Parks Annette L, Curtis Daniel
Biology Department, Boston College, Chestnut Hill, MA 02467, USA.
Trends Genet. 2007 Mar;23(3):140-50. doi: 10.1016/j.tig.2007.01.008. Epub 2007 Feb 5.
Presenilin, the catalytic member of the gamma-secretase proteolytic complex, was discovered through its roles in generating Alzheimer's-disease-associated amyloid-beta peptides from the amyloid-beta precursor protein and in releasing the transcriptionally active domain of the receptor Notch. Recent work has revealed many additional cleavage substrates and interacting proteins, suggesting a diversity of roles for presenilin during development and adult life, some of which might contribute to Alzheimer's disease progression. Although many of these functions depend on the proteolytic activity of gamma-secretase, others are independent of its role as a protease. Here, we review recent data on candidate functions for presenilin and its interactors and on their potential significance in disease.
早老素是γ-分泌酶蛋白水解复合物的催化成员，它是通过在从淀粉样前体蛋白生成与阿尔茨海默病相关的淀粉样β肽以及释放受体Notch的转录活性结构域中所起的作用而被发现的。最近的研究揭示了许多其他的切割底物和相互作用蛋白，这表明早老素在发育和成年期具有多种作用，其中一些作用可能会促进阿尔茨海默病的进展。尽管这些功能中的许多都依赖于γ-分泌酶的蛋白水解活性，但其他功能则与其作为蛋白酶的作用无关。在这里，我们综述了关于早老素及其相互作用分子的候选功能及其在疾病中的潜在意义的最新数据。
