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Journal articles on the topic "Shadow of prion protein gene"
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Won, Sae-Young, Yong-Chan Kim, Seon-Kwan Kim, and Byung-Hoon Jeong. "The First Report of Genetic and Structural Diversities in the SPRN Gene in the Horse, an Animal Resistant to Prion Disease." Genes 11, no. 1 (December 28, 2019): 39. http://dx.doi.org/10.3390/genes11010039.
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Prion diseases are fatal neurodegenerative diseases and are characterized by the accumulation of abnormal prion protein (PrPSc) in the brain. During the outbreak of the bovine spongiform encephalopathy (BSE) epidemic in the United Kingdom, prion diseases in several species were reported; however, horse prion disease has not been reported thus far. In previous studies, the shadow of prion protein (Sho) has contributed to an acceleration of conversion from normal prion protein (PrPC) to PrPSc, and the shadow of prion protein gene (SPRN) polymorphisms have been significantly associated with the susceptibility of prion diseases. We investigated the genotype, allele and haplotype frequencies of the SPRN gene using direct sequencing. In addition, we analyzed linkage disequilibrium (LD) and haplotypes among polymorphisms. We also investigated LD between PRNP and SPRN single nucleotide polymorphisms (SNPs). We compared the amino acid sequences of Sho protein between the horse and several prion disease-susceptible species using ClustalW2. To perform Sho protein modeling, we utilized SWISS-MODEL and Swiss-PdbViewer programs. We found a total of four polymorphisms in the equine SPRN gene; however, we did not observe an in/del polymorphism, which is correlated with the susceptibility of prion disease in prion disease-susceptible animals. The SPRN SNPs showed weak LD value with PRNP SNP. In addition, we found 12 horse-specific amino acids of Sho protein that can induce significantly distributional differences in the secondary structure and hydrogen bonds between the horse and several prion disease-susceptible species. To the best of our knowledge, this is the first report regarding the genetic and structural characteristics of the equine SPRN gene.
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Kim, Yong-Chan, Hyeon-Ho Kim, Kiwon Kim, An-Dang Kim, and Byung-Hoon Jeong. "Novel Polymorphisms and Genetic Characteristics of the Shadow of Prion Protein Gene (SPRN) in Cats, Hosts of Feline Spongiform Encephalopathy." Viruses 14, no. 5 (May 6, 2022): 981. http://dx.doi.org/10.3390/v14050981.
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Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrPSc) originating from normal prion protein (PrPC) and have been reported in several types of livestock and pets. Recent studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene (SPRN) interacts with prion protein (PrP) and accelerates prion diseases. In addition, genetic polymorphisms in the SPRN gene are related to susceptibility to prion diseases. However, genetic polymorphisms in the feline SPRN gene and structural characteristics of the Sho have not been investigated in cats, a major host of feline spongiform encephalopathy (FSE). We performed amplicon sequencing to identify feline SPRN polymorphisms in the 623 bp encompassing the open reading frame (ORF) and a small part of the 3′ untranslated region (UTR) of the SPRN gene. We analyzed the impact of feline SPRN polymorphisms on the secondary structure of SPRN mRNA using RNAsnp. In addition, to find feline-specific amino acids, we carried out multiple sequence alignments using ClustalW. Furthermore, we analyzed the N-terminal signal peptide and glycosylphosphatidylinositol (GPI)-anchor using SignalP and PredGPI, respectively. We identified three novel SNPs in the feline SPRN gene and did not find strong linkage disequilibrium (LD) among the three SNPs. We found four major haplotypes of the SPRN polymorphisms. Strong LD was not observed between PRNP and SPRN polymorphisms. In addition, we found alterations in the secondary structure and minimum free energy of the mRNA according to the haplotypes in the SPRN polymorphisms. Furthermore, we found four feline-specific amino acids in the feline Sho using multiple sequence alignments among several species. Lastly, the N-terminal signal sequence and cutting site of the Sho protein of cats showed similarity with those of other species. However, the feline Sho protein exhibited the shortest signal sequence and a unique amino acid in the omega-site of the GPI anchor. To the best of our knowledge, this is the first report on genetic polymorphisms of the feline SPRN gene.
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Kim, Yong-Chan, and Byung-Hoon Jeong. "First report of prion-related protein gene (PRNT) polymorphisms in cattle." Veterinary Record 182, no. 25 (April 17, 2018): 717. http://dx.doi.org/10.1136/vr.104123.
