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Journal articles on the topic 'Shadow of prion protein gene'

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Published: 4 June 2021

Last updated: 29 January 2023

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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.

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11

Caramelli, Paulo. "Prion protein gene in Alzheimer's disease." Arquivos de Neuro-Psiquiatria 71, no. 7 (July 2013): 419–20. http://dx.doi.org/10.1590/0004-282x20130093.

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12

Kovács, Gábor G., Gianriccardo Trabattoni, Johannes A. Hainfellner, James W. Ironside, Richard S. G. Knight, and Herbert Budka. "Mutations of the Prion Protein Gene." Journal of Neurology 249, no. 11 (November 1, 2002): 1567–82. http://dx.doi.org/10.1007/s00415-002-0896-9.

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13

Schätzl, Hermann M., Maria Da Costa, Leslie Taylor, Fred E. Cohen, and Stanley B. Prusiner. "Prion Protein Gene Variation Among Primates." Journal of Molecular Biology 245, no. 4 (January 1995): 362–74. http://dx.doi.org/10.1006/jmbi.1994.0030.

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14

Schätzl, Hermann M., Maria Da Costa, Leslie Taylor, Fred E. Cohen, and Stanley B. Prusiner. "Prion protein gene variation among primates." Journal of Molecular Biology 265, no. 2 (January 1997): 257. http://dx.doi.org/10.1006/jmbi.1996.0791.

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15

Sakudo, Akikazu, Takashi Onodera, and Kazuyoshi Ikuta. "Prion Protein Gene-Deficient Cell Lines: Powerful Tools for Prion Biology." Microbiology and Immunology 51, no. 1 (January 2007): 1–13. http://dx.doi.org/10.1111/j.1348-0421.2007.tb03877.x.

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16

Resende, Catarina G., Tiago F. Outeiro, Laina Sands, Susan Lindquist, and Mick F. Tuite. "Prion protein gene polymorphisms in Saccharomyces cerevisiae." Molecular Microbiology 49, no. 4 (July 4, 2003): 1005–17. http://dx.doi.org/10.1046/j.1365-2958.2003.03608.x.

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17

Scott, Michael R. D., Darel A. Butler, Dale E. Bredesen, Monika Wälchli, Karen K. Hsiao, and Stanley B. Prusiner. "Prion protein gene expression in cultured cells." "Protein Engineering, Design and Selection" 2, no. 1 (1988): 69–76. http://dx.doi.org/10.1093/protein/2.1.69.

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18

Jeong, Min-Ju, and Byung-Hoon Jeong. "No polymorphisms in the coding region of the prion-like protein gene in Thoroughbred racehorses." Acta Veterinaria Hungarica 67, no. 2 (June 2019): 174–82. http://dx.doi.org/10.1556/004.2019.019.

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Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of an abnormal prion protein isoform (PrPSc), which is converted from the normal prion protein (PrPC). Prion diseases have been reported in an extensive number of species but not in horses up to now; therefore, horses are known to be a species resistant to prion diseases. The prion-like protein gene (PRND) is closely located downstream of the prion protein gene (PRNP) and the prion-like protein (Doppel) is a homologue with PrP. Previous studies have shown that an association between prion diseases and polymorphisms of the PRND gene is reported in the main hosts of prion diseases. Hence, we examined the genetic variations of the PRND gene in Thoroughbred horses. Interestingly, polymorphisms of the PRND gene were not detected. In addition, we conducted a comparative analysis of the amino acid sequences of the PRND gene to identify the differences between horses and other species. The amino acid sequence of the horse PRND gene showed the highest identity to that of sheep (83.7%), followed by that of goats, cattle and humans. To the best of our knowledge, this is the first genetic study of the PRND gene in horses.

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19

Mastrangelo, Peter, and David Westaway. "Biology of the prion gene complex." Biochemistry and Cell Biology 79, no. 5 (October 1, 2001): 613–28. http://dx.doi.org/10.1139/o01-142.

