Chen M, Yankner B A
Department of Neurology, Harvard Medical School, Boston, MA.
Neurosci Lett. 1991 Apr 29;125(2):223-6. doi: 10.1016/0304-3940(91)90034-q.
An epitope-specific antibody directed against the first 16 amino acids of the beta amyloid protein (anti-BP16) immunoprecipitated the secreted form of the amyloid precursor protein (APP) from the conditioned medium of PC12 cells. This antibody caused neurite retraction in differentiated PC12 cells and inhibited cell-substratum adhesion in many neuronal and non-neuronal cell types. The inhibitory effect of anti-BP16 was abolished by preabsorption of the antibody with BP16 peptide. Antibodies directed against other domains of APP did not inhibit cell adhesion. The secreted form of APP may be important for cell adhesion in many different mammalian cell types.
一种针对β淀粉样蛋白前16个氨基酸的表位特异性抗体(抗BP16)从PC12细胞的条件培养基中免疫沉淀出淀粉样前体蛋白(APP)的分泌形式。该抗体导致分化的PC12细胞中神经突回缩,并在许多神经元和非神经元细胞类型中抑制细胞与底物的粘附。用BP16肽预先吸附该抗体可消除抗BP16的抑制作用。针对APP其他结构域的抗体不抑制细胞粘附。APP的分泌形式可能对许多不同哺乳动物细胞类型中的细胞粘附很重要。