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Analysis of the Electrophoretic Profiles of prion protein in Carcinous and Pericarcinous Lysates of Six Different Types of Cancers

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Biomedical and Environmental Sciences 2021年第9期34卷 683-692页

作者： WEI Wei WU Yue Zhang XIAO Kang XU Guo Hui SONG Yun Tao SHI Qi DONG Xiao Ping Key Laboratory of Carcinogenesis and Translational Research(Ministry of Education) Head and Neck Surgery DepartmentPeking University Cancer Hospital&InstituteBeijing 100142China State Key Laboratory for Infectious Disease Prevention and Control Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases(Zhejiang University)National Institute for Viral Disease Control and PreventionChinese Center for Disease Control and PreventionBeijing 102206China Center for Global Public Health Chinese Center for Disease Control and PreventionBeijing 102206China Wuhan Institute of Virology Chinese Academy of ScienceWuhan 430071Hubei China China Academy of Chinese Medical Sciences Beijing 100700China

Objective To find the different electrophoretic profiles of prion protein in carcinous and individual pericarcinous tissues in lysates of gastric,colon,liver,lung,thyroid,and laryngeal cancers.Methods Sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE)and Western blot were used to test the amounts and electrophoretic patterns of total Pr P and the tolerance of PK(protease K)digestion among six various cancer tissue types.Results A mass of Pr P signals with a large molecular weight were identified in the homogenates of peripheral tissues.The amounts and electrophoretic patterns of total Pr P did not differ significantly between carcinous and pericarcinous tissues.Pr Ps in all types of the tested cancer samples were PK sensitive but showed diversity in the tolerance of PK digestion among various tissue types.Conclusions The study revealed that the included electrophoretic patterns of carcinous and pericarcinous tissues were almost similar.Unlike Pr P-specific immunohistochemical assay,evaluation of Pr P electrophoretic patterns in the peripheral organs and tissues by Western blot does not reflect tumor malignancy.

关键词： prion protein Cancer Electrophoretic profiles

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Tumor Necrosis Factor a Reduces SNAP29 Dependent Autolysosome Formation to Increase prion protein Level and Promote Tumor Cell Migration

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Virologica Sinica 2021年第3期36卷 458-475页

作者： Huan Li Ren Wang Ze Yu Run Shi Jie Zhang Shanshan Gao Ming Shao Shuzhong Cui Zhenxing Gao Jiang Xu Man-Sun Sy Chaoyang Li Wuhan Institute of Virology Chinese Academy of SciencesWuhan 430071China University of Chinese Academy of Sciences Beijing 100000China Affiliated Cancer Hospital and Institute of Guangzhou Medical University State Key Laboratory of Respiratory DiseaseGuangzhou 510095China Department of Stomatology First Affiliated HospitalSchool of MedicineShihezi UniversityShihezi 832008China Abdominal Surgery Affiliated Cancer Hospital and Institute of Guangzhou Medical UniversityGuangzhou 510095China Department of Pathology School of MedicineCase Western Reserve UniversityClevelandOH 44106USA

Tumor Necrosis Factor α(TNFα) is best known as a mediator of inflammation and immunity, and also plays important roles in tumor biology. However, the role of TNFα in tumor biology is complex and not completely understood. In a human melanoma cell line, M2, and a lung carcinoma cell line, A549, TNFα up-regulates prion protein(PrP) level, and promotes tumor cell migration in a PrP dependent manner. Silencing PRNP abrogates TNFα induced tumor cell migration;this phenotype is reversed when PRNP is re-introduced. Treatment with TNFα activates nuclear factor kappa B(NF-κB)signaling, which then mitigates autophagy by reducing the expression of Forkhead Box P3(FOXP3). Down regulation of FOXP3 reduces the transcription of synaptosome associated protein 29(SNAP29), which is essential in the fusion of autophagosome and lysosome creating autolysosome. FOXP3 being a bona fide transcription factor for SNAP29 is confirmed in a promoter binding assay. Accordingly, silencing SNAP29 in these cell lines also up-regulates PrP, and promotes tumor cell migration without TNFα treatment. But, when SNAP29 or FOXP3 is silenced in these cells, they are no longer respond to TNFα. Thus, a reduction in autophagy is the underlying mechanism by which expression of PrP is up-regulated,and tumor cell migration is enhanced upon TNFα treatment. Disrupting the TNFα-NF-κB-FOXP3-SNAP29 signaling axis may provide a therapeutic approach to mitigate tumor cell migration.

