Dalfó E, Albasanz J L, Martin M, Ferrer I
Instituto de Neuropatologia, Servicio de Anatomia Patológica, IDIBELL-Hospital Universitario de Bellvitge, Hospitalet de Llobregat, Spain.
Brain Pathol. 2004 Oct;14(4):388-98. doi: 10.1111/j.1750-3639.2004.tb00082.x.
Diffuse Lewy body disease (DLBD) is a degenerative disease of the nervous system, involving the brain stem, diencephalic nuclei and cerebral cortex, associated with abnormal a-synuclein aggregation and widespread formation of Lewy bodies and Lewy neurites. DLBD presents as pure forms (DLBDp) or in association with Alzheimer disease (AD) in the common forms (DLBDc). Several neurotransmitter abnormalities have been reported including those of the nigrostriatal and mesocorticolimbic dopaminergic system, and central noradrenergic, serotoninergic and cholinergic pathways. The present work examines metabotropic glutamate receptor (mGluR) expression and signaling in the frontal cortex of DLBDp and DLBDc cases in comparison with age-matched controls. Abnormal L-[3H]glutamate specific binding to group I and II mGluRs, and abnormal mGluR1 levels have been found in DLBD. This is associated with reduced expression levels of phospholipase C beta1 (PLCbeta1), the effector of group I mGluRs following protein G activation upon glutamate binding. Additional modification in the solubility of PLCbeta1 and reduced PLCbeta1 activity in pure and common DLBD further demonstrates for the first time abnormal mGluR signaling in the cerebral cortex in DLBD. In order to look for a possible link between abnormal mGluR signaling and a-synuclein accumulation in DLBD, immunoprecipitation studies have shown alpha-synuclein/PLCbeta1 binding in controls and decreased alpha-synuclein/PLCbeta1 binding in DLBD. This is accompanied by a shift in the distribution of a-synuclein, but not of PLCbeta1, in DLBD when compared with controls. Together, these results support the concept that abnormal a-synuclein in DLBD produces functional effects on cortical glutamatergic synapses, which are associated with reduced alpha-synuclein/PLCbeta1 interactions, and, therefore, that mGluRs are putative pharmacological targets in DLBD. Finally, these results emphasize the emergence of a functional neuropathology that has to be explored for a better understanding of the effects of abnormal protein interactions in degenerative diseases of the nervous system.
弥漫性路易体病(DLBD)是一种神经系统退行性疾病,累及脑干、间脑核和大脑皮质,与α-突触核蛋白异常聚集以及路易体和路易神经突的广泛形成有关。DLBD以纯形式(DLBDp)出现,或以常见形式(DLBDc)与阿尔茨海默病(AD)相关联。已报道了几种神经递质异常,包括黑质纹状体和中皮质边缘多巴胺能系统以及中枢去甲肾上腺素能、5-羟色胺能和胆碱能通路的异常。本研究将DLBDp和DLBDc病例额叶皮质中的代谢型谷氨酸受体(mGluR)表达及信号传导与年龄匹配的对照进行比较。在DLBD中发现L-[3H]谷氨酸与I组和II组mGluR的特异性结合异常,以及mGluR1水平异常。这与磷脂酶Cβ1(PLCβ1)的表达水平降低有关,PLCβ1是I组mGluR在谷氨酸结合后通过G蛋白激活的效应器。在纯合型和常见型DLBD中,PLCβ1溶解度的额外改变以及PLCβ1活性降低首次进一步证明了DLBD大脑皮质中mGluR信号传导异常。为了寻找DLBD中mGluR信号传导异常与α-突触核蛋白积聚之间的可能联系,免疫沉淀研究显示对照中有α-突触核蛋白/PLCβ1结合,而DLBD中α-突触核蛋白/PLCβ1结合减少。与对照相比,DLBD中α-突触核蛋白的分布发生了变化,但PLCβ1的分布没有变化。这些结果共同支持了这样一种概念,即DLBD中异常的α-突触核蛋白对皮质谷氨酸能突触产生功能影响,这与α-突触核蛋白/PLCβ1相互作用减少有关,因此,mGluR是DLBD中假定的药理学靶点。最后,这些结果强调了一种功能性神经病理学的出现,必须对其进行探索,以便更好地理解异常蛋白质相互作用在神经系统退行性疾病中的作用。