SLC26A6

SLC26A6, also known as Pendrin-related transporter or PAT1, is a protein encoded by the SLC26A6 gene in humans. It is a member of the SLC26 family of anion exchangers, a group of membrane transport proteins that facilitate the exchange of various anions across cell membranes.

Specifically, SLC26A6 primarily functions as a chloride/bicarbonate (Cl-/HCO3-) exchanger. This means it transports chloride ions into the cell in exchange for bicarbonate ions moving out, or vice versa, depending on the electrochemical gradients. It can also transport other anions such as oxalate and sulfate, though the affinity for these may vary.

SLC26A6 is expressed in several tissues, with notable expression in the kidney and intestine. In the kidney, it plays a vital role in regulating chloride reabsorption and bicarbonate secretion in the proximal tubule, contributing to overall acid-base balance and fluid homeostasis. In the intestine, it contributes to chloride absorption and bicarbonate secretion, affecting intestinal pH and electrolyte balance, and is thought to be involved in fluid secretion and stool consistency.

Mutations in the SLC26A6 gene have been associated with several disorders. These include increased risk of kidney stone formation (nephrolithiasis), potentially due to altered oxalate transport in the kidney. Furthermore, alterations in intestinal chloride and bicarbonate transport due to SLC26A6 dysfunction can contribute to gastrointestinal problems, particularly constipation and diarrhea. Studies have also suggested a potential role for SLC26A6 in cystic fibrosis-related gastrointestinal issues, as its function can be affected by defects in the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) protein.

The precise regulation and physiological importance of SLC26A6 continue to be areas of active research. Its role in multiple organ systems and its association with specific diseases make it an important target for understanding ion transport mechanisms and developing potential therapeutic interventions.