Rat renal preglomerular vessels, glomeruli and papillae do not express detectable quantities of B-type natriuretic peptide receptor.
METHODS
Atrial natriuretic factor (ANF) receptor subtypes were quantitated by radioligand studies in three different rat renal isolated tissues: preglomerular vessels, glomeruli and papillae.


RESULTS
In preglomerular vessels 100% of [125I]-ANF binding was displaced with high affinity by ANF. C-ANF (des-[Gln18,Ser19,Gly20,Leu21,Gly22]ANP(4- 23)) a specific ligand for ANP-C receptors, displaced 30% of total binding with a lower affinity than ANF. C-type natriuretic peptide (CNP) displaced [125I]-ANF binding in a biphasic manner, indicating that it binds to two sites with affinities three orders of magnitude apart. When CNP was incubated in the presence of 0.1 mumol/l C-ANF to saturate ANP-C receptors, the high-affinity binding site vanished and maximum binding decreased to 70%, suggesting that CNP binds with high affinity to ANP-C receptors. Since the ANP-A receptor has little or no avidity for CNP, it is probably the low-affinity binding site. CNP and C-ANF displaced most [125I]-[Tyr]CNP(1-22) binding with very close affinities, indicating that CNP binds primarily preglomerular vascular ANP-C receptors. In glomeruli CNP behaved similarly to C-ANF in its ability to displace approximately 85% of [125I]-ANF binding; the remaining 15% was completely displaced by ANF. C-ANF and CNP inhibited 100% of [125I]-[Tyr]CNP(1-22) binding. Both findings suggest that [125I]-[Tyr]CNP(1-22) binds ANP-C receptors exclusively. In renal papillae no displacement of [125I]-ANF by C-ANF was observed, and CNP was bound to ANP-A receptors with the same very low affinity as in preglomerular vessels. The absence of [125I]-[Tyr]CNP(1-22) binding to papillary membranes indicates that ANP-B receptors are not expressed in that tissue. Unlike ANF, CNP stimulated cGMP production in glomeruli and papillae only at extremely high, supraphysiological concentrations.


CONCLUSIONS
The present results suggest that ANP-B receptors either are absent or are present in undetectable amounts in rat renal preglomerular vessels, glomeruli and papillae.
de Leon
H
H
Laboratory of Experimental Hypertension and Vasoactive Peptides, Clinical Research Institute of Montreal, Quebec, Canada.
Bonhomme
M C
MC
Garcia
R
R
D000818:Animals; D009320:Atrial Natriuretic Factor / Q000378:metabolism; D001667:Binding, Competitive; D006152:Cyclic GMP / Q000096:biosynthesis; D007678:Kidney Glomerulus / Q000098:blood supply* / Q000378:metabolism*; D007679:Kidney Medulla / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D017461:Receptors, Atrial Natriuretic Factor / Q000378:metabolism*; D012079:Renal Circulation
C080026:C-type natriuretic peptide (1-22), Tyr(0)-; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; C058930:brain natriuretic peptide receptor; D009320:Atrial Natriuretic Factor; D017461:Receptors, Atrial Natriuretic Factor; D006152:Cyclic GMP