Fatal familial insomnia (FFI) and familial Creutzfeldt-Jakob disease (fCJD) are familial prion diseases with autosomal dominant inheritance of the D178N mutation. FFI has been reported in at least 27 pedigrees around the world. Twelve apparently unrelated FFI and fCJD pedigrees with the characteristic D178N mutation have been reported in the Prion Diseases Registry of the Basque Country since 1993. The high incidence of familial prion diseases in this region may reflect a unique ancestral origin of the chromosome carrying this mutation. In order to investigate this putative founder effect, we developed "happy typing", a new approach to the happy mapping method, which consists of the physical isolation of large haploid genomic DNA fragments and their analysis by the Polymerase Chain Reaction in order to perform haplotypic analysis instead of pedigree analysis. Six novel microsatellite markers, located in a 150-kb genomic segment flanking the PRNP gene were characterized for typing haploid DNA fragments of 285 kb in size. A common haplotype was found in patients from the Basque region, strongly suggesting a founder effect. We propose that "happy typing" constitutes an efficient method for determining disease-associated haplotypes, since the analysis of a single affected individual per pedigree should provide sufficient evidence.
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http://dx.doi.org/10.1007/s00439-005-1277-0 | DOI Listing |
Sleep Med
December 2024
Department of Neurology, Henan Provincial People's Hospital, Zhengzhou University People's Hospital, Zhengzhou, Henan Province, China. Electronic address:
Fatal familial insomnia (FFI) is a rare autosomal dominant neurodegenerative disorder characterized by rapidly progressive dementia, severe sleep disturbances, and autonomic dysfunction. The clinical manifestations of FFI can exhibit substantial variations, making it crucial to rule out other conditions, such as autoimmune encephalitis and Creutzfeldt-Jakob disease, during early diagnosis. In this study, we describe the case of a 58-year-old man who experienced persistent insomnia, autonomic symptoms, gait instability, and rapidly progressive dementia.
View Article and Find Full Text PDFFront Cell Dev Biol
July 2024
Department of Genetics and Genomics, College of Medicine and Health Sciences, United Arab Emirates University, Abu Dhabi, United Arab Emirates.
Background: Familial hypercholesterolemia (FH) is an autosomal dominant disorder characterized by increased LDL-cholesterol levels. About 85% of FH cases are caused by mutations encoding the low-density lipoprotein receptor (LDLR). LDLR is synthesized in the endoplasmic reticulum (ER) where it undergoes post-translational modifications and then transported through Golgi apparatus to the plasma membrane.
View Article and Find Full Text PDFMost cases of human prion disease arise due to spontaneous misfolding of WT or mutant prion protein, yet recapitulating this event in animal models has proven challenging. It remains unclear whether spontaneous prion generation can occur within the mouse lifespan in the absence of protein overexpression and how disease-causing mutations affect prion strain properties. To address these issues, we generated knockin mice that express the misfolding-prone bank vole prion protein (BVPrP).
View Article and Find Full Text PDFActa Neuropathol
July 2024
Division of Neuropathology, Department of Pathology, Brigham and Women's Hospital, Boston, MA, USA.
Creutzfeldt-Jakob Disease (CJD), the most common human prion disease, is associated with pathologic misfolding of the prion protein (PrP), encoded by the PRNP gene. Of human prion disease cases, < 1% were transmitted by misfolded PrP, ~ 15% are inherited, and ~ 85% are sporadic (sCJD). While familial cases are inherited through germline mutations in PRNP, the cause of sCJD is unknown.
View Article and Find Full Text PDFbioRxiv
June 2024
Division of Neuropathology, Department of Pathology, Brigham and Women's Hospital, Boston, MA, USA.
Creutzfeldt-Jakob Disease (CJD), the most common human prion disease, is associated with pathologic misfolding of the prion protein (PrP), encoded by the gene. Of human prion disease cases, ~1% were transmitted by misfolded PrP, ~15% are inherited, and ~85% are sporadic (sCJD). While familial cases are inherited through germline mutations in , the cause of sCJD is unknown.
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