Journal
PHYSIOLOGICAL AND BIOCHEMICAL ZOOLOGY
Volume 79, Issue 6, Pages 981-996Publisher
UNIV CHICAGO PRESS
DOI: 10.1086/507658
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Despite all the efforts and technological advances during the last few decades, the cellular mechanisms for branchial chloride uptake in freshwater (FW) fish are still unclear. Although a tight 1 : 1 link with HCO3- secretion has been established, not much is known about the identity of the ion-transporting proteins involved or the energizing steps that allow for the inward transport of Cl- against the concentration gradient. We propose a new model for Cl- uptake in FW fish whereby the combined action of an apical anion exchanger, cytoplasmic carbonic anhydrase, and basolateral V-type H+-ATPase creates a local high enough to energize Cl- uptake. Our model is [HCO3-] based on analyses of structure-function relationships, reinterpretation of previous results, and novel observations about gill cell subtypes and immunolocalization of the V-H+-ATPase.
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