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Prion diseases are caused by structural changes in normal prion protein (PrPC). The prion gene family includes four members: prion protein (PRNP), prion-like protein (PRND), shadow of PRNP (SPRN) and prion-related protein (PRNT). Genetic association studies of prion diseases and the other genes in the prion gene family, except for PRNT, have been performed in cattle. Our previous studies indicated that the distribution of PRNP promoter polymorphisms related with bovine spongiform encephalopathy susceptibility is significantly different in Hanwoo (Korean native cattle) and Holstein cattle. However, PRNT polymorphisms have not been reported thus far in cattle. Hence, we examined the PRNT single nucleotide polymorphisms (SNPs) in 315 Hanwoo and 140 Holstein cattle. We found a total of two SNPs, PRNT c.-87C>T and PRNT c.-37G>C, in the 5’ untranslated region of exon 2. The c.-87C>T and c.-37G>C genotype (P<0.0001) and allele (P<0.0001) frequencies exhibited significant differences in the distribution between Hanwoo and Holstein cattle. In addition, the c.-37G<C polymorphism was not found in Hanwoo. Interestingly, we did not find any polymorphisms in the ORF of bovine PRNT, which is in contrast with the highly polymorphic ovine PRNT ORF region. This is the first genetic research of the PRNT gene in cattle.
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Kim, Yong-Chan, and Byung-Hoon Jeong. "The first report of prion-related protein gene (PRNT) polymorphisms in goat." Acta Veterinaria Hungarica 65, no. 2 (June 2017): 291–300. http://dx.doi.org/10.1556/004.2017.028.
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Prion protein is encoded by the prion protein gene (PRNP). Polymorphisms of several members of the prion gene family have shown association with prion diseases in several species. Recent studies on a novel member of the prion gene family in rams have shown that prion-related protein gene (PRNT) has a linkage with codon 26 of prion-like protein (PRND). In a previous study, codon 26 polymorphism of PRND has shown connection with PRNP haplotype which is strongly associated with scrapie vulnerability. In addition, the genotype of a single nucleotide polymorphism (SNP) at codon 26 of PRND is related to fertilisation capacity. These findings necessitate studies on the SNP of PRNT gene which is connected with PRND. In goat, several polymorphism studies have been performed for PRNP, PRND, and shadow of prion protein gene (SPRN). However, polymorphism on PRNT has not been reported. Hence, the objective of this study was to determine the genotype and allelic distribution of SNPs of PRNT in 238 Korean native goats and compare PRNT DNA sequences between Korean native goats and several ruminant species. A total of five SNPs, including PRNT c.-114G > T, PRNT c.-58A > G in the upstream of PRNT gene, PRNT c.71C > T (p.Ala24Val) and PRNT c.102G > A in the open reading frame (ORF) and c.321C > T in the downstream of PRNT gene, were found in this study. All five SNPs of caprine PRNT gene in Korean native goat are in complete linkage disequilibrium (LD) with a D’ value of 1.0. Interestingly, comparative sequence analysis of the PRNT gene revealed five mismatches between DNA sequences of Korean native goats and those of goats deposited in the GenBank. Korean native black goats also showed 5 mismatches in PRNT ORF with cattle. To the best of our knowledge, this is the first genetic research of the PRNT gene in goat.
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Won, Sae-Young, Yong-Chan Kim, Kyoungtag Do, and Byung-Hoon Jeong. "The First Report of Genetic Polymorphisms of the Equine SPRN Gene in Outbred Horses, Jeju and Halla Horses." Animals 11, no. 9 (September 1, 2021): 2574. http://dx.doi.org/10.3390/ani11092574.
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Prion disease is a fatal infectious disease caused by the accumulation of pathogenic prion protein (PrPSc) in several mammals. However, to date, prion disease has not been reported in horses. The Sho protein encoded by the shadow of the prion protein gene (SPRN) plays an essential role in the pathomechanism of prion diseases. To date, the only genetic study of the equine SPRN gene has been reported in the inbred horse, Thoroughbred horse. We first discovered four SPRN single nucleotide polymorphisms (SNPs) in 141 Jeju and 88 Halla horses by direct DNA sequencing. In addition, we found that the genotype, allele and haplotype frequencies of these SNPs of Jeju horses were significantly different from those of Halla and Thoroughbred horses, this latter breed is also included in this study. Furthermore, we observed that the minimum free energy and mRNA secondary structure were significantly different according to haplotypes of equine SPRN polymorphisms by the RNAsnp program. Finally, we compared the SNPs in the coding sequence (CDS) of the SPRN gene between horses and prion disease-susceptible species. Notably, prion disease-susceptible animals had polymorphisms that cause amino acid changes in the open reading frame (ORF) of the SPRN gene, while these polymorphisms were not found in horses.
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Lampo, Evelyne, Mario Van Poucke, Karine Hugot, Hélène Hayes, Alex Van Zeveren, and Luc J. Peelman. "Characterization of the genomic region containing the Shadow of Prion Protein (SPRN) gene in sheep." BMC Genomics 8, no. 1 (2007): 138. http://dx.doi.org/10.1186/1471-2164-8-138.
