Regulating Factors of PrPres Glycosylation in Creutzfeldt-Jakob Disease
Author Information
Author(s): Levavasseur Etienne, Laffont-Proust Isabelle, Morain Émilie, Faucheux Baptiste A., Privat Nicolas, Peoc'h Katell, Sazdovitch Véronique, Brandel Jean-Philippe, Hauw Jean-Jacques, Haïk Stéphane
Primary Institution: INSERM, Avenir Team - Human Prion Diseases, Paris, France
Hypothesis
We aimed to determine whether and how PrPres glycosylation is regulated in the brain of patients with sporadic and variant Creutzfeldt-Jakob disease.
Conclusion
The study found that the regional distribution of PrPres glycoforms within one individual is heterogeneous in sporadic CJD and suggests that specific regulations may contribute to the targeting of prion strains in the brain.
Supporting Evidence
- The regional distribution of PrPres glycoforms was found to be heterogeneous in sporadic CJD patients.
- PrPres glycoforms ratio significantly correlated with the genotype at codon 129 of the prion protein gene.
- In some cases of sporadic CJD, the glycoprofile of thalamic PrPres was similar to that observed in variant CJD.
Takeaway
This study looked at how a specific protein changes in different parts of the brain in people with a disease called Creutzfeldt-Jakob disease, finding that these changes can vary a lot depending on the person.
Methodology
PrPres glycoprofiles in four brain regions from 134 patients with sporadic or variant CJD were analyzed as a function of the genotype at codon 129 of PRNP and the Western blot type of PrPres.
Limitations
The study excluded patients with familial and iatrogenic CJD, which may limit the generalizability of the findings.
Participant Demographics
123 sporadic CJD cases (55 male, 68 female) and 11 variant CJD cases (4 male, 7 female) with a mean age at death of 68 for sCJD and 36 for vCJD.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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