Mechanisms of cell polarity and aquaporin sorting in the nephron

Pflugers Arch. 2011 Jun;461(6):607-21. doi: 10.1007/s00424-011-0928-3. Epub 2011 Feb 16.

Abstract

The kidneys participate in whole-body homeostasis, regulating acid-base balance, electrolyte concentrations, extracellular fluid volume, and regulation of blood pressure. Many of the kidney's functions are accomplished by relatively simple mechanisms of filtration, reabsorption, and secretion, which take place in the nephron. The kidneys generate 140-180 l of primary urine per day, while reabsorbing a large percentage, allowing for only the excretion of approximately 2 l of urine. Within the nephron, the majority of the filtered water and solutes are reabsorbed. This is mainly facilitated by specialized transporters and channels which are localized at different segments of the nephron and asymmetrically localized within the polarized epithelial cells. The asymmetric localization of these transporters and channels is essential for the physiological tasks of the renal tissues. One family of these proteins are the water-permeable aquaporins which are selectively expressed in cells along the nephron and localized at different compartments. Here, we discuss potential molecular links between mechanisms involved in the establishment of cell polarity and the members of the aquaporin family. In the first part of this review, we will focus on aspects of apical cell polarity. In the second part, we will review the motifs identified so far that are involved in aquaporin sorting and point out potential molecular links.

Publication types

  • Review

MeSH terms

  • Animals
  • Aquaporins / physiology*
  • Cell Polarity / physiology*
  • Epithelial Cells / physiology
  • Eye Proteins / physiology
  • Humans
  • Membrane Proteins / physiology
  • Nephrons / metabolism*
  • Nerve Tissue Proteins / physiology
  • Nucleoside-Phosphate Kinase / physiology
  • Tight Junction Proteins

Substances

  • Aquaporins
  • CRB1 protein, human
  • Eye Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • PATJ protein, human
  • Tight Junction Proteins
  • Nucleoside-Phosphate Kinase
  • MPP5 protein, human