Prestin

Prestin is the motor protein of the outer hair cells of the inner ear of the mammalian cochlea [cite web |url=http://www.nature.com/nature/journal/v405/n6783/abs/405149a0.html |title=Prestin is the motor protein of cochlear outer hair cells |accessdate=2007-02-17 |last=Zheng |first=Jing |coauthors=Weixing Shen, David Z. Z. He, Kevin B. Long, Laird D. Madison, Peter Dallos |date=2000-05-11 |work=Nature |pages=pp. 149-155 (405)] . It is highly expressed in the outer hair cells, and is not expressed in the nonmotile inner hair cells. Immunolocalization shows prestin is expressed in the lateral plasma membrane of the outer hair cells, the region where electromotility occurs. The expression pattern correlates with the appearance of outer hair cell electromotility.

Prestin (mol. wt. 80 kDa) is a member of a distinct family of anion transporters, SLC26. Members of this family are structurally well conserved and can mediate the electroneutral exchange of chloride and carbonate across the plasma membrane of mammalian cells, two anions found to be essential for outer hair cell motility. Unlike the classical, enzymatically driven motors, the function of this new type of motor is based on direct voltage-to-displacement conversion. It acts several orders of magnitude faster than cellular motor proteins. A targeted gene disruption strategy of prestin showed a >100-fold (or 40 dB) loss of auditory sensitivity [cite web |url=http://www.nature.com/nature/journal/v419/n6904/abs/nature01059.html |title=Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier |accessdate=2007-02-17 |last=Liberman |first=M. Charles |coauthors=Jiangang Gao, David Z. Z. He, Xudong Wu, Shuping Jia, Jian Zuo |date=2002-08-28 |work=Nature |pages=pp. 300-304 (419)] .

Prestin was discovered and named by Jing Zheng "et al." in 2000 from the musical notation presto.

The prestin molecule was patented in 2003 [cite web |url=http://space.newscientist.com/article.ns?id=dn11158&print=true |title=Motion-sensitive spacesuits could generate power |accessdate=2007-02-17 |last=Young |first=Kelly |date=2007-02-14 |work=NewScientist.com news service] .

Electromotile function of mammalian prestin is blocked by the amphiphilic anion salicylate at millimolar concentrations. Application of salicylate via the extracellular solution blocked transport currents in a dose-dependent and readily reversible manner.

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