关键词： Tumor necrosis factorα(TNFα) prion protein Synaptosome associated protein 29(SNAP29) Autophagy Nuclear factor kappa B(NF-κB) Forkhead box P3(FOXP3)

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Saccharomyces cerevisiae in neuroscience:how unicellular organism helps to better understand prion protein?

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Neural Regeneration Research 2021年第3期16卷 489-495页

作者： Takao Ishikawa Department of Molecular Biology Institute of BiochemistryFaculty of BiologyUniversity of WarsawWarsawPoland

The baker's yeast Saccharomyces(S.)cerevisiae is a single-celled eukaryotic model organism widely used in research on life sciences.Being a unicellular organism,S.cerevisiae has some evident limitations in application to neuroscience.However,yeast prions are extensively studied and they are known to share some hallmarks with mammalian prion protein or other amyloidogenic proteins found in the pathogenesis of Alzheimer's,Parkinson's,or Huntington's diseases.Therefore,the yeast S.cerevisiae has been widely used for basic research on aggregation properties of proteins in cellulo and on their propagation.Recently,a yeast-based study revealed that some regions of mammalian prion protein and amyloidβ1–42 are capable of induction and propagation of yeast prions.It is one of the examples showing that evolutionarily distant organisms share common mechanisms underlying the structural conversion of prion proteins making yeast cells a useful system for studying mammalian prion protein.S.cerevisiae has also been used to design novel screening systems for anti-prion compounds from chemical libraries.Yeastbased assays are cheap in maintenance and safe for the researcher,making them a very good choice to perform preliminary screening before further characterization in systems engaging mammalian cells infected with prions.In this review,not only classical red/white colony assay but also yeast-based screening assays developed during last year are discussed.Computational analysis and research carried out using yeast prions force us to expect that prions are widely present in nature.Indeed,the last few years brought us several examples indicating that the mammalian prion protein is no more peculiar protein–it seems that a better understanding of prion proteins nature-wide may aid us with the treatment of prion diseases and other amyloid-related medical conditions.

关键词： amyloid artificial prion baker's yeast budding yeast drug screening fusion protein neurodegenerative diseases prion protein yeast-based assay

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Metabolism of minor isoforms of prion proteins Cytosolic prion protein and transmembrane prion protein

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Neural Regeneration Research 2013年第30期8卷 2868-2878页

作者： Zhiqi Song Deming Zhao Lifeng Yang State Key Laboratory for Agrobiotechnology National Animal Transmissible Spongiform Encephalopathy Laboratory College of Veterinary Medicine China Agricultural University

Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and patho- genicity. In vivo and in vitro studies have shown that several cytosolic forms of prion protein with specific topological structure can destroy intracellular stability and contribute to prion protein pathogenicity. In this study, the latest molecular chaperone system associated with endoplasmic re- ticulum-associated protein degradation, the endoplasmic reticulum resident protein quality-control system and the ubiquitination proteasome system, is outlined. The molecular chaperone system directly correlates with the prion protein degradation pathway. Understanding the molecular mechanisms will help provide a fascinating avenue for further investigations on prion disease treatment and prion protein-induced neurodegenerative diseases.

