Kometani M, Sato T, Fujii T
Thromb Res. 1986 May 15;42(4):567-77. doi: 10.1016/0049-3848(86)90220-3.
Membrane-interacting amphiphiles, lysophosphatidylcholine, cepharanthine and chlorpromazine, inhibited concanavalin A (Con A)-induced platelet activation in a dose-dependent manner, as judged by the inhibition of serotonin release. These amphiphiles did not influence the binding of Con A to surface membrane glycoproteins. Marked increase in the amount of the cytoskeletal proteins, myosin, actin and actin-binding protein, in the Triton-insoluble residue of the Con A-activated platelets, as well as in the surface membrane glycoproteins with molecular weights of 224,000, 201,000, 119,000 and 92,000 found in the same residue, was inhibited by any of the three amphiphiles in a dose-dependent manner. Such inhibitory effect, however, was abolished when the amphiphiles were washed out from the platelets before the activation. These findings suggest that these membrane-interacting amphiphiles may inhibit the Con A-induced assembly of the cytoskeletal proteins and their association with surface membrane glycoproteins, probably by physically altering the membrane properties.
膜相互作用两亲物、溶血磷脂酰胆碱、千金藤素和氯丙嗪以剂量依赖性方式抑制伴刀豆球蛋白A（Con A）诱导的血小板活化，这通过5-羟色胺释放的抑制来判断。这些两亲物不影响Con A与表面膜糖蛋白的结合。Con A活化血小板的Triton不溶性残渣中细胞骨架蛋白、肌球蛋白、肌动蛋白和肌动蛋白结合蛋白的量显著增加，以及在同一残渣中发现的分子量为224,000、201,000、119,000和92,000的表面膜糖蛋白的量显著增加，均被三种两亲物中的任何一种以剂量依赖性方式抑制。然而，当在活化前将两亲物从血小板中洗脱时，这种抑制作用就消失了。这些发现表明，这些膜相互作用两亲物可能通过物理改变膜性质来抑制Con A诱导的细胞骨架蛋白组装及其与表面膜糖蛋白的结合。