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The prion protein gene Prnp encodes PrPSc, the major structural component of prions, infectious pathogens causing a number of disorders including scrapie and bovine spongiform encephalopathy (BSE). Missense mutations in the human Prnp gene, PRNP, cause inherited prion diseases such as familial CreutzfeldtJakob Disease. In uninfected animals, Prnp encodes a GPI-anchored protein denoted PrPC, and in prion infections, PrPCis converted to PrPScby templated refolding. Although Prnp is conserved in mammalian species, attempts to verify interactions of putative PrP-binding proteins by genetic means have proven frustrating in that two independent lines of Prnp gene ablated mice (Prnp0/0mice: ZrchI and Npu) lacking PrPCremain healthy throughout development. This indicates that PrPCserves a function that is not apparent in a laboratory setting or that other molecules have overlapping functions. Shuttling or sequestration of synaptic Cu(II) via binding to N-terminal octapeptide residues and (or) signal transduction involving the fyn kinase are possibilities currently under consideration. A new point of entry into the issue of prion protein function has emerged from identification of a paralog, Prnd, with 25% coding sequence identity to Prnp. Prnd lies downstream of Prnp and encodes the Dpl protein. Like PrPC, Dpl is presented on the cell surface via a GPI anchor and has three α-helices: however, it lacks the conformationally plastic and octapeptide repeat domains present in its well-known relative. Interestingly, Dpl is overexpressed in two other lines of Prnp0/0mice (Ngsk and Rcm0) via intergenic splicing events. These lines of Prnp0/0mice exhibit ataxia and apoptosis of cerebellar cells, indicating that ectopic synthesis of Dpl protein is toxic to CNS neurons: this inference has now been confirmed by the construction of transgenic mice expressing Dpl under the direct control of the PrP promoter. Remarkably, Dpl-programmed ataxia is rescued by wt Prnp transgenes. The interaction between the Prnp and Prnd genes in mouse cerebellar neurons may have a physical correlate in competition between Dpl and PrPCwithin a common biochemical pathway that, when misregulated, leads to apoptosis.Key words: spongiform encephalopathy, neurodegenerative disease, paralogs, scrapie, CJD.

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20

Slate, Jon. "Molecular evolution of the sheep prion protein gene." Proceedings of the Royal Society B: Biological Sciences 272, no. 1579 (September 20, 2005): 2371–77. http://dx.doi.org/10.1098/rspb.2005.3259.

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21

Richt, Jürgen A., and S. Mark Hall. "BSE Case Associated with Prion Protein Gene Mutation." PLoS Pathogens 4, no. 9 (September 12, 2008): e1000156. http://dx.doi.org/10.1371/journal.ppat.1000156.

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22

Kretzschmar, H. A., M. Neumann, G. Riethmuller, and S. B. Prusiner. "Molecular cloning of a mink prion protein gene." Journal of General Virology 73, no. 10 (October 1, 1992): 2757–61. http://dx.doi.org/10.1099/0022-1317-73-10-2757.

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23

Abe, E., C. Wada, T. Hatakeyama, F. Takeda, K. Obara, M. Kobayashi, T. Imota, et al. "Clinical benefit of the prion protein gene screening." Journal of the Neurological Sciences 357 (October 2015): e109. http://dx.doi.org/10.1016/j.jns.2015.08.349.

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24

Billinis, Charalambos, Cynthia H. Panagiotidis, Vassilios Psychas, Stamatis Argyroudis, Anna Nicolaou, Sotirios Leontides, Orestis Papadopoulos, and Theodoros Sklaviadis. "Prion protein gene polymorphisms in natural goat scrapie." Journal of General Virology 83, no. 3 (March 1, 2002): 713–21. http://dx.doi.org/10.1099/0022-1317-83-3-713.

