Amyloidosis pathophysiology: Difference between revisions
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====Primary Amyloidosis==== | ====Primary Amyloidosis==== | ||
*Primary amyloidosis (AL amyloidosis) is the most common type of amyloidosis. It results from aggregation and deposition of | *Primary amyloidosis (AL amyloidosis) is the most common type of amyloidosis. It results from aggregation and deposition of monoclonal immunoglobulin (Ig) light chains that usually produced by plasma cell clones. Change in the secondary or tertiary structure of a monoclonal light chain results in abnormal folding of the light chain that abnormally form amyloid fibrils.<ref name="pmid22909024">{{cite journal |vauthors=Desport E, Bridoux F, Sirac C, Delbes S, Bender S, Fernandez B, Quellard N, Lacombe C, Goujon JM, Lavergne D, Abraham J, Touchard G, Fermand JP, Jaccard A |title=Al amyloidosis |journal=Orphanet J Rare Dis |volume=7 |issue= |pages=54 |date=August 2012 |pmid=22909024 |pmc=3495844 |doi=10.1186/1750-1172-7-54 |url=}}</ref> | ||
==== Secondary Amyloidosis ==== | ==== Secondary Amyloidosis ==== | ||
Revision as of 20:17, 8 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
- Amyloid is an abnormal insoluble extracellular protein that deposits in the different tissues and causes organic dysfunction and a wide variety of clinical syndromes.[1][2]
- These abnormal amyloids derived from misfolding and aggregation of normally soluble proteins.[3]
- 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 arranged in an antiparallel pattern. These sheets form rigid, non-branching fibrils that are proteolysis resistant. These sheets eventually cause mechanical disruption and local oxidative stress in affected organs.
Systemic Amyloidosis
- In systemic amyloidosis, amyloid gradually accumulate and amyloid deposition is widespread in the viscera, blood vessel walls, and in the different connective tissues.[2][3]
Primary Amyloidosis
- Primary amyloidosis (AL amyloidosis) is the most common type of amyloidosis. It results from aggregation and deposition of monoclonal immunoglobulin (Ig) light chains that usually produced by plasma cell clones. Change in the secondary or tertiary structure of a monoclonal light chain results in abnormal folding of the light chain that abnormally form amyloid fibrils.[4]
Secondary Amyloidosis
- Secondary or reactive amyloidosis (AA) is approximately 45% of all systemic amyloidosis.[5]
- Pathogenesis of secondary or reactive amyloidosis is multifactorial that include:
- Primary structure of the precursor protein
- Acute phase response
- Nonfibril proteins (amyloid P component, apo E, GAGs, proteoglycans and basement membrane proteins)
- Receptors
- Lipid metabolism
- Proteases
Hereditary Amyloidosis
- Hereditary amyloidosis are due to amyloidogenic mutations and subsequently deposition of amyloids, include:[6]
Organ-specific Amyloidosis
Gross Pathology
Microscopic Pathology
In microscopy pathology of amyloidosis, amyloid is detectable as:[5]
- Typical green birefringence under polarized light after Congo red staining
- Linear non-branching fibrils (indefinite length with an approximately same diameter)
- 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.
- ↑ 2.0 2.1 Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
- ↑ 3.0 3.1 Pepys MB (2006). "Amyloidosis". Annu. Rev. Med. 57: 223–41. doi:10.1146/annurev.med.57.121304.131243. PMID 16409147.
- ↑ Desport E, Bridoux F, Sirac C, Delbes S, Bender S, Fernandez B, Quellard N, Lacombe C, Goujon JM, Lavergne D, Abraham J, Touchard G, Fermand JP, Jaccard A (August 2012). "Al amyloidosis". Orphanet J Rare Dis. 7: 54. doi:10.1186/1750-1172-7-54. PMC 3495844. PMID 22909024.
- ↑ 5.0 5.1 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.
- ↑ Mahmood S, Palladini G, Sanchorawala V, Wechalekar A (February 2014). "Update on treatment of light chain amyloidosis". Haematologica. 99 (2): 209–21. doi:10.3324/haematol.2013.087619. PMC 3912950. PMID 24497558.