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Stewart, Paula, Cuicui Shen, Deming Zhao, and Wilfred Goldmann. "Genetic analysis of the SPRN gene in ruminants reveals polymorphisms in the alanine-rich segment of shadoo protein." Journal of General Virology 90, no. 10 (October 1, 2009): 2575–80. http://dx.doi.org/10.1099/vir.0.011494-0.
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Prion diseases in ruminants, especially sheep scrapie, cannot be fully explained by PRNP genetics, suggesting the influence of a second modulator gene. The SPRN gene is a good candidate for this role. The SPRN gene encodes the shadoo protein (Sho) which has homology to the PRNP gene encoding prion protein (PrP). Murine Sho has a similar neuroprotective activity to PrP and SPRN gene variants are associated with human prion disease susceptibility. SPRN gene sequences were obtained from 14 species in the orders Artiodactyla and Rodentia. We report here the sequences of more than 20 different Sho proteins that have arisen due to single amino acid substitutions and amino acid deletions or insertions. All Sho sequences contained an alanine-rich sequence homologous to a hydrophobic region with amyloidogenic characteristics in PrP. In contrast with PrP, the Sho sequence showed variability in the number of alanine residues.
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Corley, Susan M., and Jill E. Gready. "Identification of the RGG Box Motif in Shadoo: RNA-Binding and Signaling Roles?" Bioinformatics and Biology Insights 2 (January 2008): BBI.S1075. http://dx.doi.org/10.4137/bbi.s1075.
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Using comparative genomics and in-silico analyses, we previously identified a new member of the prion-protein (PrP) family, the gene SPRN, encoding the protein Shadoo (Sho), and suggested its functions might overlap with those of PrP. Extended bioinformatics and conceptual biology studies to elucidate Sho's functions now reveal Sho has a conserved RGG-box motif, a well-known RNA-binding motif characterized in proteins such as FragileX Mental Retardation Protein. We report a systematic comparative analysis of RGG-box containing proteins which highlights the motif's functional versatility and supports the suggestion that Sho plays a dual role in cell signaling and RNA binding in brain. These findings provide a further link to PrP, which has well-characterized RNA-binding properties.
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Wang, Siqi, Hui Zhao, and Yaping Zhang. "Advances in research on Shadoo, shadow of prion protein." Chinese Science Bulletin 59, no. 9 (January 28, 2014): 821–27. http://dx.doi.org/10.1007/s11434-014-0129-5.
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Nakamura, Yuko, Akikazu Sakudo, Keiichi Saeki, Tomomi Kaneko, Yoshitsugu Matsumoto, Antonio Toniolo, Shigeyoshi Itohara, and Takashi Onodera. "Transfection of prion protein gene suppresses coxsackievirus B3 replication in prion protein gene-deficient cells." Journal of General Virology 84, no. 12 (December 1, 2003): 3495–502. http://dx.doi.org/10.1099/vir.0.19222-0.
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The susceptibility of prion protein gene (Prnp)-null cells to coxsackievirus B3 (CVB3) was investigated. Primary cultures of murine Prnp −/− brain cells were more sensitive to CVBs than corresponding cells from wild-type mice. The viral susceptibility of a Prnp-null cell line (HpL3-4) derived from the murine hippocampus was compared with that of two established cell lines (HeLa and HEp-2) that are widely employed for CVB3 studies. After infection with CVB3, HpL3-4 cells showed a very rapid and complete cytopathic effect (CPE). CPE developed earlier and viruses replicated at higher titres in HpL3-4 cells compared with HeLa and HEp-2 cells. Under a semi-solid medium, plaques developed rapidly in CVB3-infected HpL3-4 cells. To confirm the effect of Prnp on virus infection, a Prnp −/− cell line and a Prnp-transfected neuronal cell line were analysed. The replication and release of infectious particles of CVB3 in Prnp −/− cells were significantly more effective than those of the Prnp-transfected cell line. Levels of type I interferon (IFN) after CVB3 infection were higher in the Prnp-transfected cell line than in Prnp −/− cells, whereas apoptotic cells were more obvious in the Prnp −/− cells than in those of the Prnp-transfected cell line. These findings suggest that the absence of Prnp retards the induction of CVB3-induced IFNs, resulting in an enhanced CVB3 production and apoptotic cell death. Furthermore, our data indicate that the HpL3-4 cell line may provide a novel and sensitive system for isolation of CVB3 from clinical specimens.
Dissertations / Theses on the topic "Shadow of prion protein gene"
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Premzl, Marko, and Premzl@anu edu au premzl@excite com Marko. "Prion Protein Gene and Its Shadow." The Australian National University. The John Curtin School of Medical Research, 2004. http://thesis.anu.edu.au./public/adt-ANU20050328.164529.