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A total of 51 goats, including seven clinical cases, from the first herd in Greece reported to have scrapie was examined to discern an association between scrapie susceptibility and polymorphisms of the gene encoding the prion protein (PrP). Each animal was evaluated for clinical signs of the disease, histopathological lesions associated with scrapie, the presence of detectable protease-resistant PrP in the brain and PrP genotype. Eleven different PrP genotypes encoding at least five unique predicted mature PrP amino acid sequences were found. These genotypes included the amino acid polymorphisms at codons 143 (H→R) and 240 (S→P) and ‘silent’ nucleotide alterations at codons 42 (a→g) and 138 (c→t). Additionally, novel caprine amino acid polymorphisms were detected at codons 21 (V→A), 23 (L→P), 49 (G→S), 154 (R→H), 168 (P→Q) and 220 (Q→H) and new silent mutations were found at codons 107 (g→a) and 207 (g→a). The following variants were found in scrapie-affected goats: VV21, LL23, GG49, SS49, HH143, HR143, RR154, PP168, PP240, SP240 and SS240. All scrapie-affected animals carried the HH143RR154 genotype, with the exception of two goats (HR143), both of which had detectable protease-resistant PrP but showed no clinical signs or histopathological lesions characteristic of scrapie.

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25

Palmer, Mark S., and John Collinge. "Mutations and polymorphisms in the prion protein gene." Human Mutation 2, no. 3 (1993): 168–73. http://dx.doi.org/10.1002/humu.1380020303.

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26

McKinley, Michael P., Bruce Hay, Vishwanath R. Lingappa, Ivan Lieberburg, and Stanley B. Prusiner. "Developmental expression of prion protein gene in brain." Developmental Biology 121, no. 1 (May 1987): 105–10. http://dx.doi.org/10.1016/0012-1606(87)90143-6.

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27

Singh, Neena, Gianluigi Zanusso, Shu G. Chen, Hisashi Fujioka, Sandra Richardson, Pierluigi Gambetti, and Robert B. Petersen. "Prion Protein Aggregation Reverted by Low Temperature in Transfected Cells Carrying a Prion Protein Gene Mutation." Journal of Biological Chemistry 272, no. 45 (November 7, 1997): 28461–70. http://dx.doi.org/10.1074/jbc.272.45.28461.

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28

Mironova, Ludmila N. "Protein inheritance and regulation of gene expression in yeast." Ecological genetics 8, no. 4 (December 15, 2010): 10–16. http://dx.doi.org/10.17816/ecogen8410-16.

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Prions of lower eukaryotes are genetic determinants of protein nature. Last years are marked by rapid development of the conception of prion inheritance. The list of yeast proteins, which have been shown to exist in the prion form in vivo, and phenotypic manifestation of prions provide good reason to believe that protein prionization may represent epigenetic mechanism regulating adaptability of a single cell and cellular population to environmental conditions.

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29

Won, Sae-Young, Yong-Chan Kim, Kyoungtag Do, and Byung-Hoon Jeong. "Absence of Strong Genetic Linkage Disequilibrium between Single Nucleotide Polymorphisms (SNPs) in the Prion Protein Gene (PRNP) and the Prion-Like Protein Gene (PRND) in the Horse, a Prion-Resistant Species." Genes 11, no. 5 (May 7, 2020): 518. http://dx.doi.org/10.3390/genes11050518.

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Prion disease is a fatal neurodegenerative disorder caused by a deleterious prion protein (PrPSc). However, prion disease has not been reported in horses during outbreaks of transmissible spongiform encephalopathies (TSEs) in various animals in the UK. In previous studies, single nucleotide polymorphisms (SNPs) in the prion protein gene (PRNP) have been significantly associated with susceptibility to prion disease, and strong linkage disequilibrium (LD) between PRNP and prion-like protein gene (PRND) SNPs has been identified in prion disease-susceptible species. On the other hand, weak LD values have been reported in dogs, a prion disease-resistant species. In this study, we investigated SNPs in the PRND gene and measured the LD values between the PRNP and PRND SNPs and the impact of a nonsynonymous SNP found in the horse PRND gene. To identify SNPs in the PRND gene, we performed direct sequencing of the PRND gene. In addition, to assess whether the weak LD value between the PRNP and PRND SNPs is a characteristic of prion disease-resistant animals, we measured the LD value between the PRNP and PRND SNPs using D’ and r2 values. Furthermore, we evaluated the impact of a nonsynonymous SNP in the Doppel protein with PolyPhen-2, PROVEAN, and PANTHER. We observed two novel SNPs, c.331G > A (A111T) and c.411G > C. The genotype and allele frequencies of the c.331G > A (A111T) and c.411G > C SNPs were significantly different between Jeju, Halla, and Thoroughbred horses. In addition, we found a total of three haplotypes: GG, AG, and GC. The GG haplotype was the most frequently observed in Jeju and Halla horses. Furthermore, the impact of A111T on the Doppel protein was predicted to be benign by PolyPhen-2, PROVEAN, and PANTHER. Interestingly, a weak LD value between the PRNP and PRND SNPs was found in the horse, a prion disease-resistant animal. To the best of our knowledge, these results suggest that a weak LD value could be one feature of prion disease-resistant animals.

