Bovine spongiform encephalopathy pathophysiology: Difference between revisions
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{{Bovine spongiform encephalopathy}} | {{Bovine spongiform encephalopathy}} | ||
{{CMG}} ; {{AE}} {{Adnan Ezici}} | |||
{{ | ==Pathophysiology== | ||
===Physiology=== | |||
The normal physiologic functions of prion protein (PrPC) can be understood as follows:<ref name="pmid28428956">{{cite journal| author=Castle AR, Gill AC| title=Physiological Functions of the Cellular Prion Protein. | journal=Front Mol Biosci | year= 2017 | volume= 4 | issue= | pages= 19 | pmid=28428956 | doi=10.3389/fmolb.2017.00019 | pmc=5382174 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=28428956 }} </ref> | |||
*Protection against [[oxidative stress]] | |||
*Neuroprotection | |||
*Neuronal differentiation | |||
*Neuronal excitability | |||
*[[Myelin]] maintenance | |||
*Regulation of [[circadian rhythm]] | |||
*Iron homeostasis | |||
*Regulation of [[Cell signaling|signaling pathways]] (e.g., ERK1/2, PI3K-Akt, cAMP-PKA, etc.) | |||
== | ===Pathogenesis=== | ||
It is understood that Bovine spongiform encephalopathy (BSE) is caused by a misfolded [[prion]] [[protein]]. Misfolded prion proteins carry the disease between individuals and cause deterioration of the [[brain]]. BSE is a type of [[transmissible spongiform encephalopathy]] (TSE).<ref name = TSE>{{cite web|url=http://www.aphis.usda.gov/publications/animal_health/content/printable_version/BSEbrochure12-2006.pdf|title=An Overview of Bovine Spongiform Encephalopaphy}}</ref> TSEs can arise in animals that carry an [[allele]] which causes normal prions to contort by themselves from an alpha-helical arrangement to a beta-pleated sheet, which is the disease-causing [[chemical conformation|shape]] for the particular protein. Transmission can occur when healthy animals come in contact with tainted tissues from others with the disease. In the brain, these proteins cause native cellular prion protein to deform into the infectious state, which then goes on to deform further prion protein in an exponential cascade. This results in protein aggregates, which then form dense [[Senile plaques|plaque]] fibers, leading to the microscopic appearance of "holes" in the brain, degeneration of physical and mental abilities, and ultimately death. | |||
Different theories exist for the origin of prion proteins in cattle. Two leading theories suggest that it may have jumped species from the disease [[scrapie]] in sheep, or that it evolved from a spontaneous form of "mad-cow disease" which has been seen occasionally in cattle for many centuries.<ref>New Scientist, 17 March 2007, p 11</ref> The British Government enquiry took the view the cause was not scrapie as had originally been postulated, and was some event in the 1970s which was not possible to identify.<ref>http://www.bseinquiry.gov.uk/report/volume1/execsum4.htm</ref> | Different theories exist for the origin of prion proteins in cattle. Two leading theories suggest that it may have jumped species from the disease [[scrapie]] in sheep, or that it evolved from a spontaneous form of "mad-cow disease" which has been seen occasionally in cattle for many centuries.<ref>New Scientist, 17 March 2007, p 11</ref> The British Government enquiry took the view the cause was not scrapie as had originally been postulated, and was some event in the 1970s which was not possible to identify.<ref>http://www.bseinquiry.gov.uk/report/volume1/execsum4.htm</ref> |
Revision as of 14:01, 30 August 2021
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1] ; Associate Editor(s)-in-Chief: Adnan Ezici, M.D[2]
Pathophysiology
Physiology
The normal physiologic functions of prion protein (PrPC) can be understood as follows:[1]
- Protection against oxidative stress
- Neuroprotection
- Neuronal differentiation
- Neuronal excitability
- Myelin maintenance
- Regulation of circadian rhythm
- Iron homeostasis
- Regulation of signaling pathways (e.g., ERK1/2, PI3K-Akt, cAMP-PKA, etc.)
Pathogenesis
It is understood that Bovine spongiform encephalopathy (BSE) is caused by a misfolded prion protein. Misfolded prion proteins carry the disease between individuals and cause deterioration of the brain. BSE is a type of transmissible spongiform encephalopathy (TSE).[2] TSEs can arise in animals that carry an allele which causes normal prions to contort by themselves from an alpha-helical arrangement to a beta-pleated sheet, which is the disease-causing shape for the particular protein. Transmission can occur when healthy animals come in contact with tainted tissues from others with the disease. In the brain, these proteins cause native cellular prion protein to deform into the infectious state, which then goes on to deform further prion protein in an exponential cascade. This results in protein aggregates, which then form dense plaque fibers, leading to the microscopic appearance of "holes" in the brain, degeneration of physical and mental abilities, and ultimately death.
Different theories exist for the origin of prion proteins in cattle. Two leading theories suggest that it may have jumped species from the disease scrapie in sheep, or that it evolved from a spontaneous form of "mad-cow disease" which has been seen occasionally in cattle for many centuries.[3] The British Government enquiry took the view the cause was not scrapie as had originally been postulated, and was some event in the 1970s which was not possible to identify.[4]
Microscopic Pathology
References
- ↑ Castle AR, Gill AC (2017). "Physiological Functions of the Cellular Prion Protein". Front Mol Biosci. 4: 19. doi:10.3389/fmolb.2017.00019. PMC 5382174. PMID 28428956.
- ↑ "An Overview of Bovine Spongiform Encephalopaphy" (PDF).
- ↑ New Scientist, 17 March 2007, p 11
- ↑ http://www.bseinquiry.gov.uk/report/volume1/execsum4.htm