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The endosomal-lysosomal system: from acidification and cargo sorting to neurodegeneration

Translational Neurodegeneration 2015年第1期4卷 141-150页

作者： Yong-Bo Hu eric B dammer Ru-Jing Ren Gang Wang Department of Neurology&Neuroscience Institute Ruijin Hospital affiliated to Shanghai Jiao Tong University School of MedicineShanghai 200025China Department of Biochemistry Center for Neurodegenerative DiseasesEmory University School of MedicineAtlantaGA 30322USA

The endosomal-lysosomal system is made up of a set of intracellular membranous compartments that dynamically interconvert,which is comprised of early endosomes,recycling endosomes,late endosomes,and the *** addition,autophagosomes execute autophagy,which delivers intracellular contents to the *** of endosomes and/or autophagosomes into a lysosome creates an unique acidic environment within the cell for proteolysis and recycling of unneeded cellular components into usable amino acids and other biomolecular building *** the endocytic pathway,gradual maturation of endosomes into a lysosome and acidification of the late endosome are accompanied by vesicle trafficking,protein sorting and targeted degradation of some sorted *** opposing sorting systems are operating in these processes:the endosomal sorting complex required for transport(ESCRT)supports targeted degradation and the retromer supports retrograde retrieval of certain *** endosomal-lysosomal system is emerging as a central player in a host of neurodegenerative diseases,demonstrating potential roles which are likely to be revealed in pathogenesis and for viable therapeutic *** we focus on the physiological process of endosomal-lysosomal maturation,acidification and sorting systems along the endocytic pathway,and further discuss relationships between abnormalities in the endosomal-lysosomal system and neurodegenerative diseases,especially Alzheimer’s disease(AD).

关键词： The endosomal-lysosomal system Neurodegeneration Acidification ESCRT Retromer Alzheimer’s disease

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Proteomics of protein post-translational modifications implicated in neurodegeneration

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Translational Neurodegeneration 2014年第1期3卷 156-168页

作者： Ru-Jing Ren eric B dammer Gang Wang Nicholas T Seyfried Allan I Levey Department of Neurology Center for Neurodegenerative DiseasesEmory University School of MedicineAtlantaGA 30322USA Department of Biochemistry Center for Neurodegenerative DiseasesEmory University School of MedicineAtlantaGA 30322USA Department of Pharmacology Center for Neurodegenerative DiseasesEmory University School of MedicineAtlantaGA 30322USA Emory Proteomics Service Center Center for Neurodegenerative DiseasesEmory University School of MedicineAtlantaGA 30322USA

Mass spectrometry(MS)-based proteomics has developed into a battery of approaches that is exceedingly adept at identifying with high mass accuracy and precision any of the following:oxidative damage to proteins(redox proteomics),phosphorylation(phosphoproteomics),ubiquitination(diglycine remnant proteomics),protein fragmentation(degradomics),and other posttranslational modifications(PTMs).Many studies have linked these PTMs to pathogenic mechanisms of *** date,identifying PTMs on specific pathology-associated proteins has proven to be a valuable step in the evaluation of functional alteration of proteins and also elucidates biochemical and structural explanations for possible pathophysiological mechanisms of neurodegenerative *** review provides an overview of methods applicable to the identification and quantification of PTMs on proteins and enumerates historic,recent,and potential future research endeavours in the field of proteomics furthering the understanding of PTM roles in the pathogenesis of neurodegeneration.

关键词： Proteomics Protein posttranslational modifications Neurodegeneration Alzheimer’s disease Parkinson’s disease

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Genetic profiles of familial late-onset Alzheimer’s disease in China:The Shanghai FLOAD study

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Genes & Diseases 2022年第6期9卷 1639-1649页

作者： Xin-Yi Xie Qian-Hua Zhao Qiang Huang a eric dammer Sheng-di Chen Ru-Jing Ren Gang Wang the Alzheimer’s Disease Neuroimaging Initiative Department of Neurology and Institute of Neurology Ruijin Hospital Affiliated with Shanghai JiaoTong University School of MedicineShanghai 200025PR China Institute of Neurology Huashan HospitalFudan UniversityShanghai 200040PR China National Clinical Research Center for Aging and Medicine Huashan HospitalFudan UniversityShanghai 200040PR China Department of Biochemistry Center for Neurodegenerative DiseaseEmory University School of MedicineAtlantaGA 30322USA

Compared with early-onset familial AD(FAD),the heritability of most familial lateonset Alzheimer’s disease(FLOAD)cases still remains ***,there are few reported genetic profiles of FLOAD to *** the present study,targeted sequencing of selected candidate genes was conducted for each of 90 probands with FLOAD and 101 unrelated matched normal controls among Chinese Han *** show a significantly lower rate of mutation in APP and PSENs,and APOE e4 genetic risk is higher for *** the Chinese FLOAD population,the most frequent variant was CR1 rs116806486[5.6%,95%CI(1.8%,12.5%)],followed by coding variants of TREM2(4.4%,95%CI(1.2%,10.9%))and novel mutations of ACE[3.3%,95%CI(0.7%,9.4%)].Next,we found that novel pathogenic mutations in ACE including frame-shift and nonsense mutations were in association with FLOAD regardless of APOE e4 *** from the Alzheimer’s disease Neuroimaging Initiative(ADNI)database also supported this finding in different *** of in vitro analysis suggest that frame-shift and nonsense mutations in ACE may be involved in LOAD through decreased ACE protein levels without affecting direct processing of APP.

关键词： ACE Alzheimer’s disease Familial late-onset Alzheimer’s disease Gene Mutation

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