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We have characterized picomolar affinity binding sites for human calcitonin gene-related peptide (CGRP) in rat brain and heart (atria and ventricle) membranes. By saturation analysis, apparent dissociation constant (KD) values of high affinity sites for [125I]-human CGRP are 9 approximately 15 pM (brain), 34 pM (ventricle) and 85 pM (atria). Low affinity sites with KD values of about 50 nM are found in rat brain and ventricle, but not in atria. Human and rat CGRP potently inhibited [125I]-human CGRP binding to these high affinity sites with apparent inhibition constant (Ki) values comparable to their KD values. Salmon calcitonin marginally inhibited these binding with Ki values between 0.1 microM and 1 microM. Extremely potent cardiovascular and gastrointestinal actions of CGRP might be mediated through CGRP binding sites with picomolar affinity which are similar to those we characterized in this study.
H Yoshizaki, and
M Takamiya, and
T Okada
October 1985,
Brain research,
H Yoshizaki, and
M Takamiya, and
T Okada
July 1995,
Canadian journal of physiology and pharmacology,
H Yoshizaki, and
M Takamiya, and
T Okada
January 1985,
Peptides,
H Yoshizaki, and
M Takamiya, and
T Okada
January 1999,
Peptides,
H Yoshizaki, and
M Takamiya, and
T Okada
May 1986,
Brain research,
H Yoshizaki, and
M Takamiya, and
T Okada
September 1992,
European journal of pharmacology,
H Yoshizaki, and
M Takamiya, and
T Okada
December 1986,
Neuroscience,
H Yoshizaki, and
M Takamiya, and
T Okada
January 1996,
Regulatory peptides,
H Yoshizaki, and
M Takamiya, and
T Okada
December 1985,
Brain research,
H Yoshizaki, and
M Takamiya, and
T Okada
January 1991,
Molecular neurobiology,
