Gandy S E, Buxbaum J D, Suzuki T, Ramabhadran T V, Caporaso G L, Nairn A C, Greengard P
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.
Neurobiol Aging. 1992 Sep-Oct;13(5):601-3. doi: 10.1016/0197-4580(92)90063-4.
The proteolytic processing and secretion of APP are regulated by protein phosphorylation, especially via protein kinase C and protein phosphatases 1 and/or 2A. Our studies of these regulatory mechanisms have led us to perform extensive experimentation on the metabolism of APP carboxyl-terminal fragments, using as our system either untransfected, undifferentiated rat pheochromocytoma (PC12) cells or APP-baculovirus infected Sf9 cells. We have not assayed APP fragments for biological activity in either system. However, we have made potentially relevant observations regarding APP carboxyl-terminal fragment trafficking. In this note, we review our published and unpublished data in relation to published reports from other laboratories using related systems.
APP的蛋白水解加工和分泌受蛋白质磷酸化调节,尤其是通过蛋白激酶C以及蛋白磷酸酶1和/或2A。我们对这些调节机制的研究促使我们对APP羧基末端片段的代谢进行广泛实验,使用未转染、未分化的大鼠嗜铬细胞瘤(PC12)细胞或感染APP杆状病毒的Sf9细胞作为我们的系统。我们尚未在任一系统中检测APP片段的生物活性。然而,我们已经对APP羧基末端片段的运输做出了潜在相关的观察。在本报告中,我们结合其他实验室使用相关系统发表的报告,回顾我们已发表和未发表的数据。