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30

Cardinale, Alessio, and Silvia Biocca. "Gene-Based Antibody Strategies for Prion Diseases." International Journal of Cell Biology 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/710406.

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Prion diseases or transmissible spongiform encephalopathies (TSE) are a group of neurodegenerative and infectious disorders characterized by the conversion of a normal cellular protein PrPCinto a pathological abnormally folded form, termed PrPSc. There are neither available therapies nor diagnostic tools for an early identification of individuals affected by these diseases. New gene-based antibody strategies are emerging as valuable therapeutic tools. Among these, intrabodies are chimeric molecules composed by recombinant antibody fragments fused to intracellular trafficking sequences, aimed at inhibiting,in vivo, the function of specific therapeutic targets. The advantage of intrabodies is that they can be selected against a precise epitope of target proteins, including protein-protein interaction sites and cytotoxic conformers (i.e., oligomeric and fibrillar assemblies). Herein, we address and discussin vitroandin vivoapplications of intrabodies in prion diseases, focussing on their therapeutic potential.

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31

Kim, Yong-Chan, Sae-Young Won, and Byung-Hoon Jeong. "Identification of Prion Disease-Related Somatic Mutations in the Prion Protein Gene (PRNP) in Cancer Patients." Cells 9, no. 6 (June 17, 2020): 1480. http://dx.doi.org/10.3390/cells9061480.

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Prion diseases are caused by misfolded prion protein (PrPSc) and are accompanied by spongiform vacuolation of brain lesions. Approximately three centuries have passed since prion diseases were first discovered around the world; however, the exact role of certain factors affecting the causative agent of prion diseases is still debatable. In recent studies, somatic mutations were assumed to be cause of several diseases. Thus, we postulated that genetically unstable cancer tissue may cause somatic mutations in the prion protein gene (PRNP), which could trigger the onset of prion diseases. To identify somatic mutations in the PRNP gene in cancer tissues, we analyzed somatic mutations in the PRNP gene in cancer patients using the Cancer Genome Atlas (TCGA) database. In addition, to evaluate whether the somatic mutations in the PRNP gene in cancer patients had a damaging effect, we performed in silico analysis using PolyPhen-2, PANTHER, PROVEAN, and AMYCO. We identified a total of 48 somatic mutations in the PRNP gene, including 8 somatic mutations that are known pathogenic mutations of prion diseases. We identified significantly different distributions among the types of cancer, the mutation counts, and the ages of diagnosis between the total cancer patient population and cancer patients carrying somatic mutations in the PRNP gene. Strikingly, although invasive breast carcinoma and glioblastoma accounted for a high percentage of the total cancer patient population (9.9% and 5.4%, respectively), somatic mutations in the PRNP gene have not been identified in these two cancer types. We suggested the possibility that somatic mutations of the PRNP gene in glioblastoma can be masked by a diagnosis of prion disease. In addition, we found four aggregation-prone somatic mutations, these being L125F, E146Q, R151C, and K204N. To the best of our knowledge, this is the first specific analysis of the somatic mutations in the PRNP gene in cancer patients.

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Ryskalin, Larisa, Carla L. Busceti, Francesca Biagioni, Fiona Limanaqi, Pietro Familiari, Alessandro Frati, and Francesco Fornai. "Prion Protein in Glioblastoma Multiforme." International Journal of Molecular Sciences 20, no. 20 (October 15, 2019): 5107. http://dx.doi.org/10.3390/ijms20205107.

