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[Prion protein: structure, functions and polymorphisms associated with human spongiform encephalopathies]
J L Laplanche1, P Beaudry, L Ripoll
1Formation de Recherche Associée Claude Bernard, Neurochimie des Communications Cellulaires, Hôpital Saint-Louis, Paris, France.
Pathologie-Biologie
|February 1, 1995
Summary
Transmissible spongiform encephalopathies (TSEs), or prion diseases, involve abnormal prion protein (PrP) accumulation in the brain. Genetic factors, including PRNP gene mutations and polymorphisms, significantly influence the development of these rare neurodegenerative disorders.
Area of Science:
- Neurodegenerative Diseases
- Biochemistry
- Molecular Genetics
Context:
- Transmissible subacute spongiform encephalopathies (TSSEs), or prion diseases, are rare neurodegenerative disorders affecting humans and animals.
- A key feature is the accumulation of abnormal prion protein (PrP) in the brain.
Purpose:
- To explore the role of the host prion protein (PrP) gene in the susceptibility and development of TSSEs.
- To understand the genetic factors influencing different forms of prion diseases.
Summary:
- Prion diseases are characterized by abnormal prion protein (PrP) accumulation, potentially due to conformational changes.
- Mutations in the human PRNP gene are found in 16% of patients and may be causative.
- A common polymorphism (129 Met/Val) in PRNP acts as a predisposing factor in individuals without mutations.
Impact:
- Advances in understanding the molecular genetics of TSSEs in humans and animals.
- Highlights the critical role of the primary structure of host PrP in disease development.
- Provides insights into genetic susceptibility for experimental, iatrogenic, and spontaneous prion diseases.