Key result
Atrial natriuretic factor stimulates endothelial cGMP accumulation via high-affinity ANF-B receptors.
Why the study?
Specific high affinity binding sites for atrial natriuretic factor on bovine pulmonary artery endothelial cells and their receptor subtypes were not fully characterized.
Answers are grounded in this paper and cite their sources.
Suggests endothelial ANF signaling via cGMP; leaves open physiologic role and clinical relevance pending in vivo data.
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.
No takes yet. Share an insight, caveat, or question.
Redmond et al. (1990) studied this question. Atrial natriuretic factor (rANF(99-126)) was evaluated on Identification of specific high affinity binding sites and cGMP accumulation. Atrial natriuretic factor (rANF(99-126)) stimulated a time-dependent rise in cellular cGMP levels in cultured bovine pulmonary artery endothelial cells, with 5-11% of receptors being the ANF-B subtype.
Synapse has enriched 10 related papers. Consider them for comparative context: