TO THE EDITOR Prion diseases are fatal and in curable n eurodegenerative diseases caused by a pathogenic form of prion protein(PrP^(Sc))derived from a cellular form of prion protein(PrP^(C)).Recent studies have report...TO THE EDITOR Prion diseases are fatal and in curable n eurodegenerative diseases caused by a pathogenic form of prion protein(PrP^(Sc))derived from a cellular form of prion protein(PrP^(C)).Recent studies have reported that aquaporin 4(AQP4)expression is dramatically upregulated in the brains of individuals with several different prion diseases.Since AQP4 is a key protein of the glymphatic system,which is the perivascular waste clearing system of the brain,and since altered expression of AQP4 has been observed in prion diseases,the glymphatic system may be associated with prion diseases.展开更多
The IFITM3 gene is classified as a member of the small interferonstimulated genes(ISGs)and plays a paramount role in defense against enveloped viruses,including influenza A viruses.1–6 Previous studies have reported ...The IFITM3 gene is classified as a member of the small interferonstimulated genes(ISGs)and plays a paramount role in defense against enveloped viruses,including influenza A viruses.1–6 Previous studies have reported that the rs12252 SNP,which is located in the open reading frame(ORF)of the IFITM3 gene,impacts the splicing procedure of protein production,which makes a truncated form of the IFITM3 protein and lowers its antiviral capacity.7–9 In addition,the rs34481144 SNP genotype affects the transcriptional regulation of the IFITM3 gene and IFITM3-neighboring genes and has a potent association with the clinical results of the H1N1 influenza 2009 pandemic in three human cohorts.10 Because several studies have reported that polymorphism of the IFITM3 gene is crucial in the host immune response,fine mapping of and extracting disease-associated SNPs from the human IFITM3 gene are important baseline studies necessary to understand how the IFITM3 protein functions in innate immunity.展开更多
基金This work was supported by a National Research Foundation of Korea(NRF)grant funded by the Korean government(MSIT)(2021R1A2C1013213)This research was supported by the Basic Science Research Program through the National Research Foundation(NRF)of Korea funded by the Ministry of Education(2017R1A6A1A03015876)+1 种基金This work was supported by an NRF(National Research Foundation of Korea)Grant funded by the Korean Government(NRF-2019-Fostering Core Leaders of the Future Basic Science Program/Global Ph.D.Fellowship Program)SYW and YCK were supported by the BK21 Plus Program in the Department of Bioactive Material Sciences.
文摘TO THE EDITOR Prion diseases are fatal and in curable n eurodegenerative diseases caused by a pathogenic form of prion protein(PrP^(Sc))derived from a cellular form of prion protein(PrP^(C)).Recent studies have reported that aquaporin 4(AQP4)expression is dramatically upregulated in the brains of individuals with several different prion diseases.Since AQP4 is a key protein of the glymphatic system,which is the perivascular waste clearing system of the brain,and since altered expression of AQP4 has been observed in prion diseases,the glymphatic system may be associated with prion diseases.
基金supported by the Ministry of Health,Welfare and Family Affairs.All samples derived from the Korea Biobank Network were obtained with informed consent under institutional review board-approved protocolssupported by the Basic Science Program through the National Research Foundation(NRF)of Korea funded by the Ministry of Education,Science and Technology(2018R1D1A1B07048711)+2 种基金supported by the Basic Science Research Program through the National Research Foundation(NRF)of Korea funded by the Ministry of Education(2017R1A6A1A03015876)supported by the BK21 Plus Program in the Department of Bioactive Material Sciencessupported by the NRF(National Research Foundation of Korea)Grant funded by the Korean Government(NRF-2019-Fostering Core Leaders of the Future Basic Science Program/Global Ph.D.Fellowship Program).
文摘The IFITM3 gene is classified as a member of the small interferonstimulated genes(ISGs)and plays a paramount role in defense against enveloped viruses,including influenza A viruses.1–6 Previous studies have reported that the rs12252 SNP,which is located in the open reading frame(ORF)of the IFITM3 gene,impacts the splicing procedure of protein production,which makes a truncated form of the IFITM3 protein and lowers its antiviral capacity.7–9 In addition,the rs34481144 SNP genotype affects the transcriptional regulation of the IFITM3 gene and IFITM3-neighboring genes and has a potent association with the clinical results of the H1N1 influenza 2009 pandemic in three human cohorts.10 Because several studies have reported that polymorphism of the IFITM3 gene is crucial in the host immune response,fine mapping of and extracting disease-associated SNPs from the human IFITM3 gene are important baseline studies necessary to understand how the IFITM3 protein functions in innate immunity.
