
a molecular mechanism of prestin with at least two voltage-dependent conformational transition steps having distinct electromechanical coupling efficiencies.
Data show that two prestin monomers are expressed on the cell surface, but only one is functional, that prestin dimerization is leads to increased voltage sensitivity, and that prestin maturation results in a depolarizing shift in voltage operating range.
These data suggest that VAPA could be involved in prestin's transportation inside outer hair cells (OHCs) and may facilitate the targeting of this abundant OHC protein to the plasma membrane.
Interaction between CFTR and prestin (SLC26A5).
Results suggest that the majority of the intra-membrane protein particles are prestin and that electrically evoked length and stiffness changes are interrelated and dependent on both prestin and on the cortical actin cytoskeletal lattice.
targeted deletion of prestin in mice results in loss of outer hair cell electromotility in vitro and a 40-60 dB loss of cochlear sensitivity in vivo, without disruption of mechano-electrical transduction in outer hair cells
Genomic characterization and expression of mouse prestin
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