1992
DOI: 10.1152/ajpregu.1992.263.4.r747
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Atrial natriuretic factor binding sites in rat area postrema: autoradiographic study

Abstract: The area postrema (AP) is a brain stem circumventricular organ implicated, among other functions, in central cardiovascular (CV) regulation. Competition binding analysis performed by quantitative in vitro autoradiography demonstrated specific, high-affinity (Kd, 0.32 +/- 0.11 nM), low-capacity (Bmax, 57.5 +/- 10.9 fmol/mg protein) atrial natriuretic factor (ANF) binding sites in the AP. C-ANF [des-(Gln116-Gly120)ANF-(Arg102-Cys121)-NH2] and ANF-(Phe106-Ile113)-NH2 (two ligands endowed with selectivity for the … Show more

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Cited by 4 publications
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“…In particular, the area postrema has natriuretic peptide binding sites with pharmacological characteristics of the NP A and NP B but not the NP C receptor subtypes. 25 Commonalities in central connections of cardiopulmonary mechanosensitive and chemosensitive afferent pathways make this an interesting possibility, although there is no evidence yet either for or against it.…”
Section: Discussionmentioning
confidence: 99%
“…In particular, the area postrema has natriuretic peptide binding sites with pharmacological characteristics of the NP A and NP B but not the NP C receptor subtypes. 25 Commonalities in central connections of cardiopulmonary mechanosensitive and chemosensitive afferent pathways make this an interesting possibility, although there is no evidence yet either for or against it.…”
Section: Discussionmentioning
confidence: 99%
“…The literature confirms that several of the identified receptors are expressed in the AP, such as the angiotensin II type 1a receptor ( Agtr1a ; Lenkei et al 1998; Huang et al 2003), vasopressin 1a receptor ( V1aR ; Tribollet et al 1999; Yang et al 2006), atrial natriuretic peptide receptor a and b ( Npr1/2 ; Konrad et al 1992 a , b ), prolactin receptor ( Prlr ; Mangurian et al 1999), neuropeptide Y1 ( Nyp1r ) and Y5 ( Nyp5r ) receptors (Dumont et al 1996; Dumont et al 1998 a , b ), glucagon‐like peptide‐1 receptor ( Glpr ; Price et al 2008), cannabinoid 1 receptor ( Cnr1 ; Partosoedarso et al 2003), adiponectin receptor ( AdipoR1/R2 ; Fry et al 2006) and receptor activity modifying protein (RAMP) mRNAs 1, 2 and 3 (Ueda et al 2001). While these RAMPs are not strictly receptors, they are accessory proteins that confer receptor specificity; for example, all three RAMPs heterodimerize with the calcitonin receptor to form three different receptors for amylin, a hormone co‐secreted with insulin (Christopoulos et al 1999; Muff et al 1999).…”
Section: Discussionmentioning
confidence: 85%