关键词： neural regeneration neurodegeneration prion protein cytosolic form of prion protein transmem-brane form of prion protein metabolism protein degeneration ubiquitination molecular chaperone molecular mechanism neuroregeneration

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Detailing the ultrastructure’s increase of prion protein in pancreatic adenocarcinoma

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World Journal of Gastroenterology 2021年第42期27卷 7324-7339页

作者： Matteo Bianchini Maria Anita Giambelluca Maria Concetta Scavuzzo Gregorio Di Franco Simone Guadagni Matteo Palmeri NiccolòFurbetta Desirée Gianardi Niccola Funel Claudio Ricci Raffaele Gaeta Luca Emanuele Pollina Alfredo Falcone Caterina Vivaldi Giulio Di Candio Francesca Biagioni Carla Letizia Busceti Luca Morelli Francesco Fornai General Surgery Unit Department of Translational Research and New Technologies in Medicine and SurgeryUniversity of PisaPisa 56124Italy Human Anatomy Department of Translational Research and New Technologies in Medicine and SurgeryUniversity of PisaPisa 56124Italy Division of Surgical Pathology Department of SurgicalMedicalMolecular Pathology and Critical AreaUniversity of PisaPisa 56124Italy Division of Medical Oncology Department of Translational Research and New Technologies in Medicine and SurgeryUniversity of PisaPisa 56124Italy IRCCS Neuromed Istituto Neurologico MediterraneoPozzilli 86077Italy EndoCAS(Center for Computer Assisted Surgery) University of PisaPisa 56124Italy

BACKGROUND Recent evidences have shown a relationship between prion protein(PrPc)expression and pancreatic ductal adenocarcinoma(PDAC).Indeed,PrPc could be one of the markers explaining the aggressiveness of this tumor.However,studies investigating the specific compartmentalization of increased PrPc expression within PDAC cells are lacking,as well as a correlation between ultrastructural evidence,ultrastructural morphometry of PrPc protein and clinical data.These data,as well as the quantitative stoichiometry of this protein detected by immuno-gold,provide a significant advancement in understanding the biology of disease and the outcome of surgical resection.AIM To analyze quantitative stoichiometry and compartmentalization of PrPc in PDAC cells and to correlate its presence with prognostic data METHODS Between June 2018 and December 2020,samples from pancreatic tissues of 45 patients treated with pancreatic resection for a preoperative suspicion of PDAC at our Institution were collected.When the frozen section excluded a PDAC diagnosis,or the nodules were too small for adequate sampling,patients were ruled out from the present study.Western blotting was used to detect,quantify and compare the expression of PrPc in PDAC and control tissues,such as those of non-affected neighboring pancreatic tissue of the same patient.To quantify the increase of PrPc and to detect the subcellular compartmentalization of PrPc within PDAC cells,immuno-gold stoichiometry within specific cell compartments was analyzed with electron microscopy.Finally,an analysis of quantitative PrPc expression according to prognostic data,such as cancer stage,recurrence of the disease at 12 mo after surgery and recurrence during adjuvant chemotherapy was made.RESULTS The amount of PrPc within specimen from 38 out of 45 patients was determined by semi-quantitative analysis by using Western blotting,which indicates that PrPc increases almost three-fold in tumor pancreatic tissue compared with healthy pancreatic regions[242.41±28.36 optical density(OD)v

关键词： Pancreatic ductal adenocarcinoma prion protein Western blotting Electron microscopy Cellular compartmentalization Neuroinvasion

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Structural and dynamical mechanisms of a naturally occurring variant of the human prion protein in preventing prion conversion

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Chinese Physics B 2020年第10期29卷 66-75页

作者：唐一鸣姚逸飞韦广红 Department of Physics State Key Laboratory of Surface Physics and Key Laboratory for Computational Physical Science(Ministry of Education)and Multiscale Research Institute of Complex SystemsFudan UniversityShanghai 200433China

