Amyloidosis: Difference between revisions
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*This type of amyloidosis most frequently involve the [[kidney]] (usually [[proteinuria]] with the [[nephrotic syndrome]]) and the [[heart]].<ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | *This type of amyloidosis most frequently involve the [[kidney]] (usually [[proteinuria]] with the [[nephrotic syndrome]]) and the [[heart]].<ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | ||
*In [[AL amyloidosis|primary (AL) amyloidosis]] survival rate depends on:<ref name="pmid229090242">{{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> | *In [[AL amyloidosis|primary (AL) amyloidosis]] survival rate depends on:<ref name="pmid229090242">{{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> | ||
**Type of organ involvement (amyloid heart disease is the main prognostic factor) | **Type of organ involvement ([[amyloid]] heart disease is the main prognostic factor) | ||
**The severity of different organs involvement | **The severity of different organs involvement | ||
**Haematological response to treatment | **[[Hematology|Haematological]] response to treatment | ||
*The median survival of patients with AL amyloidosis is aproximately 3.8 years.<ref name="pmid21483018">{{cite journal |vauthors=Merlini G, Seldin DC, Gertz MA |title=Amyloidosis: pathogenesis and new therapeutic options |journal=J. Clin. Oncol. |volume=29 |issue=14 |pages=1924–33 |date=May 2011 |pmid=21483018 |pmc=3138545 |doi=10.1200/JCO.2010.32.2271 |url=}}</ref> | *The median [[Survival analysis|survival]] of patients with [[AL amyloidosis]] is aproximately 3.8 years.<ref name="pmid21483018">{{cite journal |vauthors=Merlini G, Seldin DC, Gertz MA |title=Amyloidosis: pathogenesis and new therapeutic options |journal=J. Clin. Oncol. |volume=29 |issue=14 |pages=1924–33 |date=May 2011 |pmid=21483018 |pmc=3138545 |doi=10.1200/JCO.2010.32.2271 |url=}}</ref> | ||
For more information about primary amyloidosis click [[AL amyloidosis|'''here''']]. | For more information about primary amyloidosis click [[AL amyloidosis|'''here''']]. | ||
====Secondary Amyloidosis (AA)==== | ====Secondary Amyloidosis (AA)==== | ||
*Secondary amyloidosis is associated with chronic [[inflammation]] (such as tuberculosis or rheumatoid arthritis).<ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | *[[AA amyloidosis|Secondary amyloidosis]] is associated with chronic [[inflammation]] (such as [[tuberculosis]] or [[rheumatoid arthritis]]).<ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | ||
*Secondary or reactive amyloidosis (AA) is approximately 45% of all systemic 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> | *[[AA amyloidosis|Secondary or reactive amyloidosis (AA)]] is approximately 45% of all systemic 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 | *[[Pathogenesis]] of [[AA amyloidosis|secondary amyloidosis]] is multifactorial that include: | ||
**Primary structure of the precursor protein | **[[Primary structure]] of the [[precursor]] protein | ||
**Acute phase response | **Acute phase response | ||
**Nonfibril [[Protein|proteins]] (amyloid P component, [[Apolipoprotein E|apo E]], [[Glycosaminoglycan|GAGs]], [[Proteoglycan|proteoglycans]] and [[basement membrane]] [[Protein|proteins]]) | **Nonfibril [[Protein|proteins]] ([[amyloid]] P component, [[Apolipoprotein E|apo E]], [[Glycosaminoglycan|GAGs]], [[Proteoglycan|proteoglycans]] and [[basement membrane]] [[Protein|proteins]]) | ||
**[[Receptor (biochemistry)|Receptors]] | **[[Receptor (biochemistry)|Receptors]] | ||
**[[Lipid metabolism]] | **[[Lipid metabolism]] | ||
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====Hereditary Amyloidosis==== | ====Hereditary Amyloidosis==== | ||
*Hereditary (or familial) amyloidosis are autosomal dominant diseases that inherited variant proteins cause the production and deposition of amyloid fibrils.<ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | *Hereditary (or familial) amyloidosis are [[Autosome|autosomal]] [[Dominance relationship|dominant]] diseases that [[inherited]] variant [[Protein|proteins]] cause the production and deposition of [[amyloid]] fibrils.<ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | ||