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Prion protein (PrP) is best known for its involvement in prion diseases. A normal, dynamic isoform of prion protein (PrP^C) transforms into a pathogenic, compact isoform (PrP^Sc) during prion disease pathogenesis. The PrP^Sc, acting as a template upon which PrP^C molecules are refolded into a likeness of itself, accumulates in the brain neurones and causes disease. It is the only known component of prions, proteinaceous infectious particles. Both prion protein isoforms have the same primary amino acid structure and are encoded by the same prion protein gene (PRNP). PRNP determines susceptibility/disposition to prion diseases and their phenotypes.¶The normal function of PRNP is elusive. The Prnp knock-out mice with disrupted ORF show only very subtle phenotype. A number of hypotheses were proposed on the function of mammalian PRNP. The extracellular, GPI-anchored, glycosylated mammalian PrP^C expressed in a heterogenous set of cells could: transport copper from extracellular to intracellular milieu, buffer copper from synapse, contribute to redox signalling, act neuroprotectively, mediate cell-cell contacts, affect lymphocyte activation, participate in nucleic acid metabolism, be a memory molecule, and be a signal-transduction protein.¶ Experimental evidence demonstrated a redundancy between the PRNP and another, unknown gene. The critical issue therefore is to discover new genes homologous with PRNP, candidates for this redundancy. Using unpublished data, a sequence of zebrafish cDNA sequenced by Prof. Tatjana Simonics group (University of Milan, Italy), I discovered a new paralogue of PRNP. By searching manually, and in a targeted fashion, data deposited in public biological databases, I compiled support for the new human gene Shadow of prion protein (SPRN) including the direct evidence, homology-based evidence and ab initio gene prediction. The protein product called Shadoo (shadow in Japanese) is an extracellular, potentially glycosylated and GPI-anchored protein of a mature size of 100-odd amino acids. It is conserved from fish (zebrafish, Fugu, Tetraodon) to mammals (human, mouse, rat), and exhibits similarity of overall protein features with PrP. Most remarkably, the Sho is the first human/mammalian protein apart from PrP that contains the middle hydrophobic region that is essential for both normal and pathogenic properties of PrP. As this region is critical for heterodimerization of PrP, Sho may have potential to interact with PrP and is a likely candidate for the Protein X. Mammalian SPRN could be predominantly expressed in brain (Tatjana Simonic Lab, University of Milan, Italy).¶ Using the same approach to search public databases, I found, in addition, a fish duplicate of SPRN called SPRNB, and defined a new vertebrate SPRN gene family. Further, I also expanded a number of known fish genes from the PRNP gene family. The total number of the new genes that I discovered is 11. With the representatives of two vertebrate gene family datasets in hand, I conducted comparative genomic analysis in order to determine evolutionary trajectories of the SPRN and PRNP genes. This analysis, complemented with phylogenetic studies (Dr. Lars Jermiin, University of Sydney, Australia), demonstrated conservative evolution of the mammalian SPRN gene, and more relaxed evolutionary constraints acting on the mammalian PRNP gene. This evolutionary dialectic challenges widely adopted view on the highly conserved vertebrate PRNP and indicates that the SPRN gene may have more prominent function. More conserved Sprn could therefore substitute for the loss of less conserved, dispensable Prnp in the Prnp knock-out mice. Furthermore, the pathogenic potential of PRNP may be a consequence of relaxed evolutionary constraints.¶ Depth of comparative genomic analysis, strategy to understand biological function, depends on the number of species in comparison and their relative evolutionary distance. To understand better evolution and function of mammalian PRNP, I isolated and characterized the PRNP gene from Australian model marsupial tammar wallaby (Macropus eugenii). Marsupials are mammals separated from their eutherian relatives by roughly 180 million years. Comparison of the tammar wallaby and Brazilian opossum PrP with other vertebrate PrPs indicated patterns of evolution of the PrP regions. Whereas the repeat region is conserved within lineages but differs between lineages, the hydrophobic region is invariably conserved in all the PrPs. Conservation of PrP between marsupials and eutherians suggests that marsupial PrP could have the same pathogenic potential as eutherian PrPs. Using the marsupial PRNP gene in comparison with the PRNP genes from eutherian species in which prion diseases occur naturally (human, bovine, ovine) or experimentally (mouse), I defined gene regions that are conserved mammalian-wide and showed the utility of the marsupial genomic sequence for cross-species comparisons. These regions are potential regulatory elements that could govern gene expression and posttranscriptional control of mRNA activity. These findings shed new light on the normal function of mammalian PRNP supporting best the signal-transduction hypothesis. The normal function of PRNP may be triggering of signalling cascades which contribute to cell-cell interactions and may act anti-apoptotically. Yet, in the heterogenous set of cells expressing PrP^C these pathways will contribute to a number of cell-specific phenotypes, such as the synaptic plasticity and activation of lymphoid cells.
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Mead, Simon Harvey. "Molecular genetic analysis of the prion protein gene locus in human prion disease." Thesis, Imperial College London, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.417947.
