Creutzfeldt–Jakob or CJD is a degenerative neurological disease that is incurable and invariably fatal. CJD is at times called a human form of mad cow disease. CJD is caused by an agent called a prion. Prions are misfolded proteins that replicate by converting their properly folded counterparts, in their host, to the same misfolded structure they possess. CJD causes the brain tissue to degenerate rapidly, and as the disease destroys the brain, the brain develops holes and the texture changes to resemble that of a kitchen sponge. The first symptom of CJD is rapidly progressive dementia, leading to memory loss, personality changes, and hallucinations. Other frequently occurring features include anxiety, depression, paranoia, obsessive-compulsive symptoms, and psychosis.
The incidence of Creutzfeldt-Jakob disease in Switzerland increased two-fold in 2001, and figures from the first quarter of 2002 indicate that it continues to rise. Neither age at onset nor duration of disease were different from previous years. Genetic analysis of the 27 reported cases revealed only one disease-associated mutation in the prion gene.
No generally accepted treatment for CJD exists; the disease is invariably fatal and research continues. Amphotericin B and Doxorubicin have been investigated as potentially effective against CJD, but as yet there is no strong evidence that either drug is effective in stopping the disease. Further study has been taken with other medical drugs, but none are effective. However, drugs to reduce suffering do exist, and include valproate, an anticonvulsant agent, clonazepam and benzodiazepine, to reduce muscle jerks.
The ongoing researches in Switzerland on Creutzfeldt–Jakob disease include: The relevance of updated diagnostic criteria for sporadic Creutzfeldt-Jakob disease, Creutzfeldt-Jakob disease revealed by a logopenic variant of primary progressive aphasia, Stability and Reproducibility Underscore Utility of RT-QuIC for Diagnosis of Creutzfeldt-Jakob Disease.