Developmental expression of palmitoyl protein thioesterase in normal mice
Developmental expression of palmitoyl protein thioesterase in normal mice
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DOI：
10.1016/s0165-3806(99)00115-7
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发表时间：
1999-12-10
期刊：
影响因子：
--
通讯作者：
Peltonen, L
中科院分区：
文献类型：
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作者：
Isosomppi, J;Heinonen, O;Peltonen, L
棕榈酰蛋白硫酯酶(PPT)的缺失导致人类新皮质神经元的迅速死亡。人们对这种溶酶体酶的发育和细胞特异性表达知之甚少。在这里，我们表明PPT在小鼠大脑中表达为一个主要的2.65kb和一个次要的1.85kb的转录本。转录水平在出生后第10天到第30天之间逐渐增加。原位杂交分析表明，PPT转录本在大脑中广泛存在，但并不是同质性的。大脑皮质(II、IV-V层)、海马CA1-CA3区锥体细胞、齿状回颗粒细胞和下丘脑的信号最强。PPT免疫染色定位于胞体、轴突和树突，尤其是海马锥体细胞和颗粒细胞，与突触前囊泡膜蛋白突触素的免疫反应在空间和时间上都有很好的相关性。在整个胚胎中，在胚胎第8天，PPT mRNA的表达在整个神经上皮细胞中最为明显。从第9天起，它在所有组织中都可见。PPT的表达模式表明其对脑细胞的普遍意义，并反映了神经网络的成熟和生长的反应。轴突和树突中强烈的PPT免疫反应提示PPT可能不只是一种溶酶体酶。与突触素的显著相关性表明，PPT可能在突触机制的功能中发挥作用。(C)1999 Elsevier Science B.V.保留所有权利。
Deficiency in palmitoyl protein thioesterase (PPT) results in the rapid death of neocortical neurons in human. Very little is known about the developmental and cell-specific expression of this lysosomal enzyme. Here we show that PPT is expressed as a major 2.65 kb and a minor 1.85 kb transcript in the mouse brain. Transcript levels gradually increase between postnatal days 10 and 30. In situ hybridization analysis revealed that PPT transcripts are found widely but nor homogeneously in the brain. The most intense signal was detected in the cerebral cortex (layers II, IV-V), hippocampal CA1-CA3 pyramidal cells, dentate gyrus granule cells and the hypothalamus. Immunostaining of PPT was localized in the cell soma, axons and dendrites, especially in the pyramidal and granular cells of the hippocampus, correlating well, both spatially and temporally, with the immunoreactivity of a presynaptic vesicle membrane protein, synaptophysin. In whole embryos, at embryonic day 8, the PPT mRNA expression was most apparent throughout the neuroepithelium. and from day 9 onwards it was seen in all tissues. The expression pattern of PPT suggests its general significance for the brain cells and reflects the response to maturation and growth of the neural networks. Strong PPT immunoreactivity in the axons and dentrites would imply that PPT may not be exclusively a lysosomal enzyme. A notable correlation with synaptophysin would suggest that PPT may have a role in the function of the synaptic machinery. (C) 1999 Elsevier Science B.V. All rights reserved.