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Corneal dystrophy mutations R125H and R804H disable SLC4A11 by altering the extracellular pH dependence of the intracellular pK that governs H⁺(OH^-) transport.

ABSTRACT: Mutations in the H⁺(OH^-) conductor SLC4A11 result in corneal endothelial dystrophy. In previous studies using mouse Slc4a11, we showed that the pK value that governs the intracellular pH dependence of SLC4A11 (pK_i) is influenced by extracellular pH (pH_e). We also showed that some mutations result in acidic or alkaline shifts in pK_i, indicating that the pH dependence of SLC4A11 is important for physiological function. An R125H mutant, located in the cytosolic amino terminus of SLC4A11, apparently causes a complete loss of function, yet the anion transport inhibitor 4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid (DIDS) can partially rescue SLC4A11/R125H activity. In the present study we set out to determine whether the effect of R125H

SUBMITTER: Quade BN

PROVIDER: S-EPMC9484998 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature

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Corneal dystrophy mutations R125H and R804H disable SLC4A11 by altering the extracellular pH dependence of the intracellular pK that governs H⁺(OH^-) transport.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Corneal dystrophy mutations R125H and R804H disable SLC4A11 by altering the extracellular pH dependence of the intracellular pK that governs H+(OH-) transport.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Corneal dystrophy mutations R125H and R804H disable SLC4A11 by altering the extracellular pH dependence of the intracellular pK that governs H⁺(OH^-) transport.