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Moore, Richard C. "Gene targeting studies at the mouse prion protein locus." Thesis, University of Edinburgh, 1997. http://hdl.handle.net/1842/11184.
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The prion protein (PrPc) is a normal host-encoded glycoprotein which accumulates as a disease specific protease-resistant isoform (PrPsc) in the brains of infected hosts. In a number of species PrP polymorphisms and germline mutations are associated with the modulation of disease phenotype and the occurrence of familial prion disease. To investigate the biological consequences of manipulation of the prion protein in mice a flexible two step double replacement gene targeting strategy was developed. This method can be used to generate a series of mouse lines with alterations to the mouse prion protein gene (Prn-p). To facilitate gene targeting studies a restriction map of the 129/Ola Prn-p locus was constructed and a series of overlapping genomic clones were retrieved from a λ DASH II bacteriophage 129/Ola library. The double replacement strategy was used to generate PrP deficient mice and mice with subtle alterations to PrP codons 108 and 189. Murine PrP 108F/V_189L/T dimorphisms give rise to 2 distinct PrP allotypes, PrP-A and PrP-B and these are postulated to be responsible for the control of incubation time following challenge with a wide range of prion inocula. To test this proposal the endogenous 129/Ola PrP-A allotype [108L_189T] was converted by gene targeting to encode the PrP-B allotype [108F_189V]. Mice bearing codon 108 and 189 alterations were challenged with mouse adapted BSE isolate 301V. Gene targeting in 129/Ola derived HM-1 ES cells and breeding with 129/Ola mice enabled the investigation of the effect of PrP alterations in the absence of PrP overexpression artefacts or the influence of non-Prn-p genes. The dramatic acceleration of incubation time in mice homozygous for the Prn-pa[108F_189V] gene targeted allele confirmed the major role of codons 108 and 189 in the control of BSE isolate 301V incubation time - and probably other prion isolates. This data provides the strongest evidence yet that the incubation time control, long attributed to the action of different alleles of Sinc (Prn-i), is determined by PrP codon 108L/F and 189T/V dimorphisms.
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Soldevila, Trepat Marta. "Genetic variation in humans and chimpanzees in the prion protein gene." Doctoral thesis, Universitat Pompeu Fabra, 2005. http://hdl.handle.net/10803/7189.
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En el gen de la proteïna priònica, o PRNP, hem observat que el particular patró de variació que hem trobat basant-nos en dades de seqüenciació en humans es deu a selecció positiva, i que el mètode utilitzat per detectar selecció és crític. Utilitzant dades basades en SNPs es pot introduir un biaix al aplicar tests de neutralitat basats en diversitat de seqüències, i això pot portar a conclusions errònies. A més, hem vist que els polimorfismes en els codons 129 i 219 presenten gran diferències de freqüència en diferents poblacions humanes i també hem vist que aquestes posicions estan fixades en ximpanzés. La variació trobada en controls ha estat comparada amb el patró de variació existent en pacients per la mateixa regió. La reseqüenciació del gen PRNP en un gran nombre de mostres humanes i de ximpanzés ens ha permès obtenir un gran nombre d´informació d´aquest gen.In the prion gene or PRNP, we have observed that the particular pattern of variation that we have found in this gene based on sequencing data in humans is due to positive selection, and that the method and the approach used to detect this selection critical. Ascertainment bias can be introduced by using SNP data and applying neutrality tests based on sequence diversity, therefore leading to anomalous conclusions being drawn. Moreover, we have seen that polymorphisms in codon 129 and 219 have big differences in frequency in different human populations and we have also seen that these positions are fixed in chimpanzees. The normal variation that we found in controls have been then compared with patients for the same region. The resequencing of PRNP in a very large sample of humans and chimpanzees has provided a great deal of information on this gene.
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Thumdee, Patama. "The prenatal expression of mRNA and protein of the prion protein gene, PRNP, in sheep." [S.l.] : [s.n.], 2007. http://deposit.ddb.de/cgi-bin/dokserv?idn=983755728.
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Uzun, Begum. "Surveillance Of Prion Protein (prp) Gene Polymorphisms In Turkish Native Sheep Breeds." Master's thesis, METU, 2012. http://etd.lib.metu.edu.tr/upload/12614353/index.pdf.
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v
It was found that most of the classical scrapie genotypes belong to R3 risk group,
whereas atypical scrapie genotypes belonging to zero (0) and one (1) risk groups were
frequently seen in sheep analyzed. In other words, Turkish sheep is found to have
intermediate risk of classical scrapie and low atypical scrapie risk, in general.
