Regulation of aquaporin-2 water channel trafficking by vasopressin

https://doi.org/10.1016/S0955-0674(97)80034-8Get rights and content

Abstract

Vasopressin regulates water excretion from the kidney by increasing the osmotic water permeability of the renal collecting duct. The aquaporin-2 water channel has been demonstrated to be the target for this action of vasopressin. Recent studies have demonstrated that vasopressin, acting through cyclic AMP, triggers fusion of aquaporin-2-bearing vesicles with the apical plasma membrane of the collecting duct principal cells. The vesicle-targeting protiens synaptobrevin-2 and syntaxin-4 are proposed to play roles in this process.

References (46)

  • M Knepper et al.

    Organization of nephron function

    Am J Physiol

    (1983)
  • MA Knepper

    The aquaporin family of molecular water channels

    Proc Natl Acad Sci USA

    (1994)
  • P Agre et al.

    Aquaporins: a family of water channel proteins

    Am J Physiol

    (1993)
  • K Fushimi et al.

    Cloning and expression of apical membrane water channel of rat kidney collecting tubule

    Nature

    (1993)
  • PM Deen et al.

    Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of the urine

    Science

    (1994)
  • S Nielsen et al.

    Cellular and subcellular immunolocalization of vasopressin-regulated water channel in rat kidney

    Proc Natl Acad Sci USA

    (1993)
  • SJ Lolait et al.

    Cloning and characterization of a vasopressin V2 receptor and possible link to nephrogenic diabetes insipidus

    Nature

    (1992)
  • M Birnbaumer et al.

    Molecular cloning of the receptor for human antidiuretic hormone

    Nature

    (1992)
  • A Seibold et al.

    Structure and chromosomal localization of the human antidiuretic hormone receptor gene

    Am J Hum Genet

    (1992)
  • MA Knepper et al.

    Mechanism of vasopressin action in the renal collecting duct

    Semin Nephrol

    (1994)
  • E Miyamoto et al.

    Cyclic nucleotide-dependent protein kinases. III. Purification and properties of adenosine 3′,5′-monophosphate-dependent protein kinase from bovine brain

    J Biol Chem

    (1969)
  • HM Snyder et al.

    cAMP-dependent protein kinase mediates hydroosmotic effect of vasopressin in collecting duct

    Am J Physiol

    (1992)
  • S Homma et al.

    In situ phosphorylation of proteins in MCTs microdissected from rat kidney: effect of AVP

    Am J Physiol

    (1988)
  • Cited by (132)

    • The role of vasopressin and the vasopressin type V1a receptor agonist selepressin in septic shock

      2017, Journal of Critical Care
      Citation Excerpt :

      Another important role of AVP is water homeostasis. V2 receptor activation leads to water channel aquaphorin 2 expression and translocation in the principal cells of the collecting tubule in the kidney [34,35]. The V2 receptor has also been shown to mediate vasodilation through NO [36,37].

    • Aquaporin expression and localization in the rabbit eye

      2016, Experimental Eye Research
      Citation Excerpt :

      The mRNA expression results obtained by RT-PCR reflect that AQP1 is generally an ubiquitously expressed water channel. AQP2 is modulated by vasopressin (Knepper and Inoue, 1997) and regulates water- and electrolyte balance via the renal collecting ducts (Nielsen et al., 1993a). AQP2 mRNA analysis in ocular tissues did not show the presence of AQP2, although the primers amplified AQP2 mRNA using rabbit kidney total RNA as positive control.

    • NKCC1 and NKCC2: The pathogenetic role of cation-chloride cotransporters in hypertension

      2015, Genes and Diseases
      Citation Excerpt :

      As a consequence of this negative feedback loop, salt delivery to the distal nephron is kept within a narrow range. This process facilitates the fine adjustment of salt handling in the distal tubules by corticosteroids and peptide hormones, such as aldosterone and arginine vasopressin (AVP).42,43 Similar to TAHL, the apical membrane of the MD cells is abundant in NKCC2, which provides up to 80% of apical NaCl entry in these cells.44–46

    View all citing articles on Scopus
    View full text