Wienecke R, Maize J C, Shoarinejad F, Vass W C, Reed J, Bonifacino J S, Resau J H, de Gunzburg J, Yeung R S, DeClue J E
Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, Maryland 20892-4040, USA.
Oncogene. 1996 Sep 5;13(5):913-23.
Tuberin is the protein product of the tuberous sclerosis-2 (TSC2) gene, which is associated with tuberous sclerosis (TSC), a human genetic syndrome characterized by the development of tumors in a variety of tissues. We have previously shown that tuberin is a widely expressed 180 kDa protein which exhibits specific GTPase activating activity in vitro towards the Ras-related Rap1 protein. In this study we have used affinity-purified antibodies against tuberin to analyse its expression in human and rat tissues and to examine its subcellular localization. Tuberin expression was detected in all adult human tissues tested, with the highest levels found in brain, heart and kidney, organs that are commonly affected in TSC patients. By contrast, in adult rats the highest levels of tuberin were found in brain, liver and testis. Indirect immunofluorescence of tuberin in various cultured cell lines revealed a punctate, mostly perinuclear staining pattern. Double-indirect immunofluorescence analysis with anti-tuberin sera and antisera against known Golgi markers (mannosidase-II and furin) revealed that the staining of tuberin was consistent with its localization in the stacks of the Golgi apparatus. In support of this, treatment of cells with brefeldin A, a drug known to cause disassembly of the Golgi apparatus, abolished the perinuclear staining of tuberin. Moreover, conventional and confocal immunofluorescence demonstrated co-localization of tuberin with Rap1, which has previously been localized to the Golgi apparatus. The co-localization of tuberin and Rap1 in vivo strengthens the likelihood that the in vitro catalytic activity of tuberin toward Rap1 plays a physiologically relevant role in the tumor suppressor function of tuberin.
结节蛋白是结节性硬化症2(TSC2)基因的蛋白质产物,该基因与结节性硬化症(TSC)相关,TSC是一种人类遗传综合征,其特征是在多种组织中发生肿瘤。我们之前已经表明,结节蛋白是一种广泛表达的180 kDa蛋白质,在体外对与Ras相关的Rap1蛋白具有特定的GTP酶激活活性。在本研究中,我们使用针对结节蛋白的亲和纯化抗体来分析其在人和大鼠组织中的表达,并检查其亚细胞定位。在所有测试的成人组织中均检测到结节蛋白表达,在脑、心脏和肾脏中发现的水平最高,这些器官在TSC患者中通常会受到影响。相比之下,在成年大鼠中,结节蛋白水平最高的是脑、肝脏和睾丸。在各种培养细胞系中对结节蛋白进行间接免疫荧光显示出点状、主要是核周染色模式。用抗结节蛋白血清和针对已知高尔基体标志物(甘露糖苷酶-II和弗林蛋白酶)的抗血清进行双间接免疫荧光分析表明,结节蛋白的染色与其在高尔基体堆叠中的定位一致。支持这一点的是,用布雷菲德菌素A(一种已知会导致高尔基体解体的药物)处理细胞,消除了结节蛋白的核周染色。此外*,*传统免疫荧光和共聚焦免疫荧光都证明了结节蛋白与Rap1共定位,Rap1此前已被定位到高尔基体。结节蛋白和Rap1在体内的共定位增加了结节蛋白对Rap1的体外催化活性在结节蛋白的肿瘤抑制功能中发挥生理相关作用的可能性。