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The cellular prion protein (PrPc) is an evolutionarily conserved cell surface protein encoded by the PRNP gene. PrPc is ubiquitously expressed within nearly all mammalian cells, though most abundantly within the CNS. Besides being implicated in the pathogenesis and transmission of prion diseases, recent studies have demonstrated that PrPc contributes to tumorigenesis by regulating tumor growth, differentiation, and resistance to conventional therapies. In particular, PrPc over-expression has been related to the acquisition of a malignant phenotype of cancer stem cells (CSCs) in a variety of solid tumors, encompassing pancreatic ductal adenocarcinoma (PDAC), osteosarcoma, breast cancer, gastric cancer, and primary brain tumors, mostly glioblastoma multiforme (GBM). Thus, PrPc is emerging as a key in maintaining glioblastoma cancer stem cells’ (GSCs) phenotype, thereby strongly affecting GBM infiltration and relapse. In fact, PrPc contributes to GSCs niche’s maintenance by modulating GSCs’ stem cell-like properties while restraining them from differentiation. This is the first review that discusses the role of PrPc in GBM. The manuscript focuses on how PrPc may act on GSCs to modify their expression and translational profile while making the micro-environment surrounding the GSCs niche more favorable to GBM growth and infiltration.

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Manson, J., J. D. West, V. Thomson, P. McBride, M. H. Kaufman, and J. Hope. "The prion protein gene: a role in mouse embryogenesis?" Development 115, no. 1 (May 1, 1992): 117–22. http://dx.doi.org/10.1242/dev.115.1.117.

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The neural membrane glycoprotein PrP (prion protein) has a key role in the development of scrapie and related neurodegenerative diseases. During pathogenesis, PrP accumulates in and around cells of the brain from which it can be isolated in a disease-specific, protease-resistant form. Although the involvement of PrP in the pathology of these diseases has long been known, the normal function of PrP remains unknown. Previous studies have shown that the PrP gene is expressed tissue specifically in adult animals, the highest levels in the brain, with intermediate levels in heart and lung and low levels in spleen. Prenatally, PrP mRNA has been detected in the brain of rat and hamster just prior to birth. In this study we have examined the expression of the PrP gene during mouse embryonic development by in situ hybridisation and observed dramatic regional and temporal gene expression in the embryo. Transcripts were detected in developing brain and spinal cord by 13.5 days. In addition, PrP gene expression was detected in the peripheral nervous system, in ganglia and nerve trunks of the sympathetic nervous system and neural cell populations of sensory organs. Expression of the PrP gene was not limited to neuronal cells, but was also detected in specific non-neuronal cell populations of the 13.5 and 16.5 day embryos and in extra-embryonic tissues from 6.5 days. This cell-specific expression suggests a pleiotropic role for PrP during development.

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Varela-Nallar, L., L. Cuitino, J. P. Sagal, and N. C. Inestrosa. "Regulation of prion protein gene expression by heavy metals." Journal of Neurochemistry 81 (June 28, 2008): 5–6. http://dx.doi.org/10.1046/j.1471-4159.81.s1.1_4.x.

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Petersen, R. B., M. T. MD, L. B. MD, B. S. MD, R. M. Torack, S. L. MS, J. J. MD, et al. "Analysis of the prion protein gene in thalamic dementia." Neurology 42, no. 10 (October 1, 1992): 1859. http://dx.doi.org/10.1212/wnl.42.10.1859.

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Westaway, D., C. Cooper, S. Turner, M. Da Costa, G. A. Carlson, and S. B. Prusiner. "Structure and polymorphism of the mouse prion protein gene." Proceedings of the National Academy of Sciences 91, no. 14 (July 5, 1994): 6418–22. http://dx.doi.org/10.1073/pnas.91.14.6418.

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Laplanche, Jean-Louis, Jacqueline Chatelain, Jean-Marie Launay, Claire Gazengel, and Michel Vidaud. "Deletion in prion protein gene in a Moroccan family." Nucleic Acids Research 18, no. 22 (1990): 6745. http://dx.doi.org/10.1093/nar/18.22.6745.

