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.
Using data from Belgian neuropathological archives, completed with the results of a comprehensive study of available medical records, it was found 100 patients are positive with Creutzfeldt-Jakob d1551isease (CJD). In 50% of the population, the EEG revealed characteristic abnormalities. Ninety-six patients suffered from the sporadic type of CJD, while 4 suffered from a hereditary form.
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 Belgium on Creutzfeldt–Jakob disease include: Slowing of saccadic eye movements in sporadic Creutzfeldt-Jakob disease, 123I-ioflupane SPECT scan in a patient with Creutzfeldt-Jakob disease, Increased incidence of sporadic Creutzfeldt-Jakob disease in the age groups between 70 and 90 years in Belgium.