Characterisation of a high‐affinity VIP receptor in human lung parenchyma

FEBS Letters

Dickinson, K.E.J.¹  Schachter, M.¹  Sever, P.S.¹  Miles, C.M.¹ 

[1] Department of Clinical Pharmacology, St. Mary's Hospital Medical School, Norfolk Place, London W2, England

关键词: VIP receptor;    (Human lung);    Radioligand binding;    VIP;    vasoactive intestinal peptide;    PHI;    peptide histidine isoleucine;    PHM;    peptide histidine methionine;    PMSF;    phenylmethylsulphonyl fluoride;    GRF;    growth hormone-releasing factor;   

DOI  :  10.1016/0014-5793(86)81237-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A method is described for preparing human lung parenchymal membranes essentially free of carbon contamination. Using this technique, a high-affinity ¹²⁵I-VIP-binding site has been characterised. The receptor density is approx. 200 protein and the K _d of ¹²⁵I-VIP by saturation binding is 200 pM. The dissociation kinetics are complex and cannot be described by first-order kinetics. Several VIP-related peptides displace ¹²⁵I-VIP from this binding site with a rank order of potency: VIP > rat GRF > PHM> PHI > human GRF>secretin>glucagon. Displacement curves of these peptides exhibited slope factors significantly less than unity with the exception of human GRF.

【 授权许可】

Unknown