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Zhao, Hui, Xiao-Yan Wang, Wei Zou, and Ya-Ping Zhang. "Prion protein gene (PRNP) polymorphisms in native Chinese cattle." Genome 53, no. 2 (February 2010): 138–45. http://dx.doi.org/10.1139/g09-087.

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Polymorphisms in four regions of the bovine prion protein gene (PRNP) confer susceptibility to bovine spongiform encephalopathy (BSE). These polymorphisms include a 23-bp insertion/deletion (indel) in the promoter region, a 12-bp indel in intron 1, an octapeptide repeat or 24-bp indel in the open reading frame, and a single nucleotide polymorphism (SNP) in the coding region. In this study, we investigated the frequency distributions of genotypes, alleles, and haplotypes at these indel sites in 349 native Chinese cattle and sequence variants in 50 samples. Our results showed that cattle in southern China have low frequencies of the 12-bp deletion allele and the 23-bp deletion / 12-bp deletion haplotype, which have been suggested to be relevant to BSE susceptibility. Interestingly, a significant difference was observed between BSE-affected cattle and healthy Chinese cattle in the 12-bp indel polymorphism. A total of 14 SNPs were discovered in the coding region of PRNP in Chinese cattle. Three of these SNPs were associated with amino acid changes (K3T, P54S, and S154N). The E211K substitution that was recently reported in the US atypical BSE case was not detected in this study.

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O’DOHERTY, E., M. AHERNE, S. ENNIS, E. WEAVERS, J. F. ROCHE, and T. SWEENEY. "Prion protein gene polymorphisms in pedigree sheep in Ireland." Research in Veterinary Science 70, no. 1 (February 2001): 51–56. http://dx.doi.org/10.1053/rvsc.2000.0441.

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Owen, Frank, Mark Poulter, John Collinge, Martin Leach, Tarulata Shah, Raymond Lofthouse, Yanfang Chen, et al. "Insertions in the prion protein gene in atypical dementias." Experimental Neurology 112, no. 2 (May 1991): 240–42. http://dx.doi.org/10.1016/0014-4886(91)90075-n.

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MEYDAN, HASAN, ERKAN PEHLİVAN, MUSTAFA MUHIP ÖZKAN, MEHMET ALI YILDIZ, and WILFRED GOLDMANN. "Prion protein gene polymorphisms in Turkish native goat breeds." Journal of Genetics 96, no. 2 (May 18, 2017): 299–305. http://dx.doi.org/10.1007/s12041-017-0763-1.

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Yamada, M., S. Satoh, N. Sodeyama, H. Fujigasaki, K. Kaneko, Y. Wada, Y. Itoh, and M. Matsushita. "Spastic paraparesis and mutations in the prion protein gene." Journal of the Neurological Sciences 134, no. 1-2 (December 1995): 215–16. http://dx.doi.org/10.1016/0022-510x(95)00250-4.

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Abdel-Aziem, Sekena H., Heba A. M. Abd El-Kader, Sally S. Alam, Omaima M. Abd El-Moneim, and Othman E. Othman. "Nucleotide structure of prion protein gene in Egyptian camels." Journal of Applied Animal Research 47, no. 1 (January 1, 2019): 123–28. http://dx.doi.org/10.1080/09712119.2019.1580584.

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Dlouhy, S., Y. Feng, K. Young, T. Bird, C. DeCarli, M. E. Hodes, P. Piccardo, and B. Ghetti. "AN INTRON MUTATION IN THE PRION PROTEIN GENE (PRNP)." Journal of Neuropathology and Experimental Neurology 58, no. 5 (May 1999): 550. http://dx.doi.org/10.1097/00005072-199905000-00176.

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Zimmermann, Klaus, Peter L. Turecek, and Hans Peter Schwarz. "Genotyping of the prion protein gene at codon 129." Acta Neuropathologica 97, no. 4 (April 4, 1999): 355–58. http://dx.doi.org/10.1007/s004010050998.

