Characterization of vasopressin receptors of rat urinary bladder and spleen
By use of tritiated arginine-8-vasopressin (AVP), vasopressin specific binding sites were detected on Sprague-Dawley rat urinary bladder and spleen. In both tissues, one class of high-affinity binding sites was characterized with an equilibrium dissociation constant of 1.61 +/- 0.22 and 1.91 nM and a maximal binding capacity of 155 and 110 fmol/mg of protein, for bladder and spleen, respectively. In both tissues, several experimental arguments suggest that these receptors belong to the V/sub 1/-vascular type. AVP (10/sup -12/-10/sup -5/ M) did not modify the basal cyclic AMP production in either tissue. As cyclic AMP is known to respond to V/sub 2/ stimulation, the data suggest that the receptors measured are the V/sub 1/ type. The exploration of vasopressin receptors regulation should facilitate the comprehension of the role played by AVP in different models of experimental hypertension.
- Research Organization:
- Medical College of Ohio, Toledo
- OSTI ID:
- 6790146
- Journal Information:
- Am. J. Physiol.; (United States), Vol. 251:1
- Country of Publication:
- United States
- Language:
- English
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RECEPTORS
MOLECULAR STRUCTURE
VASOPRESSIN
RADIORECEPTOR ASSAY
AMP
BLADDER
HYPERTENSION
RATS
SPLEEN
ANIMALS
BODY
CARDIOVASCULAR DISEASES
DISEASES
HORMONES
ISOTOPE APPLICATIONS
MAMMALS
MEMBRANE PROTEINS
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANS
PEPTIDE HORMONES
PITUITARY HORMONES
PROTEINS
RODENTS
SYMPTOMS
TRACER TECHNIQUES
URINARY TRACT
VASCULAR DISEASES
VERTEBRATES
550601* - Medicine- Unsealed Radionuclides in Diagnostics