The data from the current study may help to establish a breeding program for classical
scrapie control in Turkey and will be beneficial for both the animal and public health in
the country. In addition, the outcomes of the study will fill the gap which is present in
the geographic distribution data of PrP gene polymorphisms in Eurasia.Scrapie is an infectious fatal disease of sheep and goats which affects the central nervous
system. In the present study, samples of 14 native Turkish sheep breeds (n=655) were
analyzed with respect to their polymorphisms of PrP gene (at codons: 136, 141, 154 and
171) and their classical and atypical scrapie risk levels were identified.
Turkish sheep are found to have the highest PrP genetic variability with 13 classical
scrapie alleles and 14 atypical scrapie alleles compared to all previous studies. Classical
scrapie-susceptible and wild-type ARQ allele was found as the most frequent allele in
Turkish sheep examined. The most classical scrapie-susceptible allele, VRQ was
detected at low frequencies in 5 of the breeds (Çine Ç
apari, Dagliç
, Kivircik, Karayaka and Gö
kç
eada). One novel allele (TL141HQ) was observed in Sakiz breed for the first time in this study.
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Mallucci, Giovanna Rachele. "Prion protein gene knockout in the mouse using the Cre/1oxP system." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.271231.
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Mahal, Sukhvir Paul. "Isolation and characterisation of the promoter region of the human prion protein gene." Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313746.
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Peralta, Oscar Alejandro. "Developmental Regulation of Prion Expression in Cattle and Mouse Embryonic Stem Cells." Diss., Virginia Tech, 2008. http://hdl.handle.net/10919/28584.
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The host encoded cellular prion protein (PrPC) is an N-linked glycoprotein tethered to the cell membrane by a glycophosphatidylinositol (GPI) anchor. Under certain conditions, PrPC can undergo conversion into a conformationally-altered isoform (PrPSc) widely believed to be the pathogenic agent of transmissible spongiform encephalopathies (TSEs). Thus, tissues expressing PrPC are potential sites for conversion of PrPSc during TSE pathogenesis. Although much is known about the role of PrPSc in prion diseases, the normal function of PrPC is poorly understood. Lines of mice and cattle in which PrPC has been ablated by gene knockout show no major phenotypical alterations other than resistance to TSE infection. However, recent reports using Prnp-null mouse models have suggested the participation of PrPC in neural stem/progenitor cell proliferation and differentiation. The first objective in our study was to map the expression of PrPC in twenty six somatic and reproductive tissues in ruminants. Our second objective was to characterize the ontogeny of PrPC expression during bovine embryonic and early fetal development. Finally, we used a mouse embryonic stem cell (mESC) model to study the potential role of PrPC during neurogenesis. In adult tissues, intense expression of PrPC was detected in the central nervous system (CNS), thymus and testes, whereas the liver, striated muscle and female reproductive tissues showed the lowest expression. We observed that PrPC was associated with tissues undergoing cellular differentiation including spermatogenesis, lymphocyte activation and hair follicle regeneration. Analyses in bovine embryos and fetuses indicated peaks in expression of PrPC at days 4 and 18 post-fertilization, stages associated with the maternal-zygote transition and the maternal recognition of pregnancy and initiation of placental attachment, respectively. Later in development, PrPC was expressed in the CNS where it was localized in mature neurons of the neuroepithelium and emerging neural trunks. Based on these observations, we hypothesized that PrPC was involved in neurogenesis. We tested this hypothesis in a murine embryonic stem cell model (mESC). mESC were induced to form embryoid bodies (EBs) by placing them in suspension culture under differentiating conditions and allowed to differentiate in vitro for 20 days. We detected increasing levels of PrPC starting on day 12 (8.21- fold higher vs. day 0; P < 0.05) and continuing until day 20 (20.77-fold higher vs. day 0; P < 0.05). PrPC expression was negatively correlated with pluripotency marker Oct-4 (r= -0.85) confirming that mESC had indeed differentiated. To provide a more robust system for assessing the role of PrPC in neural differentiation, mESC were cultured with or without retinoic acid (RA) to encourage differentiation into neural lineages. Induction of EBs with retinoic acid (RA) resulted in an earlier up-regulation of PrPC and nestin (day 12 vs. day 16; P < 0.05). In addition, immunofluorescence studies indicated co-expression of PrPC and nestin in the same cells. The results of these experiments suggested a temporal link between PrPC expression and expression of nestin, a marker of neural progenitor cells. We next tested whether PrPC was involved in RA-enhanced neural differentiation from mESC using a PrPC knockdown model. Plasmid vectors designed to express either a PrP-targeted shRNA or scrambled, control shRNA were transfected into mESC. Stable transfectants were selected under G418 and cloned. PrP-targeted and control shRNA clones, as well as wild-type mESC, were differentiated in presence of RA and sampled as above. PrPC expression was knocked down in PrP-targeted shRNA cultures between days 12 and 20 (62.2 % average reduction vs. scrambled shRNA controls). Nestin expression was reduced at days 16 and 20 in PrPC knockdown cells (61.3% and 70.7%, respectively vs. scrambled shRNA controls). These results provide evidence that PrPC plays a role in the neural differentiation at a point up-stream from the stages at which nestin is expressed. In conclusion, the widely distributed expression of PrPC in ruminant tissues suggests an important biological role for this protein. In the present work we have provided evidence for the participation of PrPC in the differentiation of mESC along the neurogenic pathway.Ph. D.