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Won, Sae-Young, Yong-Chan Kim, Kiwon Kim, An-Dang Kim, and Byung-Hoon Jeong. "The First Report of Polymorphisms and Genetic Features of the prion-like Protein Gene (PRND) in a Prion Disease-Resistant Animal, Dog." International Journal of Molecular Sciences 20, no. 6 (March 20, 2019): 1404. http://dx.doi.org/10.3390/ijms20061404.

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Prion disease has displayed large infection host ranges among several species; however, dogs have not been reported to be infected and are considered prion disease-resistant animals. Case-controlled studies in several species, including humans and cattle, indicated a potent association of prion protein gene (PRNP) polymorphisms in the progression of prion disease. Thus, because of the proximal location and similar structure of the PRNP gene among the prion gene family, the prion-like protein gene (PRND) was noted as a novel candidate gene that contributes to prion disease susceptibility. Several case-controlled studies have confirmed the relationship of the PRND gene with prion disease vulnerability, and strong genetic linkage disequilibrium blocks were identified in prion-susceptible species between the PRNP and PRND genes. However, to date, polymorphisms of the dog PRND gene have not been reported, and the genetic linkage between the PRNP and PRND genes has not been examined thus far. Here, we first investigated dog PRND polymorphisms in 207 dog DNA samples using direct DNA sequencing. A total of four novel single nucleotide polymorphisms (SNPs), including one nonsynonymous SNP (c.149G>A, R50H), were identified in this study. We also found two major haplotypes among the four novel SNPs. In addition, we compared the genotype and allele frequencies of the c.149G>A (R50H) SNP and found significantly different distributions among eight dog breeds. Furthermore, we annotated the c.149G>A (R50H) SNP of the dog PRND gene using in silico tools, PolyPhen-2, PROVEAN, and PANTHER. Finally, we examined linkage disequilibrium between the PRNP and PRND genes in dogs. Interestingly, we did not find a strong genetic linkage between these two genes. To the best of our knowledge, this was the first genetic study of the PRND gene in a prion disease-resistant animal, a dog.

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Crowell, Jenna, Andrew Hughson, Byron Caughey, and Richard A. Bessen. "Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype." Journal of Virology 89, no. 20 (August 5, 2015): 10427–41. http://dx.doi.org/10.1128/jvi.01586-15.

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ABSTRACTPhenotypic diversity in prion diseases can be specified by prion strains in which biological traits are propagated through an epigenetic mechanism mediated by distinct PrPScconformations. We investigated the role of host-dependent factors on phenotypic diversity of chronic wasting disease (CWD) in different host species that express the same prion protein gene (Prnp). Two CWD strains that have distinct biological, biochemical, and pathological features were identified in transgenic mice that express the Syrian golden hamster (SGH)Prnp. The CKY strain of CWD had a shorter incubation period than the WST strain of CWD, but after transmission to SGH, the incubation period of CKY CWD was ∼150 days longer than WST CWD. Limited proteinase K digestion revealed strain-specific PrPScpolypeptide patterns that were maintained in both hosts, but the solubility and conformational stability of PrPScdiffered for the CWD strains in a host-dependent manner. WST CWD produced PrPScamyloid plaques in the brain of the SGH that were partially insoluble and stable at a high concentration of protein denaturant. However, in transgenic mice, PrPScfrom WST CWD did not assemble into plaques, was highly soluble, and had low conformational stability. Similar studies using the HY and DY strains of transmissible mink encephalopathy resulted in minor differences in prion biological and PrPScproperties between transgenic mice and SGH. These findings indicate that host-specific pathways that are independent ofPrnpcan alter the PrPScconformation of certain prion strains, leading to changes in the biophysical properties of PrPSc, neuropathology, and clinical prion disease.IMPORTANCEPrions are misfolded pathogenic proteins that cause neurodegeneration in humans and animals. Transmissible prion diseases exhibit a spectrum of disease phenotypes and the basis of this diversity is encoded in the structure of the pathogenic prion protein and propagated by an epigenetic mechanism. In the present study, we investigated prion diversity in two hosts species that express the same prion protein gene. While prior reports have demonstrated that prion strain properties are stable upon infection of the same host species and prion protein genotype, our findings indicate that certain prion strains can undergo dramatic changes in biological properties that are not dependent on the prion protein. Therefore, host factors independent of the prion protein can affect prion diversity. Understanding how host pathways can modify prion disease phenotypes may provide clues on how to alter prion formation and lead to treatments for prion, and other, human neurodegenerative diseases of protein misfolding.

