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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.
Creutzfeldt-Jakob disease (CJD) is increasingly being reported over the last three decades from most countries as a result of heightened awareness of the disease. Various studies have been reported with annual incidence of 0.5-1.5 cases of CJD per million of general population.
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 Singapore on Creutzfeldt–Jakob disease include: Creutzfeldt-Jakob disease presenting with visual blurring, diplopia and visual loss: Heidenhain's variant, Combined diffusion-weighted and spectroscopic MR imaging in Creutzfeldt-Jakob disease, Bovine spongiform encephalopathy and Creutzfeldt-Jakob disease.