Krebs K E, Zagon I S, Goodman S R
Department of Physiology, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey 17033.
J Neurosci. 1987 Dec;7(12):3907-14. doi: 10.1523/JNEUROSCI.07-12-03907.1987.
An immunoreactive, structural, and functional analog of erythrocyte protein 4.1 is present in neuronal cell bodies and dendrites. Other investigators have described the isolation of a 4.1 analog in brain with structural characteristics suggesting that its identity was synapsin I, a neuronal phosphoprotein localized in the presynaptic terminal in association with small synaptic vesicles. In this report we demonstrate that the cell body/dendritic form of brain protein 4.1, which we have named amelin, is distinct from that of synapsin I on the basis of subcellular localization, migration in 2-dimensional gel electrophoresis, and structural criteria. We also demonstrate that amelin, like synapsin I, can bind brain spectrin on nitrocellulose paper. Neither amelin nor synapsin I binds calmodulin, as determined by a blot binding assay. We hypothesize that there exists in brain a family of 4.1-related proteins with distinct subcellular localization and function.
红细胞蛋白4.1的一种具有免疫反应性、结构和功能的类似物存在于神经元细胞体和树突中。其他研究者描述了在脑中分离出一种4.1类似物，其结构特征表明它是突触素I，一种定位于突触前终末并与小突触小泡相关的神经元磷蛋白。在本报告中，我们证明，基于亚细胞定位、二维凝胶电泳迁移和结构标准，我们命名为amelin的脑蛋白4.1的细胞体/树突形式与突触素I不同。我们还证明，amelin与突触素I一样，能在硝酸纤维素纸上结合脑血影蛋白。通过印迹结合试验确定，amelin和突触素I均不结合钙调蛋白。我们推测，脑中存在一个具有不同亚细胞定位和功能的4.1相关蛋白家族。
