Atrial natriuretic factor recognizes two receptor subtypes in endothelial cells cultured from bovine pulmonary artery

FEBS Lett. 1990 Aug 20;269(1):157-62. doi: 10.1016/0014-5793(90)81143-c.

Abstract

In this study specific high affinity binding sites for atrial natriuretic factor (rANF(99-126] have been identified on cultured endothelial cells of bovine pulmonary artery origin (BPAEC). A time-dependent rise in cellular cGMP levels stimulated by rANF(99-126) was followed by release of the nucleotide into the incubation medium. The use of truncated, ring-deleted and linear atrial peptide analogs in competitive displacement analysis and measurement of cGMP accumulation indicated that only a minor proportion (5-11%) of the available receptor pool was of the ANF-B receptor subtype, linked to guanylate cyclase, with the remaining major proportion possibly of the ANF-C (clearance) receptor subtype. The existence of two ANF receptor subtypes in this cell culture model would suggest a significant role for the circulating peptide in modulation of pulmonary endothelial cell function, which would influence or complement its direct actions on the underlying vasculature of the pulmonary circulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Atrial Natriuretic Factor / metabolism*
  • Binding, Competitive
  • Cattle
  • Cells, Cultured
  • Cyclic GMP / biosynthesis
  • Endocytosis
  • Endothelium, Vascular / metabolism*
  • Guanylate Cyclase / metabolism
  • Pulmonary Artery
  • Receptors, Atrial Natriuretic Factor
  • Receptors, Cell Surface / classification
  • Receptors, Cell Surface / metabolism*
  • Structure-Activity Relationship
  • Time Factors

Substances

  • Receptors, Cell Surface
  • Atrial Natriuretic Factor
  • Guanylate Cyclase
  • Receptors, Atrial Natriuretic Factor
  • Cyclic GMP