H+-coupled nutrient, micronutrient and drug transporters in the mammalian small intestine

Exp Physiol. 2007 Jul;92(4):603-19. doi: 10.1113/expphysiol.2005.029959. Epub 2007 Apr 27.

Abstract

The H(+)-electrochemical gradient was originally considered as a driving force for solute transport only across cellular membranes of bacteria, plants and yeast. However, in the mammalian small intestine, a H(+)-electrochemical gradient is present at the epithelial brush-border membrane in the form of an acid microclimate. Over recent years, a large number of H(+)-coupled cotransport mechanisms have been identified at the luminal membrane of the mammalian small intestine. These transporters are responsible for the initial stage in absorption of a remarkable variety of essential and non-essential nutrients and micronutrients, including protein digestion products (di/tripeptides and amino acids), vitamins, short-chain fatty acids and divalent metal ions. Proton-coupled cotransporters expressed at the mammalian small intestinal brush-border membrane include: the di/tripeptide transporter PepT1 (SLC15A1); the proton-coupled amino-acid transporter PAT1 (SLC36A1); the divalent metal transporter DMT1 (SLC11A2); the organic anion transporting polypeptide OATP2B1 (SLC02B1); the monocarboxylate transporter MCT1 (SLC16A1); the proton-coupled folate transporter PCFT (SLC46A1); the sodium-glucose linked cotransporter SGLT1 (SLC5A1); and the excitatory amino acid carrier EAAC1 (SLC1A1). Emerging research demonstrates that the optimal intestinal absorptive capacity of certain H(+)-coupled cotransporters (PepT1 and PAT1) is dependent upon function of the brush-border Na(+)-H(+) exchanger NHE3 (SLC9A3). The high oral bioavailability of a large number of pharmaceutical compounds results, in part, from absorptive transport via the same H(+)-coupled cotransporters. Drugs undergoing H(+)-coupled cotransport across the intestinal brush-border membrane include those used to treat bacterial infections, hypercholesterolaemia, hypertension, hyperglycaemia, viral infections, allergies, epilepsy, schizophrenia, rheumatoid arthritis and cancer.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Transport Systems / physiology
  • Amino Acid Transport Systems, Neutral / physiology
  • Animals
  • Cation Transport Proteins / physiology
  • Excitatory Amino Acid Transporter 3 / physiology
  • Humans
  • Intestinal Absorption / physiology
  • Intestine, Small / physiology*
  • Membrane Transport Proteins / physiology*
  • Monocarboxylic Acid Transporters / physiology
  • Organic Anion Transporters / physiology
  • Peptide Transporter 1
  • Proton-Coupled Folate Transporter
  • Sodium-Glucose Transporter 1 / physiology
  • Sodium-Hydrogen Exchanger 3
  • Sodium-Hydrogen Exchangers / physiology
  • Symporters / physiology

Substances

  • Amino Acid Transport Systems
  • Amino Acid Transport Systems, Neutral
  • Cation Transport Proteins
  • Excitatory Amino Acid Transporter 3
  • Membrane Transport Proteins
  • Monocarboxylic Acid Transporters
  • Organic Anion Transporters
  • Peptide Transporter 1
  • Proton-Coupled Folate Transporter
  • SLC15A1 protein, human
  • SLC36A1 protein, human
  • SLC46A1 protein, human
  • SLC9A3 protein, human
  • Slc36a1 protein, rat
  • Slc9a3 protein, rat
  • Sodium-Glucose Transporter 1
  • Sodium-Hydrogen Exchanger 3
  • Sodium-Hydrogen Exchangers
  • Symporters
  • monocarboxylate transport protein 1
  • solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2