*Hereditary amyloidosis are due to amyloidogenic [[Mutation|mutations]] and subsequently deposition of [[Amyloid|amyloids]], include:<ref name="pmid24497558">{{cite journal |vauthors=Mahmood S, Palladini G, Sanchorawala V, Wechalekar A |title=Update on treatment of light chain amyloidosis |journal=Haematologica |volume=99 |issue=2 |pages=209–21 |date=February 2014 |pmid=24497558 |pmc=3912950 |doi=10.3324/haematol.2013.087619 |url=}}</ref> | *Hereditary amyloidosis are due to amyloidogenic [[Mutation|mutations]] and subsequently deposition of [[Amyloid|amyloids]], include:<ref name="pmid24497558">{{cite journal |vauthors=Mahmood S, Palladini G, Sanchorawala V, Wechalekar A |title=Update on treatment of light chain amyloidosis |journal=Haematologica |volume=99 |issue=2 |pages=209–21 |date=February 2014 |pmid=24497558 |pmc=3912950 |doi=10.3324/haematol.2013.087619 |url=}}</ref> | ||
**[[Transthyretin|Transthyretin (TTR)]] (most common inherited mutation) | **[[Transthyretin|Transthyretin (TTR)]] (most common [[inherited]] [[mutation]]) | ||
**[[Fibrinogen]] | **[[Fibrinogen]] | ||
**[[Apolipoprotein A1]] | **[[Apolipoprotein A1]] | ||
**[[Apolipoprotein A2]] | **[[Apolipoprotein A2]] | ||
**[[Lysozyme]] | **[[Lysozyme]] | ||
**Gelsolin [[Gene|genes]] | **[[Gelsolin]] [[Gene|genes]] | ||
===Organ-specific Amyloidosis=== | ===Organ-specific Amyloidosis=== | ||
*In this type of amyloidoses, amyloid deposition occurs only in the origin organ or tissue of precursor protein.<ref name="pmid23451869">{{cite journal |vauthors=Blancas-Mejía LM, Ramirez-Alvarado M |title=Systemic amyloidoses |journal=Annu. Rev. Biochem. |volume=82 |issue= |pages=745–74 |date=2013 |pmid=23451869 |pmc=4044913 |doi=10.1146/annurev-biochem-072611-130030 |url=}}</ref> | *In this type of amyloidoses, [[amyloid]] deposition occurs only in the origin organ or tissue of [[precursor]] [[protein]].<ref name="pmid23451869">{{cite journal |vauthors=Blancas-Mejía LM, Ramirez-Alvarado M |title=Systemic amyloidoses |journal=Annu. Rev. Biochem. |volume=82 |issue= |pages=745–74 |date=2013 |pmid=23451869 |pmc=4044913 |doi=10.1146/annurev-biochem-072611-130030 |url=}}</ref> | ||
*Some neurodegenerative disorders such as Parkinson disease, Alzheimer, and Huntington disease may occur in | *Some [[Neurodegenerative disease|neurodegenerative disorders]] such as [[Parkinson's disease]], [[Alzheimer's disease|Alzheimer]], and [[Huntington's disease]] may occur in localised amyloidosis. | ||
* | *Localised amyloidoses can accure due to deposition of [[intracellular]] and/or [[extracellular]] [[amyloid]]. | ||
**Huntington's disease: intracellular protein deposition | **[[Huntington's disease]]: [[intracellular]] [[protein]] deposition | ||
**Parkinson's disease: intracellular protein deposition | **[[Parkinson's disease]]: [[intracellular]] [[protein]] deposition | ||
**Alzheimer's disease: intracellular (Tau protein fibrils) and extracellular (amyloid β fibrils) deposition | **[[Alzheimer's disease]]: [[intracellular]] ([[Tau protein]] [[Fibril|fibrils]]) and [[extracellular]] ([[amyloid]] β fibrils) deposition | ||
===Microscopic Pathology=== | ===Microscopic Pathology=== | ||
In microscopy pathology of amyloidosis, [[amyloid]] is detectable as:<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><ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | In microscopy pathology of amyloidosis, [[amyloid]] is detectable as:<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><ref name="pmid116772762">{{cite journal |vauthors=Khan MF, Falk RH |title=Amyloidosis |journal=Postgrad Med J |volume=77 |issue=913 |pages=686–93 |date=November 2001 |pmid=11677276 |pmc=1742163 |doi= |url=}}</ref> | ||
*Typical green [[birefringence]] under [[Polarization|polarized]] light after [[Congo red]] staining (appears in red under normal light) | *Typical green [[birefringence]] under [[Polarization|polarized]] light after [[Congo red]] staining (appears in red under normal light) | ||
*Linear non-branching [[Fibril|fibrils]] (indefinite length with an approximately same diameter) | *Linear non-branching [[Fibril|fibrils]] (indefinite length with an approximately same diameter) | ||