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Hara, Hideyuki, and Suehiro Sakaguchi. "Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion." International Journal of Molecular Sciences 22, no. 22 (November 18, 2021): 12439. http://dx.doi.org/10.3390/ijms222212439.

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Conformational conversion of the cellular isoform of prion protein, PrPC, into the abnormally folded, amyloidogenic isoform, PrPSc, is an underlying pathogenic mechanism in prion diseases. The diseases manifest as sporadic, hereditary, and acquired disorders. Etiological mechanisms driving the conversion of PrPC into PrPSc are unknown in sporadic prion diseases, while prion infection and specific mutations in the PrP gene are known to cause the conversion of PrPC into PrPSc in acquired and hereditary prion diseases, respectively. We recently reported that a neurotropic strain of influenza A virus (IAV) induced the conversion of PrPC into PrPSc as well as formation of infectious prions in mouse neuroblastoma cells after infection, suggesting the causative role of the neuronal infection of IAV in sporadic prion diseases. Here, we discuss the conversion mechanism of PrPC into PrPSc in different types of prion diseases, by presenting our findings of the IAV infection-induced conversion of PrPC into PrPSc and by reviewing the so far reported transgenic animal models of hereditary prion diseases and the reverse genetic studies, which have revealed the structure-function relationship for PrPC to convert into PrPSc after prion infection.

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Kovacs, G. G. "Inherited prion disease with A117V mutation of the prion protein gene: a novel Hungarian family." Journal of Neurology, Neurosurgery & Psychiatry 70, no. 6 (June 1, 2001): 802–5. http://dx.doi.org/10.1136/jnnp.70.6.802.

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Castle, Andrew R., Serene Wohlgemuth, Luis Arce, and David Westaway. "Investigating CRISPR/Cas9 gene drive for production of disease-preventing prion gene alleles." PLOS ONE 17, no. 6 (June 7, 2022): e0269342. http://dx.doi.org/10.1371/journal.pone.0269342.

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Prion diseases are a group of fatal neurodegenerative disorders that includes chronic wasting disease, which affects cervids and is highly transmissible. Given that chronic wasting disease prevalence exceeds 30% in some endemic areas of North America, and that eventual transmission to other mammalian species, potentially including humans, cannot be ruled out, novel control strategies beyond population management via hunting and/or culling must be investigated. Prion diseases depend upon post-translational conversion of the cellular prion protein, encoded by the Prnp gene, into a disease-associated conformation; ablation of cellular prion protein expression, which is generally well-tolerated, eliminates prion disease susceptibility entirely. Inspired by demonstrations of gene drive in caged mosquito species, we aimed to test whether a CRISPR/Cas9-based gene drive mechanism could, in principle, promote the spread of a null Prnp allele among mammalian populations. First, we showed that transient co-expression of Cas9 and Prnp-directed guide RNAs in RK13 cells generates indels within the Prnp open-reading frame, indicating that repair of Cas9-induced double-strand breaks by non-homologous end-joining had taken place. Second, we integrated a ~1.2 kb donor DNA sequence into the Prnp open-reading frame in N2a cells by homology-directed repair following Cas9-induced cleavages and confirmed that integration occurred precisely in most cases. Third, we demonstrated that electroporation of Cas9/guide RNA ribonucleoprotein complexes into fertilised mouse oocytes resulted in pups with a variety of disruptions to the Prnp open reading frame, with a new coisogenic line of Prnp-null mice obtained as part of this work. However, a technical challenge in obtaining expression of Cas9 in the male germline prevented implementation of a complete gene drive mechanism in mice.

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