Regional Distribution of Calcitonin Gene-Related Peptide and Its Specific Binding Sites in Rats with Particular Reference to the Nervous System

1987 ◽  
Vol 46 (2) ◽  
pp. 131-136 ◽  
Author(s):  
Sunil J. Wimalawansa ◽  
Piers C. Emson ◽  
lain Maclntyre
1995 ◽  
Vol 73 (7) ◽  
pp. 1084-1088 ◽  
Author(s):  
D. van Rossum ◽  
D. P. Ménard ◽  
R. Quirion ◽  
J. K. Chang

Adrenomedullin (ADM) is a recently identified peptide that shows some homology (~ 25%) with calcitonin gene related peptide (CGRP) and is now considered to be a new member of this peptide family. Because it shares biological effects with CGRP, we evaluated the possible affinity of human adrenomedullin (hADM) for 125I-labelled human CGRPα ([125I]hCGRPα) binding sites in the rat brain. Moreover, we evaluated the potential existence of cross-reactivity for 125I-labelled Bolton–Hunter rat amylin ([125I]BHrAMY), another member of this peptide family. In all brain areas investigated, hADM only competed with relatively low affinities for both [125I]hCGRPα and [125I]BHrAMY binding sites, with IC50 values generally in the high nanomolar – low micromolar range, the lowest affinity being observed for [125I]BHrAMY binding sites. Interestingly, the lowest affinities of hADM against both radioligands were detected in the nucleus accumbens and ventral striatum. These areas are known to be enriched with atypical CGRP – salmon calcitonin – amylin sensitive sites. It thus appears that hADM is unlikely to bind to this atypical site. Moreover, hADM demonstrated limited affinity for either [125I]hCGRPα or [125I]BHrAMY binding sites in the rat brain. This suggests that the potential biological effects of ADM in the brain could be mediated through a different class of receptors with higher affinity for this newly isolated peptide.Key words: adrenomedullin, calcitonin gene related peptide, amylin, rat brain.


1993 ◽  
Vol 84 (1) ◽  
pp. 55-60 ◽  
Author(s):  
Bing Sun ◽  
Anthony P. Davenport ◽  
Morris J. Brown

1. Binding sites for calcitonin-gene-related peptide were localized and characterized in porcine coronary arteries using quantitative autoradiography, and the density of binding sites was compared between large epicardial and small intramyocardial coronary arteries. 2. A single class of binding sites for calcitonin-gene-related peptide with a dissociation constant of 2.1 ± 0.2 nmol/l was detected in both the large and small coronary arteries. The density of specific binding sites was higher (maximum binding site density 231 ± 14 fmol/mg of protein) in the small coronary arteries than in the large epicardial coronary arteries (maximum binding site density 108 ± 5 fmol/mg of protein). β-Human calcitonin-gene-related peptide showed higher affinity than α-human calcitonin-gene-related peptide for the binding sites. Most of the specific binding sites for both peptides in the large coronary artery were localized in the intima and media. 3. In coronary artery from patients with coronary heart disease, there were more binding sites for calcitonin-gene-related peptide in the smooth muscle layer of atheromatous segments (7.2 ± 0.7 amol/mm2) than in that of normal segments (3.0 ± 0.3 amol/mm2, P < 0.002). 4. The present findings lend further support to the theory of regional variation in the vasodilator response to calcitonin-gene-related peptide in porcine coronary arteries, which seems to be due to different densities of a single type of receptor for calcitonin-gene-related peptide.


1988 ◽  
Vol 463 (2) ◽  
pp. 223-244 ◽  
Author(s):  
Lawrence Kruger ◽  
Patrick W. Mantyh ◽  
Catia Sternini ◽  
Nicholas C. Brecha ◽  
Christopher R. Mantyh

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