Walaas S I, Browning M D, Greengard P
laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.
J Neurochem. 1988 Oct;51(4):1214-20. doi: 10.1111/j.1471-4159.1988.tb03089.x.
The regional and cellular distribution of four synaptic vesicle-associated proteins, synapsins Ia and Ib (Mr 86,000 and 80,000, collectively referred to as synapsin I) and proteins IIIa and IIIb (Mr 74,000 and 55,000, collectively referred to as protein III), has been compared in selected rat brain regions, using both radioimmunoassays and back-phosphorylation assays. Lesions of several neuronal populations in the basal ganglia (corticostriatal fibers, intrinsic striatal neurons, striatonigral fibers, nigrostriatal fibers) induced decreases in the levels of these various proteins that were highly correlated (r = 0.96-0.97). Moreover, the synaptic vesicle-associated phosphoproteins displayed a similar and widespread distribution throughout the CNS. This evidence for colocalization indicates that the majority of, and possibly all, CNS neurons and nerve terminals may contain both forms of synapsin I and both forms of protein III.
利用放射免疫测定法和反向磷酸化测定法,在选定的大鼠脑区中,比较了四种突触小泡相关蛋白,即突触结合蛋白Ia和Ib(分子量分别为86,000和80,000,统称为突触结合蛋白I)以及蛋白IIIa和IIIb(分子量分别为74,000和55,000,统称为蛋白III)的区域和细胞分布。基底神经节中几个神经元群体(皮质纹状体纤维、纹状体内在神经元、纹状体黑质纤维、黑质纹状体纤维)的损伤导致这些不同蛋白水平下降,且高度相关(r = 0.96 - 0.97)。此外,突触小泡相关磷蛋白在整个中枢神经系统中呈现相似且广泛的分布。这种共定位的证据表明,大多数甚至可能所有的中枢神经系统神经元和神经末梢可能同时含有两种形式的突触结合蛋白I和两种形式的蛋白III。