Magous R, Bali J P, Escale R, Girard J P, Rechencq E, Rossi J C
Mol Pharmacol. 1986 Jan;29(1):39-44.
Using human blood-washed platelets and [3H]indomethacin, we demonstrated the presence of saturable, time- and temperature-dependent high affinity binding sites for non-steroidal anti-inflammatory drugs. The observed Kd value for indomethacin was 5 nM. Structural specificity of the non-steroidal anti-inflammatory drug site was studied with arylacetic acids, anthranilic acids, and compounds from other chemical families. Arylacetic acid drugs had affinities which were similar to the affinity of indomethacin. Affinity differences among the other drugs may be related to the presence or absence of the lipophilic substituent on the central ring. As expected, anti-inflammatory pyrrazole derivatives, aspirin, bucloxic acid, cortisol, nordihydroguaiaretic acid, and the chemotactic peptide formyl-Met-Leu-Phe were not recognized by the indomethacin binding site.
我们使用人洗过的血小板和[3H]吲哚美辛，证明了存在可饱和的、时间和温度依赖性的非甾体抗炎药高亲和力结合位点。观察到的吲哚美辛的Kd值为5 nM。用芳基乙酸、邻氨基苯甲酸和其他化学家族的化合物研究了非甾体抗炎药位点的结构特异性。芳基乙酸类药物的亲和力与吲哚美辛的亲和力相似。其他药物之间的亲和力差异可能与中心环上亲脂性取代基的存在与否有关。正如预期的那样，抗炎吡唑衍生物、阿司匹林、布氯酸、皮质醇、去甲二氢愈创木酸和趋化肽甲酰甲硫氨酰亮氨酰苯丙氨酸不被吲哚美辛结合位点识别。
