Creutzfeldt-Jakob disease causes: Difference between revisions
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{{Creutzfeldt-Jakob disease}} | {{Creutzfeldt-Jakob disease}} | ||
{{CMG}} | {{CMG}} | ||
==Overview== | |||
Creutzfeldt-Jakob disease (CJD) is a rapidly progressive, invariably fatal neurodegenerative disorder believed to be caused by an abnormal isoform of a cellular glycoprotein known as the prion protein.<ref name="www.cdc.gov">{{Cite web | last = | first = | title = http://www.cdc.gov/ncidod/dvrd/cjd/qa_cjd_infection_control.htm#what | url = http://www.cdc.gov/ncidod/dvrd/cjd/qa_cjd_infection_control.htm#what | publisher = | date = | accessdate = 14 February 2014 }}</ref> | |||
==Causes== | ==Causes== | ||
* [[Transmissible spongiform encephalopathy]] diseases are caused by [[prion]]s. The diseases are thus sometimes called prion diseases. Other prion diseases include [[Gerstmann-Sträussler-Scheinker syndrome]] (GSS), [[fatal familial insomnia]] (FFI) and [[kuru (disease)|kuru]] in humans, as well as [[bovine spongiform encephalopathy]] (BSE) commonly known as mad cow disease, [[chronic wasting disease]] (CWD) in elk and deer, and [[scrapie]] in sheep. The prion that is believed to cause Creutzfeldt-Jakob exhibits at least two stable [[chemical conformation|conformations]]. One, the native state, is water-soluble and present in healthy cells. As of 2006, its biological function is unknown. The other conformational state is very poorly water-soluble and readily forms protein aggregates. | |||
[[Transmissible spongiform encephalopathy]] diseases are caused by [[prion]]s. The diseases are thus sometimes called prion diseases. Other prion diseases include [[Gerstmann-Sträussler-Scheinker syndrome]] (GSS), [[fatal familial insomnia]] (FFI) and [[kuru (disease)|kuru]] in humans, as well as [[bovine spongiform encephalopathy]] (BSE) commonly known as mad cow disease, [[chronic wasting disease]] (CWD) in elk and deer, and [[scrapie]] in sheep. The prion that is believed to cause Creutzfeldt-Jakob exhibits at least two stable [[chemical conformation|conformations]]. One, the native state, is water-soluble and present in healthy cells. As of 2006, its biological function is unknown. The other conformational state is very poorly water-soluble and readily forms protein aggregates. | |||
==References== | ==References== | ||
Revision as of 21:47, 14 February 2014
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]
Overview
Creutzfeldt-Jakob disease (CJD) is a rapidly progressive, invariably fatal neurodegenerative disorder believed to be caused by an abnormal isoform of a cellular glycoprotein known as the prion protein.[1]
Causes
- Transmissible spongiform encephalopathy diseases are caused by prions. The diseases are thus sometimes called prion diseases. Other prion diseases include Gerstmann-Sträussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI) and kuru in humans, as well as bovine spongiform encephalopathy (BSE) commonly known as mad cow disease, chronic wasting disease (CWD) in elk and deer, and scrapie in sheep. The prion that is believed to cause Creutzfeldt-Jakob exhibits at least two stable conformations. One, the native state, is water-soluble and present in healthy cells. As of 2006, its biological function is unknown. The other conformational state is very poorly water-soluble and readily forms protein aggregates.
References
- ↑ "http://www.cdc.gov/ncidod/dvrd/cjd/qa_cjd_infection_control.htm#what". Retrieved 14 February 2014. External link in
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