RGD Reference Report - Mammalian prestin is a weak Cl⁻/HCO₃⁻ electrogenic antiporter. - Rat Genome Database

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Mammalian prestin is a weak Cl⁻/HCO₃⁻ electrogenic antiporter.

Authors: Mistrík, P  Daudet, N  Morandell, K  Ashmore, J F 
Citation: Mistrík P, etal., J Physiol. 2012 Nov 15;590(22):5597-610. doi: 10.1113/jphysiol.2012.241448. Epub 2012 Aug 13.
RGD ID: 158013775
Pubmed: PMID:22890707   (View Abstract at PubMed)
PMCID: PMC3528980   (View Article at PubMed Central)
DOI: DOI:10.1113/jphysiol.2012.241448   (Journal Full-text)

The lateral membrane of mammalian cochlear outer hair cells contains prestin, a protein which can act as a fast voltage-driven actuator responsible for electromotility and enhanced sensitivity to sound. The protein belongs to the SLC26 family of transporters whose members are characterised as able to exchange halides for SO(4)(2-) or HCO(3)(-) yet previous analyses of mammalian prestin have suggested that such exchange functions were minimal. Here anion transport is investigated both in guinea-pig outer hair cells (OHCs) and in an expression system where we employ a sensitive intracellular pH (pH(i)) probe, pHluorin, to report HCO(3)(-) transport and to monitor the small pH(i) changes observable in the cells. In the presence of extracellular HCO(3)(-), pH(i) recovered from an acid load 4 times faster in prestin-transfected cells. The acceleration required a chloride gradient established by reducing extracellular chloride to 2 mm. Similar results were also shown using BCECF as an alternative pH(i) sensor, but with recovery only found in those cells expressing prestin. Simultaneous electrophysiological recording of the transfected cells during bicarbonate exposure produced a shift in the reversal potential to more negative potentials, consistent with electrogenic transport. These data therefore suggest that prestin can act as a weak Cl(-)/HCO(3)(-) antiporter and it is proposed that, in addition to participating in wide band cochlear sound amplification, prestin may also be involved in the slow time scale (>10 s) phenomena where changes in cell stiffness and internal pressure have been implicated. The results show the importance of considering the effects of the endogenous bicarbonate buffering system in evaluating the function of prestin in cochlear outer hair cells.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
bicarbonate transport involved_inIDA 158013775PMID:22890707UniProt 
chloride transport involved_inIDA 158013775PMID:22890707UniProt 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
chloride:bicarbonate antiporter activity enablesIDA 158013775PMID:22890707UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Slc26a5  (solute carrier family 26 member 5)


Additional Information