NR ARDL
AU Grubenbecher,S.; Hefter,H.; Korth,C.
TI Prevalence of prion protein polymorphisms in patients with Wilson's Disease
QU TSE-Forum, 4. Kongress - Nationale TSE-Forschungsplattform, Düsseldorf 28.10.-29.10.2004, Poster EPI-01
PT Konferenz-Poster
AB
Wilson Disease (WD) is an autosomal recessive disorder of copper metabolism, characterised by toxic copper accumulation mainly in liver and brain. Patients with WD lack of functional ATP7b, a copper transporting P-type ATPase. The function of the normal prion protein is still unclear and due to copper-binding characteristics of PrP it has been suggested that PrP may have a function in copper metabolism.
In order to investigate whether the prion protein influences the phenotype of WD, ie influence the dominance of liver or neurological symptoms (ie, "liver phenotype" or "brain phenotype") we sequenced the prion protein gene (Prnp) in patients with clinical WD with the goal of correlating disease symptoms with Prnp polymorphisms. Prnp polymorphisms at codon 129 have been found to be preferentially associated with disease conditions such as Alzheimer's disease and cerebral ageing.
Analysis of the Prnp gene in a selection of 42 patients admitted to an outpatient WD service of the Department of Neurology of the University of Duesseldorf revealed a distribution of codon 129 polymorphisms of MM 50%, MV 43%, VV 7%. A control from 128 German individuals was previously published to have a distribution of MM 41.4%, MV 43.8%, VV 14.8% (Schulz-Schaeffer et al., 1996 Clin. Neuropathology 15:353-357). Whether this slight bias in the allele frequency of the WD patient group reflects a selection bias for neurological symptoms or is due to differences in ethnic background is currently investigated.
AD Stephanie Grubenbecher, Carsten Korth, Institute for Neuropathology, Heinrich Heine University of Duesseldorf; Harald Hefter, Department of Neurology, Heinrich Heine University of Duesseldorf
SP englisch
PO Deutschland
OR Tagungsband