*Distinct X-ray diffraction pattern consistent with Pauling's model of a cross-beta fibril | *Distinct [[X-rays|X-ray]] diffraction pattern consistent with Pauling's model of a cross-beta fibril | ||
==Case Studies== | ==Case Studies== | ||
[[Amyloidosis case study one|Case #1]] | [[Amyloidosis case study one|Case #1]] | ||
Revision as of 18:10, 13 June 2018
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Amyloidosis Microchapters |
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Diagnosis |
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Treatment |
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Case Studies |
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Amyloidosis On the Web |
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American Roentgen Ray Society Images of Amyloidosis |
For patient information, click here
Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Shaghayegh Habibi, M.D.[2]
Overview
Historical Perspective
- In 1639, Nicolaus Fontanus autopsied a young man who had ascites, jaundice, liver abscess and splenomegaly and his report has been the first description of amyloidosis.[1]
- In 1854, Rudolph Virchow introduced the term of amyloid as an macroscopic abnormality in some tissues.[2]
- In 1867, Weber reported the first case of amyloidosis associated with multiple myeloma.[1]
- In 1922, Bennhold introduced Congo red staining of amyloid that remains the gold standard for diagnosis.[3]
- In 1959, Cohen and Calkins used ultrathin sections of amyloidotic tissues and assessed by electron microscopic examination, explained the presence of nonbranching fibrils with indeterminate length and variable width.[2][1]
Classification
Amyloidosis may be classified based on precursor of amyloidogenic protein into different subtypes, include:[4][5]
| Type | Amyloidogenic protein/ fibril | Clinical syndrome |
|---|---|---|
| AL (primary amyloidosis) | Light chains of immunoglobulines (most common type) | Monoclonal gammopathy |
| AA (secondary amyloidosis) | Serum amyloid A protein | Chronic inflammatory diseases |
| AF | Mutant transthyretin, A1-apolipoprotein, gelsolin, fibrinogen, etc. | Familial polyneuropathy/cardiomyopathy/nephropathy |
| ATTRwt | Wild-type transthyretin | Senile restrictive cardiomyopathy _ Transthyretin-related amyloidosis wild-type |
| AH | ß2-microglobulin | Long-term hemodialysis |
Amyloidosis also may classified by their organ involvement as below:[6][7]
| Classification | subtypes | Causes | Important clinical findings |
|---|---|---|---|
| Systemic amyloidosis | Primary amyloidosis (AL) |
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| Secondary amyloidosis (AA) |
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| Hereditary amyloidosis | |||
| Organ-specific amyloidosis | Renal amyloidosis |
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| Cardiac amyloidosis | |||
| Hepatic amyloidosis |
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| Amyloid neuropathy | |||
| Gastrointestinal amyloidosis |
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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.[8][9]
- These abnormal amyloids derived from misfolding and aggregation of normally soluble proteins.[10]
- Amyloid deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.[11]
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.[9][10]
Primary Amyloidosis (AL)
- Primary (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 structure or tertiary structure of a monoclonal light chain results in abnormal folding of the light chain that abnormally form amyloid fibrils.[12]
- This type of amyloidosis most frequently involve the kidney (usually proteinuria with the nephrotic syndrome) and the heart.[13]
- In primary (AL) amyloidosis survival rate depends on:[14]
- Type of organ involvement (amyloid heart disease is the main prognostic factor)
- The severity of different organs involvement
- Haematological response to treatment
- The median survival of patients with AL amyloidosis is aproximately 3.8 years.[15]
For more information about primary amyloidosis click here.
