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1
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Molecular analysis of prion protein (PrP) and glial fibrillary acidic protein (GFAP) transcripts in experimental Creutzfeldt Jakob disease in mice

100%
Kordek R., Liberski P. P., Yanagihra R., Isaacson S., Gajdusek D. C.
Acta Neurobiologiae Experimentalis
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1997
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vol. 57
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issue 2
85-90
EN
Prion protein (PrPsc) which accumulates in the brains affected with subacute spongiform encephalopathies (SSE) is altered isoform of normal, cellular isoform (PrPc), and PrP deposition is accompanied with spongiosis and astrogliosis. To find the amounts of PrP and GFAP transcripts during progression of experimental Creutzfeldt Jakob disease we performed comparative RT PCR on the terminally sick mice brains, 22 weeks following inoculation with Fujisaki strain of CJD agent, and on control brains. The intensity of bands for PrP mRNA and control beta actin were similar for infected and uninfected brains, while amounts of transcripts for GFAP increased as for cytokines released by glial cells TNF-alpha and IL-1 alpha. This study supports thesis that PrPc to PrPsc conversion is post translational process not related to PrP overproduction. Increased amounts of GFAP mRNA during the course of the disease correlated with astrocytosis estimated by immunohistochemistry with anti GFAP antibody.
2

Prion octapeptide-repeat polymorphism in Polish Black-and-White cattle

80%
Walawski K., Czarnik U.
Journal of Applied Genetics
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2003
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vol. 44
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issue 2
191-195
EN
The study was carried out in a Polish Black-and-White cattle population, represented by 167 AI sires, 200 young tested bulls, 190 bull-dams, and 606 randomly chosen cows from commercial herds. The fragment of the bovine prion protein gene (PRNP) coding the octapeptide-repeat sequence, was identified by PCR analysis. Two different gene variants of 349 bp and 373 bp in size, produced three genotypes: PRNP 6/6, PRNP 6/5 and PRNP 5/5, respectively. Allele frequency in all examined populations, on average 0.894 for PRNP 6 and 0.106 for PRNP 5, shows a significant difference between the group of cows from commercial herds, characterised by high frequency of PRNP 5 (q = 0.137) in comparison to AI sires (q = 0.077), young tested bulls (q = 0.052) and bull-dams (q = 0.084). Moreover, both analysed female groups of bull-dams and cows from commercial herds are distinguished by the presence of PRNP 5/5 homozygous animals, which were not recorded in the AI sires and young tested bulls, and had never been recognised in earlier examined Holstein-Friesian populations. Analysis of the genetic equilibrium indicates a very high conformity between observed and expected number of animals in the separate PRNP genotype groups. However, some tendency of difference is observed in highly selected cows, qualified as bull-dams on the basis of very high level of milk performance traits.
3
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Codon 219 in Creutzfeldt-Jakob disease in Poland

80%
Bratosiewicz-Wasik J., Wasik T. J., Liberski P. P.
Acta Neurobiologiae Experimentalis
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2002
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vol. 62
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issue 3
149-151
EN
Prion diseases are a group of etiologically heterogenous diseases. In addition to familial cases linked to mutations of PRNP open reading frame they include also cases of unknown etiology. One of the susceptibility factors to sporadic as well as iatrogenic prion diseases are PRNP polymorphisms. In the present study, we analyzed sequences of the PRNP gene codon 219 of 16 Polish CJD cases and we found heterozygous GAG to GAT changes on the sense strand and only wild type sequence on an antisense strand. The RFLP technique was used to verify this divergence and only wild type sequences were revealed.
4

Importance of genetic factors in pathogenesis of subacute spongiform viral encephalopathies

