|Type of paper:||Literature review|
|Categories:||Medicine Mental disorder Dementia|
Creutzfeldt-Jakob disease (CJD) is a human prion disease. It is a condition of the neurodegenerative disorder with the standard features of the clinical and the diagnostic characteristics (Brown, 2008). The disease is primarily believed to be caused by a case of an abnormal isoform of the cellular glycoprotein referred to as the prion protein. The first of the CJD's symptoms are mainly the rapid progressive dementia, which results in the loss of the memory, changes in the personality as well as hallucinations (Brown, 2012). Other symptoms that are commonly witnessed for the diseases include depression, anxiety, paranoia, psychosis, and obsessive-compulsive symptoms. The physical challenges follow this, for instance, speech impairment, coordination dysfunction (ataxia), and balance rigid posture and changes in gait (Collinge, 2009). In most of the patients with the disease, the symptoms are followed by the movements, i.e., involuntary movements.
Concerning the CJD Pathophysiology (mechanism), the defective proteins can be transmitted through some of the defective proteins and corneal graft, electrode implants as well as human hormone (Lasmezas, 2016). The disease affects some of the parts of the human brain. In the form of familial CJDs, a mutation has occurred in the gene for PrP in that family. All the CJD types are transmissible regardless of how they occur in the person (Palmer, 2015). The prions may not be inactivated by means of the routine sterilization process of the surgical instrument
CJDs are mainly caused by prions. The prions are special kinds of proteins occurring within the neurons of the central nervous system. The protein can affect the signaling processes once misfolded, leading to the neuron damages and causing degeneration, which can result in spongiform appearance in the brain parts which are affected (Masters, 2013). For the condition's diagnosis and treatment, there has been no certain cure for the CJD, but some of the symptoms, for instance, twitching, can be managed (Johnson, 2008). The main treatment that can be used is through palliative care. Cases like depression and anxiety can be treated using the antidepressants or the sedatives.
The disease can have an impact to the human brain whereby the condition's symptoms are caused by the progressive failure of the nerve cells in the brain, which are commonly associated with the abnormal prion protein's build-up forming within the brain (Collinge, 2010). In the case of the examination of the brain tissues of the person infected with the CJD using the microscope, some of the tiny holes can be seen where the nerve cells have failed. Some of the brain's parts may resemble a sponge where the prion was infecting the brain's areas (Nitrini, 2013).
For the familial CJD, it is usually an inherited condition, and some of the common forms of this category are Gerstmann-Straussler-Scheinker disease (GSS) and fatal familial insomnia (FFI) (Mok, 2017). Finally, the iatrogenic infection of CJD is inadvertently transmitted from the sporadic cases in the course of surgical treatment (Sikorska, 2012).
The doctors normally suspect the disease's diagnosis in relation to the typical signs and symptoms as well as the disease's progression. In most of the patients suffering from the condition, the cerebrospinal fluid's protein or even a typical electroencephalogram pattern are both seen as the ways of diagnosing the CJD (Ironside, 2012). However, CJD's confirmatory diagnosis demands immunodiagnostic and neuropathology testing of the tissues of the brain obtained at either autopsy or biopsy. In the iatrogenic cases, person to person transmission of the disease has been associated with the corneal transplant during mater grafts, the peripheral injections of the pooled pituitary gland extracts and the use of the contaminated neurosurgical instruments.
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Collinge, J. (2009). Human prion diseases and bovine spongiform encephalopathy (BSE). Human molecular genetics, 6(10), 1699-1705. https://academic.oup.com/hmg/article/6/10/1699/588063
Lasmezas, C. I., Fournier, J. G., Nouvel, V., Boe, H., Marce, D., Lamoury, F., ... & Dormont, D. (2016). Adaptation of the bovine spongiform encephalopathy agent to primates and comparison with Creutzfeldt-Jakob disease: implications for human health. Proceedings of the National Academy of Sciences, 98(7), 4142-4147. https://www.pnas.org/content/98/7/4142.short
Collinge, J., Beck, J., Campbell, T., Estibeiro, K., & Will, R. G. (2010). Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease. The Lancet, 348(9019), 56. https://www.thelancet.com/journals/lancet/article/PIIS0140-6736(05)64378-4/fulltext
Ironside, J. W. (2012). Variant Creutzfeldt-Jakob disease: an update. Folia Neuropathol, 50(1), 50-56. https://pdfs.semanticscholar.org/0688/c405bf4fce87393ebca83b33e003e2c25fb3.pdf
Johnson, R. T., & Gibbs Jr, C. J. (2008). Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies. New England Journal of Medicine, 339(27), 1994-2004.
Johnson, R. T. (2016). Prion diseases. The Lancet Neurology, 4(10), 635-642.. https://www.thieme-connect.com/products/ejournals/html/10.1055/s-0039-1687841
Mok, T., Jaunmuktane, Z., Joiner, S., Campbell, T., Morgan, C., Wakerley, B., ... & Wadsworth, J. D. (2017). Variant Creutzfeldt-Jakob disease in a patient with heterozygosity at PRNP codon 129. The New England journal of medicine, 376(3), 292-294. https://discovery.ucl.ac.uk/id/eprint/1538404/1/Brandner_NEJM%20MokExtract.pdf
Masters, C. L., & Richardson, E. P. (2013). Subacute spongiform encephalopathy (Creutzfeldt-Jakob disease): the nature and progression of spongiform change. Department of Health, Education, and Welfare,[Public Health Service], National Institutes of Health.
Nitrini, R., Rosemberg, S., PassosBueno, M. R., da Silva, L. S. T., Iughetti, P., Papadopoulos, M., ... & LeBlanc, A. (2013). Familial spongiform encephalopathy associated with a novel prion protein gene mutation. Annals of Neurology: Official Journal of the American Neurological Association and the Child Neurology Society, 42(2), 138-146. https://onlinelibrary.wiley.com/doi/abs/10.1002/ana.410420203
Palmer, M. S., Dryden, A. J., Hughes, J. T., & Collinge, J. (2015). Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature, 352(6333), 340-342. https://www.nature.com/articles/352340a0
Sikorska, B., Knight, R., Ironside, J. W., & Liberski, P. P. (2012). Creutzfeldt-Jakob disease. In Neurodegenerative Diseases (pp. 76-90). Springer, New York, NY. https://link.springer.com/chapter/10.1007/978-1-4614-0653-2_6
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