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- W295655498 abstract "Atrial natriuretic factor (ANF) interacts with at least two distinct receptors to produce various biological effects. The two receptors that bind ANF with similar affinities can be differentiated by molecular mass. The larger receptor, termed the R1 or B receptor, generates cyclic guanosine monophosphate (cGMP) on stimulation with ANF; moreover, cloning studies have identified it as a particulate guanylate cyclase. The smaller receptor is identified as the R2 or clearance receptor, existing as a monomer or a dimer. The R2 receptor specifically binds the truncated ANF derivative, ANF–NH2(cANF), whereas this analog does not activate the R1 receptor. Therefore, cANF has been utilized in numerous studies to identify specific ANF binding to the R1 receptor and to displace binding from the R2 receptor. Moreover, cANF mimics the effects of ANF on peripheral sympathetic neurons to suppress the evoked catecholamine release and adenylate cyclase activity in a manner similar to ANF. These results suggest that the R2 receptor is the biologically functional ANF receptor in the peripheral sympathetic nervous system. Methods for the identification of neuronal ANF receptors involve: (1) binding of labeled cANF to membranes, (2) coupling of [125I]ANF to receptors with subsequent identification of R1 or R2 receptors by molecular mass, and (3) utilizing cANF to displace selectively ANF binding to the R2 receptor." @default.
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- W295655498 date "1993-01-01" @default.
- W295655498 modified "2023-09-25" @default.
- W295655498 title "Atrial Natriuretic Factor Binding to Clearance Receptors in Isolated Neuronal Membranes" @default.
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- W295655498 doi "https://doi.org/10.1016/b978-0-12-185275-7.50012-3" @default.
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