prion diseases are associated with the misfolding of the normal helical cellular form of prion protein (PrPC) into the β-sheet-rich scrapie form (PrPSc) and the subsequent aggregation of PrPSc into amyloid fibrils. Recent studies demonstrated that a naturally occurring variant V127 of human PrPC is intrinsically resistant to prion conversion and aggregation, and can completely prevent prion diseases. However, the underlying molecular mechanism remains elusive. Herein we perform multiple microsecond molecular dynamics simulations on both wildtype (WT) and V127 variant of human PrPC to understand at atomic level the protective effect of V127 variant. Our simulations show that G127V mutation not only increases the rigidity of the S2–H2 loop between strand-2 (S2) and helix-2 (H2), but also allosterically enhances the stability of the H2 C-terminal region. Interestingly, previous studies reported that animals with rigid S2–H2 loop usually do not develop prion diseases, and the increase in H2 C-terminal stability can prevent misfolding and oligomerization of prion protein. The allosteric paths from G/V127 to H2 C-terminal region are identified using dynamical network analyses. Moreover, community network analyses illustrate that G127V mutation enhances the global correlations and intra-molecular interactions of PrP, thus stabilizing the overall PrPC structure and inhibiting its conversion into PrPSc. This study provides mechanistic understanding of human V127 variant in preventing prion conversion which may be helpful for the rational design of potent anti-prion compounds.

关键词： prion protein V127 variant molecular dynamics simulations dynamic network analysis

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Correlation between prion protein gene codon 129 polymorphism and late-onset Alzheimer's disease

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Neural Regeneration Research 2009年第6期4卷 468-473页

作者： Hairong Qian Luning Wang Xiaokun Qi Jianwei Liu Jing Liu Ling Ye Hengge Xie WeiWang Feng Qiu Department of Neurology Naval General Hospital of Chinese PLA Beijing 100037 China Department of Geriatric Neurology General Hospital of Chinese PLA Beijing 100853 China Institute of Geriatrics General Hospital of Chinese PLA Beijing 100853 China

BACKGROUND： Studies addressing the correlation between prion protein gene codon 129 polymorphism, Alzheimer＇s disease, and cognitive disorders have mainly focused on Caucasians. However, prion protein gene codon 129 polymorphism is thought to also affect the Chinese Han and Wei populations. OBJECTIVE： To analyze the differences of prion protein gene codon 129 distribution among the elderly Chinese Han, East Asian, and Caucasian populations, and to study the correlation between prion protein gene codon 129 distribution and late-onset Alzheimer＇s disease. DESIGN, TIME AND SETTING： A gene polymorphism analysis was performed in the Institute of Geriatrics, General Hospital of Chinese PLA between January 2006 and January 2007. PARTICIPANTS： A total of 152 elderly Chinese Han people were selected from the Beijing Troop Cadre＇s Sanitarium. Among them, 60 patients with late-onset Alzheimer＇s disease, with a mean age of （82 ± 7） years （range 67-94 years） and disease course of （5.9 ± 4.4） years, comprising 44 males with a mean age of （83 ± 7） years and 16 females with a mean age of （78 ±7） years, were selected for the case group. An additional 92 healthy elderly subjects, with a mean of （76 ± 9） years （range 60-94 years）, comprising 76 males with a mean age of （77 ± 9） years and 16 females with a mean age of （70 ± 8） years, were selected for the control group. There were no significant differences in age and gender between the two groups （P〉 0.05）. METHODS： DNA was extracted from peripheral blood leukocytes using routine phenol/chloroform methodology. prion protein gene codon 129 potymorphism and ApoE polymorphism were measured using PCR-restriction fragment length polymorphism. The ApoEε allele was considered the standard for analyzing correlations between prion protein gene codon 129 polymorphism and late-onset Alzheimer＇s disease. MAIN OUTCOME MEASURES： prion protein gene codon 129 distribution; correlation between genotypic frequency and allele frequency of prion protein gene codon 129 with Alzheimer＇s disease; relat

关键词： Alzheimer＇s disease prion protein polymorphism

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Unraveling the molecular mechanism of prion disease:Insights fromα2 area mutations in human prion protein

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Chinese Physics B 2023年第12期32卷 657-665页

