Creutzfeldt-Jakob disease causes: Difference between revisions

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{{‪Creutzfeldt-Jakob disease‬}}
{{‪Creutzfeldt-Jakob disease‬}}
{{CMG}}
{{CMG}} {{AE}}, {{MMJ}}
==Overview==
Creutzfeldt-Jakob disease is caused by the presence of a [[prion]] [[protein]], an abnormal isoform of a [[cellular]] [[glycoprotein]]. [[Prion]]s are transmissible particles that are devoid of [[nucleic acid]] and seem to be composed exclusively of a modified protein (PrPSc). The normal, [[cellular]] PrP ([[PrPC]]) is converted into [[PrPSc]] through a posttranslational process during which it acquires a high beta-sheet content.


==Causes==
==Causes==
 
*Creutzfeldt-Jakob disease is caused by the presence of a [[prion]] [[protein]], an abnormal isoform of a [[cellular]] [[glycoprotein]].<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>
[[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.
*[[Prion]]s are transmissible particles that are devoid of [[nucleic acid]] and seem to be composed exclusively of a modified protein ([[PrPSc]]). The normal, cellular PrP ([[PrPC]]) is converted into [[PrPSc]] through a posttranslational process during which it acquires a high beta-sheet content.<ref name="pmid9811807">{{cite journal| author=Prusiner SB| title=Prions. | journal=Proc Natl Acad Sci U S A | year= 1998 | volume= 95 | issue= 23 | pages= 13363-83 | pmid=9811807 | doi= | pmc=33918 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=9811807  }} </ref>
 
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.
 
People can also acquire CJD genetically through a mutation of a gene (needs to be defined). This only occurs in 5-10% of all CJD cases.


==References==
==References==
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Latest revision as of 19:46, 7 July 2020

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1] Associate Editor(s)-in-Chief: , Mohamadmostafa Jahansouz M.D.[2]

Overview

Creutzfeldt-Jakob disease is caused by the presence of a prion protein, an abnormal isoform of a cellular glycoprotein. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrPSc). The normal, cellular PrP (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high beta-sheet content.

Causes

  • Creutzfeldt-Jakob disease is caused by the presence of a prion protein, an abnormal isoform of a cellular glycoprotein.[1]
  • Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrPSc). The normal, cellular PrP (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high beta-sheet content.[2]

References

  1. "http://www.cdc.gov/ncidod/dvrd/cjd/qa_cjd_infection_control.htm#what". Retrieved 14 February 2014. External link in |title= (help)
  2. Prusiner SB (1998). "Prions". Proc Natl Acad Sci U S A. 95 (23): 13363–83. PMC 33918. PMID 9811807.

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