Secondary Amyloidosis (AA)
- Secondary amyloidosis is associated with chronic inflammation (such as tuberculosis or rheumatoid arthritis).[13]
- Secondary or reactive amyloidosis (AA) is approximately 45% of all systemic amyloidosis.[16]
- Pathogenesis of secondary 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
For more information about secondary amyloidosis click here.
Hereditary Amyloidosis
- Hereditary (or familial) amyloidosis are autosomal dominant diseases that inherited variant proteins cause the production and deposition of amyloid fibrils.[13]
- Hereditary amyloidosis are due to amyloidogenic mutations and subsequently deposition of amyloids, include:[17]
Organ-specific Amyloidosis
- In this type of amyloidoses, amyloid deposition occurs only in the origin organ or tissue of precursor protein.[18]
- Some neurodegenerative disorders such as Parkinson's disease, Alzheimer, and Huntington's disease may occur in localised amyloidosis.
- Localised amyloidoses can accure due to deposition of intracellular and/or extracellular amyloid.
- Huntington's disease: intracellular protein deposition
- Parkinson's disease: intracellular protein deposition
- Alzheimer's disease: intracellular (Tau protein fibrils) and extracellular (amyloid β fibrils) deposition
Microscopic Pathology
In microscopy pathology of amyloidosis, amyloid is detectable as:[16][13]
- Typical green birefringence under polarized light after Congo red staining (appears in red under normal light)
- 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
Case Studies
- ↑ 1.0 1.1 1.2 Kyle RA (June 2011). "Amyloidosis: a brief history". Amyloid. 18 Suppl 1: 6–7. doi:10.3109/13506129.2011.574354001. PMID 21838413.
- ↑ 2.0 2.1 Sipe JD, Cohen AS (June 2000). "Review: history of the amyloid fibril". J. Struct. Biol. 130 (2–3): 88–98. doi:10.1006/jsbi.2000.4221. PMID 10940217.
- ↑ Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
- ↑ Real de Asúa D, Costa R, Galván JM, Filigheddu MT, Trujillo D, Cadiñanos J (2014). "Systemic AA amyloidosis: epidemiology, diagnosis, and management". Clin Epidemiol. 6: 369–77. doi:10.2147/CLEP.S39981. PMC 4218891. PMID 25378951.
- ↑ Misumi Y, Ando Y (July 2014). "[Classification of amyloidosis]". Brain Nerve (in Japanese). 66 (7): 731–7. PMID 24998818.
- ↑ Bilginer Y, Akpolat T, Ozen S (August 2011). "Renal amyloidosis in children". Pediatr. Nephrol. 26 (8): 1215–27. doi:10.1007/s00467-011-1797-x. PMC 3119800. PMID 21360109.
- ↑ Khoor A, Colby TV (February 2017). "Amyloidosis of the Lung". Arch. Pathol. Lab. Med. 141 (2): 247–254. doi:10.5858/arpa.2016-0102-RA. PMID 28134587.
- ↑ 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.
- ↑ 9.0 9.1 Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
- ↑ 10.0 10.1 Pepys MB (2006). "Amyloidosis". Annu. Rev. Med. 57: 223–41. doi:10.1146/annurev.med.57.121304.131243. PMID 16409147.
- ↑ Jerzykowska S, Cymerys M, Gil LA, Balcerzak A, Pupek-Musialik D, Komarnicki MA (2014). "Primary systemic amyloidosis as a real diagnostic challenge - case study". Cent Eur J Immunol. 39 (1): 61–6. doi:10.5114/ceji.2014.42126. PMC 4439975. PMID 26155101.
- ↑ 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.
- ↑ 13.0 13.1 13.2 13.3 Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
- ↑ 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.
- ↑ Merlini G, Seldin DC, Gertz MA (May 2011). "Amyloidosis: pathogenesis and new therapeutic options". J. Clin. Oncol. 29 (14): 1924–33. doi:10.1200/JCO.2010.32.2271. PMC 3138545. PMID 21483018.
- ↑ 16.0 16.1 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.
- ↑ Blancas-Mejía LM, Ramirez-Alvarado M (2013). "Systemic amyloidoses". Annu. Rev. Biochem. 82: 745–74. doi:10.1146/annurev-biochem-072611-130030. PMC 4044913. PMID 23451869.