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At a glance

GSS is characterized by cerebellar ataxia, pyramidal and extra-pyramidal features, and progressive dementia, eventually leading to death. GSS is invariably fatal and there is no proven treatment or prophylaxis. It is a rare infectious syndrome related to a mutation in the prion protein. It is familial form of subacute spongiform encephalopathy resulting in widespread degeneration of the nervous system, usually beginning in the fourth or fifth decade of life. Special consideration must be given to potential contamination of the attending personnel, other patients, and medical materials.

Synonyms

Amyloid Dependent Subacute Spongiform Ence­phalopathy; Cerebellar Ataxia-Progressive Dementia Syndrome; Cerebellar Ataxia with Progressive Dementia and Amyloid Deposits in CNS; Cerebral Amyloidosis with Spongiform Encephalopathy Syndrome; Gerstmann Syndrome I; Gerstmann-Sträussler-Scheinker Disease (or Syndrome); Prion Dementia; Sträussler Disease (or Syndrome); Subacute Spongiform Encephalopathy, Gerstmann-Sträussler Type; Gerstmann-Sträussler-Scheinker (GSS) Syndrome.

Incidence

Rare; incidence estimated to be 1 to 10:100,000,000 in the general population. From 1993 to 2000, in 10 countries, the majority in Western Europe, 2,774 transmissible spongiform encephalopathy (TSE) patients were reported, including 24 with GSS.

Genetic inheritance

Autosomal dominant with point mutation of the prion protein gene (20 different mutations of the human Prion protein (PrP) gene are reported). Gene map locus is 20pter-p12.

Pathophysiology

Transmissible spongiform encephalopathy (TSE) agents, or prions, induce neurodegenerative fatal diseases in humans and in some other mammalian species. Human TSEs include GSS, Creutzfeldt-Jakob disease, Kuru, and Fatal Familial Insomnia. It is characterized by amyloid deposits called kuru plaques, the presence of spongiform changes in the brain, and possible transmissibility to experimental animals. Evidence indicates this disorder is caused by mutation in the prion protein gene (PRNP). PrPC is a normal glycoprotein that seems to have a central role in the pathogenesis of transmissible subacute spongiform encephalopathies. The isoform, which is associated with the disease, is the result of a conformational change of PrPC and designated PrPSc. Mutations in the 102nd codon of the PrP gene can produce neurodegeneration, which is the main feature of the prion diseases.

Diagnosis

Classified with other transmissible spongiform encephalopathies that represent a group of neurodegenerative diseases with lethal outcome. The differential diagnosis between Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler disease (GSD) has proved to be difficult because of the clinical similarities. However, it differs histologically from CJD by the presence of Kuru-type amyloid plaques and numerous multicentric, floccular plaques in the cerebral and cerebellar cortex, basal ganglia, and white matter. Whereas only 5 to 15% of CJD cases are familial, most cases of GSD are family-related. In addition to spinocerebellar and corticospinal tract degeneration, extensive amyloid plaques are found throughout the central nervous system (CNS), and in many cases spongiform degeneration is found. An abnormal isoform of prion protein (PrP) in the brain can be detected by Western blotting and ...

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