Karniguian A, Legrand Y J, Lefrancier P, Caen J P
Thromb Res. 1983 Dec 15;32(6):593-604. doi: 10.1016/0049-3848(83)90061-0.
The interaction of platelets with collagen involves short aminoacid sequences which recur along the fibres. Platelet aggregation by collagen and serotonin release is inhibited by a synthetic octapeptide LYS-PRO-GLY-GLU- PRO-GLY-PRO-LYS- derived from type III collagen. In contrast, this octapeptide inhibits only weakly the retention of platelets labelled with 111Indium to collagen, suggesting that it has a limited effect on platelet adhesion. Preincubation of the octapeptide with platelets inhibits the rise of cAMP level caused by activating adenylate cyclase by various concentrations of PGI2. The octapeptide at 5 mM reverses the inhibition by PGI2 of the adhesion of platelets to collagen. These results suggest that the octapeptide affects the intrinsic activity (manifested as platelet aggregation and secretion) more than the recognition of collagen by its receptor (manifested by adhesion).
血小板与胶原蛋白的相互作用涉及沿纤维反复出现的短氨基酸序列。源自III型胶原蛋白的合成八肽LYS-PRO-GLY-GLU-PRO-GLY-PRO-LYS可抑制胶原蛋白诱导的血小板聚集和5-羟色胺释放。相比之下，该八肽仅微弱抑制用铟-111标记的血小板与胶原蛋白的结合，表明其对血小板黏附的影响有限。八肽与血小板预温育可抑制不同浓度前列环素（PGI2）激活腺苷酸环化酶所引起的环磷酸腺苷（cAMP）水平升高。5 mM的八肽可逆转PGI2对血小板与胶原蛋白黏附的抑制作用。这些结果表明，八肽对内在活性（表现为血小板聚集和分泌）的影响大于其受体对胶原蛋白的识别（表现为黏附）。