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Ribeiro, Fernanda Trentini Lopes. "Polimorfismo do gene da proteína prion celular (prpc) e imunohistoquímica de tecido linfóide em ovinos = Polymorphism of cellular prion protein (PrPC) and immunohistochemistry of lymphoid tissue of sheep / Fernanda Trentini Lopes Ribeiro ; orientadora, Cristina Santos Sotomaior." reponame:Biblioteca Digital de Teses e Dissertações da PUC_PR, 2011. http://www.biblioteca.pucpr.br/tede/tde_busca/arquivo.php?codArquivo=2231.
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Dissertação (mestrado) - Pontifícia Universidade Católica do Paraná, São José dos Pinhais, 2011Inclui bibliografias
Scrapie é uma doença neurodegenerativa, progressiva e fatal de ovinos e caprinos, pertencente ao grupo das Encefalopatias Espongiformes Transmissíveis (EETs), ou doenças priônicas. O acúmulo de uma isoforma normal (PrPSc) da proteína prion celular (PrPC)
Scrapie is a fatal, neurodegenerative disease that affects sheep and goats and belongs to the Transmissible Spongiform Encephalopathies (TSEs) or prion diseases. It is caused by the deposition of an abnormal isoform (PrPSc) of the host-encoded cellular pr
Books on the topic "Shadow of prion protein gene"
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Mouillet-Richard, Sophie, and Jean-Luc Vilotte, eds. Promiscuous Functions of the Prion Protein Gene Family. Frontiers Media SA, 2015. http://dx.doi.org/10.3389/978-2-88919-605-0.
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Hope, James, and Mark P. Dagleish. Prion-protein-related diseases of animals and man. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198570028.003.0041.
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Scrapie, bovine spongiform encephalopathy (BSE), Creutzfeldt–Jakob disease (CJD), and related diseases of mink (transmissible mink encephalopathy), mule deer and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE). These diseases can be transmitted by prions from affected to healthy animals by inoculation or by feeding diseased tissues. Prions are cellular proteins that can transfer metabolic and pathological phenotypes vertically from parent to progeny or horizontally between cells and animals. TSEs are characterised by the accumulation of the prion form of the mammalian prion protein (PrPC) in the central nervous system or peripheral tissues of animals and humans. Mutations of the human PrP gene are linked to rare, familial forms of disease and prion-protein gene polymorphisms in humans and other species are linked to survival time and disease characteristics in affected individuals. Iatrogenic transmission of CJD in man has occurred, and a variant form of CJD (vCJD) is due to cross-species transmission of BSE from cattle to humans. Atypical forms of scrapie and BSE have been identified during large-scale monitoring for TSEs worldwide. This chapter outlines our current understanding of scrapie, BSE, CJD and other TSEs and highlights recent progress in defining the role in disease of the prion protein, PrP.
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Mastrianni, James A., and Joshuae G. Gallardo. Prion Diseases. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0166.
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Prion diseases are transmissible fatal neurodegenerative disorders resulting from the accumulation of misfolded prion protein. Although primarily sporadic diseases, 5% to 10% result from a mutation of the prion protein gene (PRNP), and less than 1% occur from exposure to prions. The current family of prion diseases includes Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker disease (GSS), fatal insomnia (FI), variant CJD (vCJD), and variably protease-sensitive prionopathy (VPSPr). Kuru is a disease of historical interest that was transmitted through cannibalistic rituals. Iatrogenic CJD (iCJD) is the result of secondary transmission of prion disease from contaminated biologicals.
Book chapters on the topic "Shadow of prion protein gene"
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Nitrini, Ricardo, Sergio Rosemberg, Maria Rita Passos-Bueno, Luis S. Texeira da Silva, Paula Iughetti, Maria Papadopoulos, P. M. Carrilho, et al. "Human Prion Protein Gene Mutation at Codon 183 Associated with an Atypical Form of Prion Disease." In Prions and Brain Diseases in Animals and Humans, 25–32. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1896-3_3.
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Gupta, N., S. Choudhary, G. Malik, A. Pandey, and S. C. Gupta. "Single Nucleotide Polymorphism (SNP) in Prion Protein Gene (PRNP) exon-3 in Gaddi Sheep." In Animal Genomics for Animal Health, 261–66. Basel: KARGER, 2008. http://dx.doi.org/10.1159/000317169.