作者：谈荣日夏奎寻大毛宗文军余幼胜 Department of Physics Jiangxi Science and Technology Normal UniversityNanchang 330013China School of Science East China University of TechnologyNanchang 330013China

prion diseases are a class of fatal neurodegenerative diseases caused by misfolded prion proteins.The main reason is that pathogenic prion protein has a strong tendency to aggregate,which easily induces the damage to the central nervous system.Point mutations in the human prion protein gene can cause prion diseases such as Creutzfeldt-Jakob and Gerstmann's syndrome.To understand the mechanism of mutation-induced prion protein aggregation,the mutants in an aqueous solution are studied by molecular dynamics simulations,including the wild type,V180I,H187R and a double point mutation which is associated with CJD and GSS.After running simulations for 500 ns,the results show that these three mutations have different effects on the kinetic properties of PrP.The high fluctuations around the N-terminal residues of helix 2 in the V180I variant lead to a decrease in hydrogen bonding on helix 2,while an increase in the number of hydrogen bonds between the folded regions promotes the generation ofβ-sheet.Meanwhile,partial deletion of salt bridges in the H187R and double mutants allows the sub-structural domains of the prion protein to separate,which would accelerate the conversion from PrPC to PrPSc.A similar trend is observed in both SASA and Rg for all three mutations,indicating that the conformational space is reduced and the structure is compact.

关键词： prion protein mutations misfolding molecular dynamics simulations

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Astrocyte in prion disease: a double-edged sword

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Neural Regeneration Research 2022年第8期17卷 1659-1665页

作者： Waqas Tahir Simrika Thapa Hermann M.Schatzl Department of Comparative Biology&Experimental Medicine Faculty of Veterinary MedicineUniversity of CalgaryCalgaryABCanada Calgary prion Research Unit University of CalgaryCalgaryABCanada Hotchkiss Brain Institute University of CalgaryCalgaryABCanada

prion diseases are infectious protein misfolding disorders of the central nervous system that result from misfolding of the cellular prion protein(PrPC)into the pathologic isoform PrPSc.Pathologic hallmarks of prion disease are depositions of pathological prion protein PrPSc,neuronal loss,spongiform degeneration and astrogliosis in the brain.prion diseases affect human and animals,there is no effective therapy,and they invariably remain fatal.For a long time,neuronal loss was considered the sole reason for neurodegeneration in prion pathogenesis,and the contribution of non-neuronal cells like microglia and astrocytes was considered less important.Recent evidence suggests that neurodegeneration during prion pathogenesis is a consequence of a complex interplay between neuronal and non-neuronal cells in the brain,but the exact role of these non-neuronal cells during prion pathology is still elusive.Astrocytes are non-neuronal cells that regulate brain homeostasis under physiological conditions.However,astrocytes can deposit PrPSc aggregates and propagate prions in prion-infected brains.Additionally,sub-populations of reactive astrocytes that include neurotrophic and neurotoxic species have been identified,differentially expressed in the brain during prion infection.Revealing the exact role of astrocytes in prion disease is hampered by the lack of in vitro models of prion-infected astrocytes.Recently,we established a murine astrocyte cell line persistently infected with mouse-adapted prions,and showed how such astrocytes differentially process various prion strains.Considering the complexity of the role of astrocytes in prion pathogenesis,we need more in vitro and in vivo models for exploring the contribution of sub-populations of reactive astrocytes,their differential regulation of signaling cascades,and the interaction with neurons and microglia during prion pathogenesis.This will help to establish novel in vivo models and define new therapeutic targets against prion diseases.In this review,we will discuss the comp

关键词： Alzheimer’s disease astrocytes central nervous system Creutzfeldt-Jakob disease glial cells neurodegeneration prion prion disease prion protein scrapie

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Valine 127 is very important for amyloid fibril formation of human prion protein

Valine 127 is very important for amyloid fibril formation of...

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中国生物化学与分子生物学会2016年全国学术会议

作者： Jun-Jie Huang Chuan-Wei Yi Jie Chen Yi Liang State Key Laboratory of Virology College of Life Sciences Wuhan University

prion diseases are a group of fatal neurodegenerative diseases caused by the conformational changes of prion protein(Pr P).Recently,a new novel human Pr P variant,G127V,has been reported to be under positive evolutionary selection during the epidemic of kuru.However,the molecular mechanism why G127V can protect people from prion diseases is still unknown.

关键词： prion protein prion diseases Amyloid fibril formation Amino acid substitution protein aggregation

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