80%
Wierzba W., Wajgt A.
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5

Abnormal segregation of prion protein octapeptide-repeat alleles in cattle

70%
Walawski K., Czarnik U., Wojciechowski R., Pareek C. S.
Journal of Applied Genetics
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2003
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vol. 44
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issue 3
375-378
EN
The study was conducted on full-families of Black-and-White cattle obtained as 25 AI sire families and 355 cows, as well as their progenies, mostly heifers at the age of 1-3 months. The sire group was composed by the casual qualification of 10 PRNP 6/6 and 15 PRNP 6/5 individuals on the basis of accessible young progenies. The randomly selected group of cows is characterised by a very high frequency of PRNP 6/6 (74.9%), followed by lower frequency of PRNP 6/5 (24.5%) and a very low frequency of PRNP 5/5 genotype (0.6%). The progenies represent all expected genotypes, such as: PRNP 6/6 (60.5%), PRNP 6/5 (35.8%) and PRNP 5/5 (3.7%), respectively. Taking into consideration the genotypes of parents and progenies, the segregation of PRNP 6 and PRNP 5 alleles was analysed. Results of the non-informative mating variant of male PRNP 6/6 ? female PRNP 6/6 (n = 87) are affected by the PRNP 6/6 progeny genotype in all cases. Subsequently, the results of mating variants male PRNP 6/6 ? female PRNP 6/5 (n = 29) and male PRNP 6/5 female PRNP 6/6 (n = 179) showed statistically non-significant differences in both above-mentioned alternations. The progeny group related from male PRNP 6/5 ? female PRNP 6/5 parental mating obtained fully informative and most valuable results based on the presented research concept. In the common group of 58 calves, the genotype PRNP 6/6 is represented by 26 individuals (44.8 %), PRNP 6/5 ? by 19 individuals (32.8 %) and PRNP 5/5 ? by 13 individuals (22.4 %). Therefore, the theoretical genotype rate (25% : 50% : 25%) is drastically deformed and the differentiation between the observed and expected numbers of animals is statistically highly significant (chi2= 12.72; 2 df.). These differences are affected by two times higher PRNP 6/6 homozygous (chi2 = 9.12; 1 df.) and responsively by the low number of PRNP 6/5 heterozygous animals (chi2 = 3.45; 1 df.). Further investigations are carried out to explain the genetic determination of abnormal PRNP octa-peptide repeat allele segregation, which suggests possible lethal cis-trans linkage effects.
6
Content available remote

Molecular biology of prions

61%
Weissmann C., Enari M., Klohn P.-C., Rossi D., Flechsig E.
Acta Neurobiologiae Experimentalis
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2002
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vol. 62
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issue 3
153-166
EN
The ?protein only? hypothesis holds that the infectious agent causing transmissible spongiform encephalopathies is a conformational isomer of PrP, a host protein predominantly expressed in brain and is strongly supported by many lines of evidence. Prion diseases are so far unique among conformational diseases in that they are transmissible, not only experimentally but also by natural routes, mainly by ingestion. The pathway of prions to the brain has been elucidated in outline. A striking feature of prions is their extraordinary resistance to conventional sterilisation procedures, and their capacity to bind to surfaces of metal and plastic without losing infectivity. This property, first observed in a clinical setting, is now being investigated in experimental settings, both in animals and in cell culture.
7

3D domain swapping ? implications for conformational disorders and ways of control

51%
Jaskolski M.
Biotechnologia
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2011
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issue 1
34-44
EN
3D Domain swapping is a mechanism of protein aggregation, in which a structural element of a protein fold is replaced by an identical element from another subunit. Some proteins, for instance RNase A, can assume many domain- swapped forms, thus undermining the dogma,'one sequence ? one structure' in a particularly spectacular way. Completed in a mutual fashion, it is a mechanism of protein oligomerization. In an open-ended fashion, 3D domain swapping could be a mechanism of amyloid fibril formation. In another mechanism, possibly operating together with domain swapping, a specific sequence, such as a glutamine expansion, could form a ?-spine of the fibril in a motif called steric zipper. The first connection between 3D domain swapping and amyloidogenicity was established in human cystatin C (HCC), the second - in the prion protein (PrP). In both cases, a disulfide bridge (natural in PrP, engineered in HCC) can be used for redox control of 3D domain swapping and to demonstrate that it is indeed involved in amyloid fibril formation. HCC has a naturally occurring L68Q mutant with drastically increased propensity for aggregation. The L68Q mutation occurs at the closed interface, or protein core. Mutations in other areas, such as the flexible hinge (especially deletions and insertions) can also be used to control 3D domain swapping and aggregation. Paradoxically, 3D domain swapping can also be used by Nature for prevention of nucleation processes that lead to high-order aggregates or crystals. Such a situation exists in the eye lens, where despite astronomical concentration of crystallins, the solution remains clear. One of the Nature's tricks to achieve polydispersity is to use a palindromic sequence for the swapped domain, thereby frustrating the growth of aggregates by constantly changing the interaction topology.
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