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Zecevic, Ervin, Admir Dokso, Alma Rustempasic, and Muhamed Brka. "Polymorphisms of the ovine prion protein (PrP) Gene in the Pramenka Sheep Breed Population(s) in Bosnia and Herzegovina - Kupreski Strain." In 30th Scientific-Experts Conference of Agriculture and Food Industry, 109–16. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-40049-1_14.
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Nihat, Akin, TzeHow Mok, and John Collinge. "Prion disease." In New Oxford Textbook of Psychiatry, edited by John R. Geddes, Nancy C. Andreasen, and Guy M. Goodwin, 414–23. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198713005.003.0042.
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Prion diseases are fatal neurodegenerative conditions that may arise sporadically or be inherited or acquired by environmental exposure to infectious prions—transmissible agents composed of multimeric assemblies of misfolded protein. The core clinical features are progressive cognitive decline, accompanied with ataxia, myoclonus, and pyramidal or extra-pramidal motor signs. While the most common form—sporadic Creutzfeldt–Jakob disease—is generally rapidly progressive over weeks or months, inherited prion diseases can span many years, with diverse clinical features readily mimicking other neurodegenerative diseases. Psychiatric features, including agitation, anxiety, depression, hallucinations, and behavioural disturbances, are common in the early stages. Diagnosis can usually be made with confidence by the combination of clinical criteria, diffusion-weighted magnetic resonance imaging, electroencephalogram, and specialized cerebrospinal fluid analysis. Inherited prion disease can be confirmed with prion protein gene analysis, which should be considered in all early-onset dementing and ataxic conditions. It is now becoming clear that the fundamental molecular pathogenesis—seeded protein polymerization—is relevant to other neurodegenerative diseases, notably Alzheimer’s disease.
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Ironside, James W. "Human Prion Diseases." In Escourolle and Poirier's Manual of Basic Neuropathology, 159–71. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190675011.003.0006.
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Human prion diseases include idiopathic, genetic, and acquired disorders. Heterogeneous clinicopathologic features make diagnosis challenging. Accurate diagnosis requires a combined clinical, neuropathologic, genetic, and biochemical approach. Neuropathologic assessment is performed following autopsy in most cases. The brain is sampled and studied by tinctorial stains and immunohistochemistry for disease-associated form of the prion protein. Unfixed frozen brain tissue is retained for Western blot analysis of protease-resistant prion protein isoform and for DNA extraction to sequence the prion protein gene. Assessment of spongiform change, gliosis neuronal loss, and accumulation of disease-associated prion protein in the brain can help to determine major categories of human prion disease. Additional clinical, genetic, and biochemical data allow diagnosis and subclassification into disease subtypes, particularly in sporadic Creutzfeldt–Jakob disease. Neuropathology continues to play a role in the recognition and understanding of the expanding spectrum of human prion disease and identification of disease variants that may emerge in the future.
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Urwin, Patrick JM, and Anna M. Molesworth. "The neuroepidemiology of human prion disease." In Oxford Textbook of Neurologic and Neuropsychiatric Epidemiology, edited by Carol Brayne, Valery L. Feigin, Lenore J. Launer, and Giancarlo Logroscino, 367–78. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198749493.003.0035.
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Human prion diseases comprise a number of rare and fatal neurodegenerative conditions that result from the accumulation in the central nervous system of an abnormal form of a naturally occurring protein, called the prion protein. The diseases occur in genetic, sporadic, and acquired forms: genetic disease is associated with mutations in the prion protein gene (PRNP); sporadic disease is thought to result from a spontaneous protein misfolding event; acquired disease results from transmission of infection from an animal or another human. The potential transmissibility of the prion in any of these forms, either in disease states or during the incubation period, has implications for public health. Here we focus on Creutzfeldt-Jakob Disease (CJD), including variant Creutzfeldt-Jakob Disease (vCJD), although we will also discuss other forms of human prion disease.
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McKinley, Michael P., Frank M. Longo, Janice S. Valletta, Fonda Rahbar, Rachael L. Neve, Stanley B. Prusiner, and William C. Mobley. "Chapter 19 Nerve growth factor induces gene expression of the prion protein and βbT-amyloid protein precursor in the developing hamster central nervous system." In Progress in Brain Research, 227–38. Elsevier, 1990. http://dx.doi.org/10.1016/s0079-6123(08)63180-5.
Full textConference papers on the topic "Shadow of prion protein gene"
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GHETTI, BERNARDINO, LETICIA MIRAVALLE, KEIJI YAMAGUCHI, FRANCINE EPPERSON, JILL R. MURRELL, TONY PERKINS, SIU HUI, et al. "ROLE OF THE POLYMORPHISM AT CODON 129 OF THE PRION PROTEIN GENE IN THE PHENOTYPIC EXPRESSION OF GERSTMANN-STRÄUSSLER-SCHEINKER DISEASE ASSOCIATED WITH THE F198S MUTATION." In The 32nd Session of International Seminars and International Collaboration. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812701787_0015.
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