Daigle I, Li C
Department of Biology, Boston University, MA 02215.
Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):12045-9. doi: 10.1073/pnas.90.24.12045.
The major component of senile plaques found in the brains of Alzheimer disease patients is the beta-amyloid peptide, which is derived from a larger amyloid precursor protein (APP). Recently, a number of APP and APP-related proteins have been identified in different organisms and constitute the family of APP proteins. We have isolated several cDNAs encoding an APP-related protein in the nematode Caenorhabditis elegans and have designated the corresponding gene as apl-1. The apl-1 transcripts undergo two forms of posttranscriptional modification: trans-splicing and alternative polyadenylylation. In vitro translation of an apl-1 cDNA results in a protein of approximately the expected size. Similar to the Drosophila, human, and mouse APP-related proteins, APL-1 does not appear to contain the beta-amyloid peptide. Because APP-related proteins seem to be conserved through evolution, the apl-1 gene from C. elegans should be important for determining the normal function of human APP.
在阿尔茨海默病患者大脑中发现的老年斑的主要成分是β-淀粉样肽，它来源于一种更大的淀粉样前体蛋白（APP）。最近，在不同生物体中鉴定出了许多APP及与APP相关的蛋白质，它们构成了APP蛋白家族。我们在秀丽隐杆线虫中分离出了几个编码与APP相关蛋白的cDNA，并将相应的基因命名为apl-1。apl-1转录本经历两种形式的转录后修饰：反式剪接和可变聚腺苷酸化。对apl-1 cDNA进行体外翻译会产生一种大小约为预期的蛋白质。与果蝇、人类和小鼠的APP相关蛋白类似，APL-1似乎不包含β-淀粉样肽。由于APP相关蛋白似乎在进化过程中是保守的，秀丽隐杆线虫的apl-1基因对于确定人类APP的正常功能应该很重要。
