Amyloidosis pathophysiology: Difference between revisions
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====Secondary Amyloidosis==== | ====Secondary Amyloidosis==== | ||
* Approximately 45% of generalized amyloidosis are secondary or reactive (AA) amyloidosis. | * Approximately 45% of generalized amyloidosis are secondary or reactive (AA) amyloidosis.<ref name="pmid119640392">{{cite journal |vauthors=Röcken C, Shakespeare A |title=Pathology, diagnosis and pathogenesis of AA amyloidosis |journal=Virchows Arch. |volume=440 |issue=2 |pages=111–122 |date=February 2002 |pmid=11964039 |doi=10.1007/s00428-001-0582-9 |url=}}</ref> | ||
** | * Pathogenesis of secondary amyloidosis is multifactorial involving many variables such as: | ||
** | ** Primary structure of the precursor protein | ||
** | ** Acute phase response | ||
** | ** Presence of non-fibril proteins (amyloid P component, apolipoprotein E, glycosaminoglycans, proteoglycans and basement membrane proteins) | ||
** | ** Receptors | ||
** Lipid metabolism | |||
** Proteases | |||
=== Organ-specific Amyloidosis === | === Organ-specific Amyloidosis === | ||
Revision as of 15:54, 3 May 2018
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Shaghayegh Habibi, M.D.[2]
Overview
Pathophysiology
Systemic Amyloidosis
- Amyloid is an abnormal extracellular fibrillar protein that is insoluble and deposit in the tissues and causes disturbance of organ function and a wide variety of clinical syndromes that are classified according to the respective fibril protein precursor.[1][2]
- Approximately 27 amyloidogenic proteins that are associated with known human disease have been identified. The mutual feature of these proteins is their tendency to form β-pleated sheets that aligned in an antiparallel pattern. These sheets form rigid, nonbranching fibrils that resist proteolysis and eventually cause mechanical disruption and local oxidative stress in affected organs.
- In systemic amyloidosis, amyloid deposition is widespread and amyloid typically accumulate gradually.
Primary/Hereditary Amyloidosis
Secondary Amyloidosis
- Approximately 45% of generalized amyloidosis are secondary or reactive (AA) amyloidosis.[3]
- Pathogenesis of secondary amyloidosis is multifactorial involving many variables such as:
- Primary structure of the precursor protein
- Acute phase response
- Presence of non-fibril proteins (amyloid P component, apolipoprotein E, glycosaminoglycans, proteoglycans and basement membrane proteins)
- Receptors
- Lipid metabolism
- Proteases
Organ-specific Amyloidosis
Gross Pathology
Microscopic Pathology
In microscopy pathology of amyloidosis, amyloid is detectable as:[4]
- Typical green birefringence in polarised light after staining with Congo red
- Non-branching linear fibrils (indefinite length with an approximate diameter of 10-12 nm)
- Distinct X-ray diffraction pattern consistent with Pauling's model of a cross-beta fibril
Other Diseases Associated with the Amyloid Protein
References
- ↑ Gillmore JD, Hawkins PN (October 2013). "Pathophysiology and treatment of systemic amyloidosis". Nat Rev Nephrol. 9 (10): 574–86. doi:10.1038/nrneph.2013.171. PMID 23979488.
- ↑ Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
- ↑ Röcken C, Shakespeare A (February 2002). "Pathology, diagnosis and pathogenesis of AA amyloidosis". Virchows Arch. 440 (2): 111–122. doi:10.1007/s00428-001-0582-9. PMID 11964039.
- ↑ Röcken C, Shakespeare A (February 2002). "Pathology, diagnosis and pathogenesis of AA amyloidosis". Virchows Arch. 440 (2): 111–122. doi:10.1007/s00428-001-0582-9. PMID 11964039.