Dataset Information

Physiological and Pathophysiological Relevance of the Anion Transporter Slc26a9 in Multiple Organs.

ABSTRACT: Transepithelial Cl^- and HCO₃^- transport is crucial for the function of all epithelia, and HCO₃^- is a biological buffer that maintains acid-base homeostasis. In most epithelia, a series of Cl^-/HCO₃^- exchangers and Cl^- channels that mediate Cl^- absorption and HCO₃^- secretion have been detected in the luminal and basolateral membranes. Slc26a9 belongs to the solute carrier 26 (Slc26) family of anion transporters expressed in the epithelia of multiple organs. This review summarizes the expression pattern and functional diversity of Slc26a9 in different systems based on all investigations performed thus far. Furthermore, the physical and functional interactions between Slc26a9 and cystic fibrosis transmembrane conductance regulator (CFTR) are discussed due to their overlapping expression pattern in multiple organs. Finally, we focus on the relationship between slc26a9 mutations and disease onset. An understanding of the physiological and pathophysiological relevance of Slc26a9 in multiple organs offers new possibilities for disease therapy.

SUBMITTER: Liu X

PROVIDER: S-EPMC6127633 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Physiological and Pathophysiological Relevance of the Anion Transporter Slc26a9 in Multiple Organs.

Liu Xuemei X Li Taolang T Tuo Biguang B

Frontiers in physiology 20180828

Transepithelial Cl- and HCO3- transport is crucial for the function of all epithelia, and HCO3- is a biological buffer that maintains acid-base homeostasis. In most epithelia, a series of Cl-/HCO3- exchangers and Cl- channels that mediate Cl- absorption and HCO3- secretion have been detected in the luminal and basolateral membranes. Slc26a9 belongs to the solute car ...[more]

PMID: 30233393

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Project description:Human bronchial epithelial (HBE) cells exhibit constitutive anion secretion that is absent in cells from cystic fibrosis (CF) patients. The identity of this conductance is unknown, but SLC26A9, a member of the SLC26 family of CF transmembrane conductance regulator (CFTR)-interacting transporters, is found in the human airway and exhibits chloride channel behavior. We sought differences in the properties of SLC26A9 and CFTR expressed in HEK 293 (HEK) cells as a fingerprint to identify HBE apical anion conductances. HEK cells expressing SLC26A9 displayed a constitutive chloride current that was inhibited by the CFTR blocker GlyH-101 (71 +/- 4%, 50 microM) and exhibited a near-linear current-voltage (I-V) relation during block, while GlyH-101-inhibited wild-type (wt)CFTR exhibited a strong inward-rectified (IR) I-V relation. We tested polarized HBE cells endogenously expressing either wt or DeltaF508-CFTR for similar activity. After electrical isolation of the apical membrane using basolateral alpha-toxin permeabilization, wtCFTR monolayers displayed constitutive chloride currents that were inhibited by GlyH-101 (68 +/- 6%) while maintaining a near-linear I-V relation. In the absence of blocker, the addition of forskolin stimulated a current increase having a linear I-V; GlyH-101 blocked 69 +/- 7% of the current and shifted the I-V relation IR, consistent with CFTR activation. HEK cells coexpressing SLC26A9 and wtCFTR displayed similar properties, as well as forskolin-stimulated currents that exceeded the sum of those in cells separately expressing SLC26A9 or wtCFTR, and an I-V relation during GlyH-101 inhibition that was moderately IR, indicating that SLC26A9 contributed to the stimulated current. HBE cells from CF patients expressed SLC26A9 mRNA, but no constitutive chloride currents. HEK cells coexpressing SLC26A9 with DeltaF508-CFTR also failed to exhibit SLC26A9 current. We conclude that SLC26A9 functions as an anion conductance in the apical membranes of HBE cells, it contributes to transepithelial chloride currents under basal and cAMP/protein kinase A-stimulated conditions, and its activity in HBE cells requires functional CFTR.

Dataset Information

Physiological and Pathophysiological Relevance of the Anion Transporter Slc26a9 in Multiple Organs.

Publications

Physiological and Pathophysiological Relevance of the Anion Transporter Slc26a9 in Multiple Organs.

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