Urny Jens, Hermans-Borgmeyer Irm, Gercken Günther, Schaller H Chica
Zentrum für Molekulare Neurobiologie, Universität Hamburg, Martinistr 52, 20246, Hamburg, Germany.
Gene Expr Patterns. 2003 Oct;3(5):685-91. doi: 10.1016/s1567-133x(03)00094-2.
Recently, a new member of the presenilin family was identified as an aspartyl protease that cleaves signal peptides within hydrophobic domains, and was, therefore, named signal peptide peptidase (SPP). We isolated cDNAs coding for mouse and human orthologues of SPP. The human gene spans 55 kilobases on chromosome 20q11.21. The SPP-protein is encoded in mouse and man by 12 exons. The highly conserved intron/exon-structure in the SPP/presenilin family hints at a common precursor. Northern blot and in situ hybridization analysis revealed a widespread expression of SPP in many tissues. A distinct pattern of expression in the mature murine brain and during development indicates that SPP plays an important role in the establishment and maintenance of the nervous system. We prepared an antiserum against the carboxy-terminal domain of SPP, which is highly conserved between species. It reacted specifically, both in western blots and in immunocytochemical preparations, with SPP from various mammalian origins. The antiserum was used to demonstrate that SPP is oriented in the membrane of the endoplasmic reticulum with its carboxy-terminal tail extending into the cytosol.
最近，早老素家族的一个新成员被鉴定为一种天冬氨酸蛋白酶，它能在疏水结构域内切割信号肽，因此被命名为信号肽酶（SPP）。我们分离出了编码小鼠和人类SPP直系同源物的cDNA。人类基因位于20号染色体q11.21上，跨度为55千碱基。SPP蛋白在小鼠和人类中由12个外显子编码。SPP/早老素家族中高度保守的内含子/外显子结构提示存在一个共同的前体。Northern印迹和原位杂交分析显示SPP在许多组织中广泛表达。在成熟小鼠大脑和发育过程中的独特表达模式表明，SPP在神经系统的建立和维持中起重要作用。我们制备了一种针对SPP羧基末端结构域的抗血清，该结构域在物种间高度保守。在蛋白质印迹和免疫细胞化学制剂中，它都能与来自各种哺乳动物的SPP发生特异性反应。该抗血清被用于证明SPP在内质网膜中的取向是其羧基末端尾巴延伸到细胞质中。
