阿尔茨海默病中Tau蛋白与相关分子作用的探究

doi:10.3969/j.issn.1674-490X.2014.03.019

摘要/Abstract

摘要： 阿尔茨海默病(Alzheimer's disease, AD)是一种致死性神经退行性脑病，细胞外间隙β淀粉样蛋白（Aβ）沉积形成的老年斑以及细胞内过度磷酸化Tau蛋白聚集形成的神经原纤维缠结（NFTs）是其主要特征性病变。Tau蛋白的异常与阿尔茨海默病的神经变性和记忆认知减退密切相关。而Tau蛋白与相关分子的相互作用进一步促进了阿尔茨海默病的发生发展。本文综述了Tau蛋白与Aβ、14-3-3ζ、p62在阿尔茨海默病中的相互联系和作用。

关键词: 阿尔茨海默病, Tau蛋白, Aβ, 14-3-3ζ, p62

Abstract: Alzheimer's disease (AD) is a fatal neurodegenerative brain disease. The senile plaques formed by Aβamyloids’ sedimentary in extracellular space and intracellular neuroifbrillary tangles(NFTs) formed by excessive phosphate Tau protein aggregation are the main characteristic lesions. The abnormal Tau protein is closely related to the neurodegeneration and the decline of cognitive abnormalities of AD. The interaction between Tau protein and related molecules has further promoted the occurrence and development of AD. This paper reviews the interactions and relationships between Tau protein and Aβ, 14-3-3ζ, p62 in AD.

Key words: Alzheimer's disease, Tau protein, Aβ, 14-3-3ζ, p62

中图分类号:

李艳霞,曹梦媛,李艳萌,张庆云,邵海锐,董晓东. 阿尔茨海默病中Tau蛋白与相关分子作用的探究[J]. 医学研究与教育, 2014, 31(3): 72-75,87.

LI Yanxia,CAO Mengyuan,LI Yanmeng,ZHANG Qingyun,SHAO Hairui,DONG Xiaodong. The exploration between Tau protein and related molecules in Alzheimer’s disease[J]. Medical Reserch and Education, 2014, 31(3): 72-75,87.

参考文献

[1] RHEIN V, SONG X, WIESNER A. Amyloid-β and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice [J]. Proceedings of the National Academy of Sciences(USA) 2009, 106(01).
[2] David DC, Hauptmann S, Scherping I, Schuessel K, Keil U, Rizzu P, Ravid R, Drose S, Brandt U, Muller WE. [J]. The Journal of biological chemistry 2005.
[3] Hauptmann S, Keil U, Scherping I, Bonert A, Eckert A, Muller WE. Mitochondrial dysfunction in sporadic and genetic Alzheimer's disease. [J]. Experimental Gerontology 2006, 7(7).
[4] ECKERT A, HAUPTMANN S, SCHERPING I. Soluble betaamyloid leads to mitochondrial defects in amyloid precursor protein and tau transgenic mice [J]. NEURO-DEGENERATIVE DISEASES 2005, 5(01).
[5] LEWIS J, DICKSON D W, LIN W L. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP [J]. SCIENCE 2001, 293(01).
[6] Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, Metherate R, Mattson MP, Akbari Y, LaFerla FM. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. [J]. Neuron 2003, 3(3).
[7] BLURTON-JONES M, LAFERLA F M. Pathways by which Abeta facilitates tau pathology [J]. Current Alzheimer Research 2006, 3(01).
[8] Frank M. LaFerla. [J]. Biochemical Society Transactions 2010.
[9] Yifat Miller, Buyong Ma, Ruth Nussinov. Synergistic Interactions between Repeats in Tau Protein and Aβ Amyloids May Be Responsible for Accelerated Aggregation via Polymorphic States [J]. Biochemistry 2011, 23(23).
[10] Daniela Berg, Carsten Holzmann, Olaf Riess. 14-3-3 Proteins in the nervous system [J]. Nature reviews neuroscience 2003, 9(9).
[11] Layfield R, Fergusson J, Aitken A, Lowe J, Landon M, Mayer RJ. [J]. Neuroscience Letters: An International Multidisciplinary Journal Devoted to the Rapid Publication of Basic Research in the Brain Sciences 1996.
[12] UMAHARA T, UCHIHARA T, TSUCHIYA K. 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease [J]. Acta Neuropathologica 2004, 108(04).
[13] Soulie C, Nicole A, Delacourte A, Ceballos Picot I. Examination of stress-related genes in human temporal versus occipital cortex in the course of neurodegeneration: involvement of 14-3-3 zeta in this dynamic process. [J]. Neuroscience Letters: An International Multidisciplinary Journal Devoted to the Rapid Publication of Basic Research in the Brain Sciences 2004, 1(1).
[14] Chun J, Kwon T, Lee EJ, Kim CH, Han YS, Hong SK, Hyun S, Kang SS. 14-3-3 Protein mediates phosphorylation of microtubuleassociated protein tau by serum- and glucocorticoid-induced protein kinase 1 [J]. Molecules and cells 2004, 3(3).
[15] Li T, Paudel HK. [J]. Neuroscience Letters: An International Multidisciplinary Journal Devoted to the Rapid Publication of Basic Research in the Brain Sciences 2007.
[16] Sadik G, Tanaka T, Kato K, Yanagi K, Kudo T, Takeda M. Differential interaction and aggregation of 3-repeat and 4-repeat tau isoforms with 14-3-3zeta protein. [J]. Biochemical and Biophysical Research Communications 2009, 1(1).
[17] Sadik G, Tanaka T, Kato K, Yamamori H, Nessa BN, Morihara T, Takeda M. [J]. Journal of Neurochemistry: Offical Journal of the International Society for Neurochemistry 2009.
[18] Sluchanko NN, Seit Nebi AS, Gusev NB. Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta. [J]. FEBS Letters: For the Rapid Publication of Short Reports in Biochemistry, Biophysics and Molecular Biology 2009, 17(17).
[19] Qureshi, H.Y., Li, T., MacDonald, R., Cho, C.M., Leclerc, N., Paudel, H.K.. Interaction of 14-3-3β with microtubule-associated protein tau within alzheimer's disease neurofibrillary tangles [J]. Biochemistry 2013, 37(37).
[20] Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4 [J]. EMBO Journal 2007, 7(7).
[21] Underwood BR, Imarisio S, Fleming A, Rose C, Krishna G, Heard P, Quick M, Korolchuk VI, Renna M, Sarkar S, Garcia Arencibia M, O'Kane CJ, Murphy MP, Rubinsztein DC. Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease. [J]. Human Molecular Genetics 2010, 17(17).
[22] Underwood BR, Imarisio S, Fleming A, Rose C, Krishna G, Heard P, Quick M, Korolchuk VI, Renna M, Sarkar S, Garcia Arencibia M, O'Kane CJ, Murphy MP, Rubinsztein DC. Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease. [J]. Human Molecular Genetics 2010, 17(17).
[23] Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R, Yokoyama M, Mishima K, Saito I, Okano H. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice [J]. Nature 2006, 7095(7095).
[24] Komatsu M, Waguri S, Koike M, Sou Y, Ueno T, Hara T, Mizushima N, Iwata J, Ezaki J, Murata S. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice [J]. Cell 2007, 6(6).
[25] ZHENG Xianhong, WANG Weiwei, LIU Ruizhi. Effect of p62 on tau hyperphosphorylation in a rat model of Alzheimer's disease [J]. Neural Regen Res 2012, 7(17).