Nakajima K, Nagata K, Hamanoue M, Takemoto N, Shimada A, Kohsaka S
Department of Neurochemistry, National Institute of Neuroscience, Tokyo, Japan.
FEBS Lett. 1993 Nov 1;333(3):223-8. doi: 10.1016/0014-5793(93)80658-h.
To investigate the receptor-like molecule(s) for plasminogen (PGn) on the neuronal surface, the properties of binding of PGn to the plasma membrane of cultured embryonic rat neocortical neurons were investigated. [125I]PGn was found to specifically bind to the plasma membrane depending on the incubation temperature and time. The binding was also affected strongly by ionic strength and slightly by Ca2+. Furthermore, ligand blotting analysis revealed that [125I]PGn binds to a major protein with an apparent molecular weight of 45 kDa among plasma membrane proteins. These results suggest that the 45-kDa protein is a PGn receptor-like molecule on the neuronal surface.
为了研究神经元表面纤溶酶原（PGn）的受体样分子，对PGn与培养的胚胎大鼠新皮质神经元质膜的结合特性进行了研究。发现[125I]PGn根据孵育温度和时间特异性结合质膜。结合也受到离子强度的强烈影响，并受到Ca2+的轻微影响。此外，配体印迹分析显示，[125I]PGn在质膜蛋白中与一种表观分子量为45 kDa的主要蛋白质结合。这些结果表明，45 kDa蛋白是神经元表面的一种PGn受体样分子。
