Amyloidosis: Difference between revisions

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 Amyloidosis is a condition caused due to deposition of abnormal [[protein|proteins]] in various [[Organ|organs]] and [[tissue|tissues]]. There are many sub classes of amyloidosis.
Amyloid fibrils are [[polymers|polymers]] of identical [[proteins|proteins]]. When functional, they are beneficial to long-term [[memory formation|memory formation]] and release of [[peptide hormones|peptide hormones]]<ref>Amyloid assembly and disassembly Edward Chuang, Acacia M. Hori, Christina D. Hesketh, James Shorter J Cell Sci 2018 131: jcs189928 doi: 10.1242/jcs.189928 Published 13 April 2018</ref>. However, issues with amyloid assembly can lead to the formation of abnormal (misfolded) proteins. This aggregation of pathogenic amyloids is amyloidosis. It happens in various [[Organ|organs]] and [[Tissue|tissues]]. There are many sub classes of amyloidosis. Some amyloid fibrils are pathogens in diseases such as [[Alzheimer's_disease|Alzheimer's disease]] and [[Parkinson's disease|Parkinson's disease]]<ref>Amyloid assembly and disassembly Edward Chuang, Acacia M. Hori, Christina D. Hesketh, James Shorter J Cell Sci 2018 131: jcs189928 doi: 10.1242/jcs.189928 Published 13 April 2018</ref>.
 
=== References  ===
 
<references />

Latest revision as of 07:41, 20 October 2018

Amyloid fibrils are polymers of identical proteins. When functional, they are beneficial to long-term memory formation and release of peptide hormones[1]. However, issues with amyloid assembly can lead to the formation of abnormal (misfolded) proteins. This aggregation of pathogenic amyloids is amyloidosis. It happens in various organs and tissues. There are many sub classes of amyloidosis. Some amyloid fibrils are pathogens in diseases such as Alzheimer's disease and Parkinson's disease[2].

References

  1. ↑ Amyloid assembly and disassembly Edward Chuang, Acacia M. Hori, Christina D. Hesketh, James Shorter J Cell Sci 2018 131: jcs189928 doi: 10.1242/jcs.189928 Published 13 April 2018
  2. ↑ Amyloid assembly and disassembly Edward Chuang, Acacia M. Hori, Christina D. Hesketh, James Shorter J Cell Sci 2018 131: jcs189928 doi: 10.1242/jcs.189928 Published 13 April 2018
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