For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
64
views
30
references
 Top references
cited by
5
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      255
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Evaluation of PRNP Expression Based on Genotypes and Alleles of Two Indel Loci in the Medulla Oblongata of Japanese Black and Japanese Brown Cattle

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Background

          Prion protein (PrP) level plays the central role in bovine spongiform encephalopathy (BSE) susceptibility. Increasing the level of PrP decreases incubation period for this disease. Therefore, studying the expression of the cellular PrP or at least the messenger RNA might be used in selection for preventing the propagation of BSE and other prion diseases. Two insertion/deletion (indel) variations have been tentatively associated with susceptibility/resistance of cattle to classical BSE.

          Methodology/Principal Findings

          We studied the expression of each genotype at the two indel sites in Japanese Black (JB) and Japanese Brown (JBr) cattle breeds by a standard curve method of real-time PCR. Five diplotypes subdivided into two categories were selected from each breed. The two cattle breeds were considered differently. Expression of PRNP was significantly ( p<0.0001) greater in the homozygous deletion genotype at the 23-bp locus in JB breed. Compared to the homozygous genotypes, the expression of PRNP was significantly greater in the heterozygous genotype at the 12-bp locus in JB ( p<0.0001) and in JBr ( p = 0.0394) breeds. In addition, there was a statistical significance in the PRNP levels between the insertion and the deletion alleles of the 23-bp locus in JB ( p = 0.0003) as well as in JBr ( p = 0.0032). There was no significance in relation to sex, age, geographical location or due to their interactions ( p>0.05).

          Conclusion

          Our results suggest that the del/del genotype or at least its del allele may modulate the expression of PRNP at the 23-bp locus in the medulla oblongata of these cattle breeds.

          Related collections

          Most cited references30

          • Record: found
          • Abstract: found
          • Article: not found

          Polar overdominance at the ovine callipyge locus.

          Suzanne S. Jackson, F Farnir, N Cockett … (1996)
          An inheritable muscular hypertrophy was recently described in sheep and shown to be determined by the callipyge gene mapped to ovine chromosome 18. Here, the callipyge phenotype was found to be characterized by a nonmendelian inheritance pattern, referred to as polar overdominance, where only heterozygous individuals having inherited the callipyge mutation from their sire express the phenotype. The possible role of parental imprinting in the determinism of polar overdominance is envisaged.
          Article 0 comments Cited 46 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: a systematic analysis of predisposing mutations and allelic variation in the PRNP gene.

            Timothy M. Palmer, T Esmonde, K Sidle … (1996)
            Creutzfeldt-Jakob disease (CJD) is a transmissible neurodegenerative disorder characterized by the accumulation of aggregates of a cellular protein, PrP, in the brain. In both human and animals, genetic alterations to the gene encoding PrP (PRNP in human) modulate susceptibility to CJD. The recent epidemic of bovine spongi-form encephalopathy in the UK has raised the possibility of transmission from animal produce to humans. To provide a baseline against which to assess possible risk factors, we have determined the frequencies of predisposing mutations and allelic variants in PRNP and their relative contributions to disease. Systematic PRNP genotype analysis was performed on suspected CJD cases referred to the National Surveillance Unit in the UK over the period 1990-1993. Inspection of 120 candidate cases revealed 67 patients with definite and probable CJD, based on clinical and neuropathological criteria. No PRNP mutations were detected in any of the remaining 53 patients assessed as "non-CJD". A disease-associated mutation in the PRNP gene was identified in nine (13.4%) definite and probable cases of CJD, a reliable estimate of the incidence of PRNP-related inherited CJD based on a prospective epidemiological series. Within the group of sporadic CJD patients (lacking PRNP mutations), we confirmed that the genotype distribution with respect to the common methionine/valine (Met/Val) polymorphism at codon 129 within PRNP was significantly different from the normal Caucasian population. The incidence of Met homozygosity at this site was more than doubled and correlated with increased susceptibility to the development of sporadic CJD. Unlike other recent studies, Val homozygosity was also confirmed to be a significant risk factor in sporadic CJD, with the relative risks for the three genotypes Met/Met: Val/Val:Met/Val being 11:4:1.
            Article 0 comments Cited 36 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Human prion diseases.

              K Hsiao, S Prusiner (1994)
              The prion diseases, sometimes referred to as the "transmissible spongiform encephalopathies," include kuru, Creutzfeldt-Jakob disease, and Gerstmann-Sträussler-Scheinker disease of humans as well as scrapie and bovine spongiform encephalopathy of animals. For many years, the prion diseases were thought to be caused by viruses despite intriguing evidence to the contrary. The unique characteristic common to all of these disorders, whether sporadic, dominantly inherited, or acquired by infection, is that they involve the aberrant metabolism of the prion protein (PrP). In many cases, the cellular prion protein is converted into the scrapie isoform by a posttranslational process that involves a conformational change. Often, the human prion diseases are transmissible to experimental animals and all of the inherited prion diseases segregate with PrP gene mutations.
              Article 0 comments Cited 36 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                : Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2011
                Publication date (Electronic): 18 May 2011
                Volume: 6
                Issue: 5
                Electronic Location Identifier: e18787
                Affiliations
                [1 ]United Graduate School of Agriculture, Kagoshima University, Kagoshima City, Japan
                [2 ]Faculty of Agriculture, Kagoshima University, Kagoshima City, Japan
                [3 ]Frontier Science Research Center, Kagoshima University, Kagoshima City, Japan
                [4 ]National Institute of Agrobiological Sciences, Tsukuba, Japan
                [5 ]Heifer Breeding Project, NARCO Kikulula-Karagwe, Kagera, Tanzania
                Public Library of Science, United Kingdom
                Author notes

                Conceived and designed the experiments: GM TS YM. Performed the experiments: GM S. Ohno. Analyzed the data: GM TS. Contributed reagents/materials/analysis tools: TS S. Okamoto KK MM YM. Wrote the paper: GM. Edited manuscript: GM TS YM S. Okamoto.

                Article
                Publisher ID: PONE-D-10-01809
                DOI: 10.1371/journal.pone.0018787
                PMC ID: 3097178
                PubMed ID: 21611160
                SO-VID: 670b9fda-f0c9-4449-8221-0d1c903fb7cd
                Copyright © Msalya et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                Date received : 15 September 2010
                Date accepted : 20 March 2011
                Page count
                Pages: 7
                Categories
                Subject: Research Article
                Subject: Agriculture
                Subject: Animal Management
                Subject: Animal Genetics
                Subject: Biology
                Subject: Genetics
                Subject: Population Genetics
                Subject: Gene Flow
                Subject: Genetic Polymorphism
                Subject: Haplotypes
                Subject: Animal Genetics
                Subject: Gene Expression
                Subject: Genetics of Disease
                Subject: Medicine
                Subject: Infectious Diseases
                Subject: Prion Diseases
                Subject: Bovine Spongiform Encephalopathy
                Subject: Veterinary Science
                Subject: Animal Management
                Subject: Animal Genetics
                Subject: Animal Types
                Subject: Large Animals
                Subject: Veterinary Diseases
                Subject: Zoonotic Diseases
                Subject: Bovine Spongiform Encephalopathy
                Subject: Prion Diseases
                Subject: Veterinary Prion Diseases

                ScienceOpen disciplines: Uncategorized
                Data availability:
                ScienceOpen disciplines: Uncategorized

                Comments

                Comment on this article

                scite_

                Similar content255

                See all similar

                Cited by5

                See all cited by

                Most referenced authors163

                See all reference authors