ArticlePrion
Prion protein and susceptibility to kainate-induced seizures: genetic pitfalls in the use of PrP knockout mice.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- The prion protein is required for normal responses to light stimuli by photoreceptors and bipolar cells.iScience · 2024Article
- Second passage experiments of chronic wasting disease in transgenic mice overexpressing human prion protein.Veterinary research · 2022Article
- Show Me Your Friends and I Tell You Who You Are: The Many Facets of Prion Protein in Stroke.Cells · 2020Review
- Probable sporadic Creutzfeldt-Jakob disease mimicking focal epilepsy.Epilepsy & behavior case reports · 2019Article
- Prion gene paralogs are dispensable for early zebrafish development and have nonadditive roles in seizure susceptibility.The Journal of biological chemistry · 2018Article
- Inhibition of IL-1β Signaling Normalizes NMDA-Dependent Neurotransmission and Reduces Seizure Susceptibility in a Mouse Model of Creutzfeldt-Jakob Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017Review
- Advanced tests for early and accurate diagnosis of Creutzfeldt-Jakob disease.Nature reviews. Neurology · 2016Review
- Functions of the cellular prion protein, the end of Moore's law, and Ockham's razor theory.Prion · 2016Article
- Altered Monoaminergic Systems and Depressive-like Behavior in Congenic Prion Protein Knock-out Mice.The Journal of biological chemistry · 2015Article
- Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice.mBio · 2015Article
- Involvement of PrP(C) in kainate-induced excitotoxicity in several mouse strains.Scientific reports · 2015Article
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3 authors at 2 institutions in 1 country.
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Abstract
Prion protein (PrP) is a cell surface glycoprotein which is required for susceptibility to prion infection and disease. However, PrP is expressed in many different cell types located in numerous organs. Therefore, in addition to its role in prion diseases, PrP may have a large variety of other biological functions involving the nervous system and other systems. We recently showed that susceptibility to kainate-induced seizures differed in Prnp(-/-) and Prnp(+/+) mice on the C57BL/10SnJ background. However, in a genetic complementation experiment a PrP expressing transgene was not able to rescue the Prnp(+/+) phenotype. Thus the apparent effect of PrP on seizures was actually due to genes flanking the Prnp(-/-) gene rather that the Prnp deletion itself. We discuss here several pitfalls in the use of Prnp(-/-) genotypes expressed in various mouse genetic backgrounds to determine the functions of PrP. In particular, the use of Prnp(-/-) mice with heterogeneous mixed genetic backgrounds may have weakened the conclusions of many previous experiments. Use of either co-isogenic mice or congenic mice with more homogeneous genetic backgrounds is now feasible. For congenic mice, the potential problem of flanking genes can be mitigated by the use of appropriate transgene rescue experiments to confirm the conclusions.
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