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(/* Amyloidosis also may classified by their extension of organ involvement as below:{{cite journal |vauthors=Bilginer Y, Akpolat T, Ozen S |title=Renal amyloidosis in children |journal=Pediatr. Nephrol. |volume=26 |issue=8 |pages=1215–27 |date=August...)
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== Historical Perspective ==
== Historical Perspective ==
*In 1639, Nicolaus Fontanus [[Autopsy|autopsied]] a young man who had [[ascites|ascitis]], [[jaundice]], [[liver abscess]] and [[splenomegaly]] and his report has been the first description of amyloidosis.<ref name="pmid218384133">{{cite journal |vauthors=Kyle RA |title=Amyloidosis: a brief history |journal=Amyloid |volume=18 Suppl 1 |issue= |pages=6–7 |date=June 2011 |pmid=21838413 |doi=10.3109/13506129.2011.574354001 |url=}}</ref>
*In 1639, Nicolaus Fontanus [[Autopsy|autopsied]] a young man who had [[ascites|ascitis]], [[jaundice]], [[liver abscess]] and [[splenomegaly]] and his report has been the first description of amyloidosis.
*In 1854, Rudolph Virchow introduced the term of [[amyloid]] as an macroscopic abnormality in some tissues.<ref name="pmid10940217">{{cite journal |vauthors=Sipe JD, Cohen AS |title=Review: history of the amyloid fibril |journal=J. Struct. Biol. |volume=130 |issue=2-3 |pages=88–98 |date=June 2000 |pmid=10940217 |doi=10.1006/jsbi.2000.4221 |url=}}</ref>
*In 1854, Rudolph Virchow introduced the term of [[amyloid]] as an macroscopic abnormality in some tissues.
*In 1867, Weber reported the first case of amyloidosis associated with [[multiple myeloma]].<ref name="pmid218384133">{{cite journal |vauthors=Kyle RA |title=Amyloidosis: a brief history |journal=Amyloid |volume=18 Suppl 1 |issue= |pages=6–7 |date=June 2011 |pmid=21838413 |doi=10.3109/13506129.2011.574354001 |url=}}</ref>
*In 1867, Weber reported the first case of amyloidosis associated with [[multiple myeloma]].<ref name="pmid218384133">{{cite journal |vauthors=Kyle RA |title=Amyloidosis: a brief history |journal=Amyloid |volume=18 Suppl 1 |issue= |pages=6–7 |date=June 2011 |pmid=21838413 |doi=10.3109/13506129.2011.574354001 |url=}}</ref>
*In 1922, Bennhold introduced [[Congo red|Congo red staining]] of [[amyloid]] that remains the [[Gold standard (test)|gold standard]] for [[diagnosis]].<ref name="pmid11677276">{{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 1922, Bennhold introduced [[Congo red|Congo red staining]] of [[amyloid]] that remains the [[Gold standard (test)|gold standard]] for [[diagnosis]].
*In 1959, Cohen and Calkins used ultra-thin sections of amyloidotic tissues and assessed by [[Electron microscope|electron microscopic]] examination, explained the presence of non-branching [[Fibril|fibrils]] with indeterminate length and variable width.<ref name="pmid10940217">{{cite journal |vauthors=Sipe JD, Cohen AS |title=Review: history of the amyloid fibril |journal=J. Struct. Biol. |volume=130 |issue=2-3 |pages=88–98 |date=June 2000 |pmid=10940217 |doi=10.1006/jsbi.2000.4221 |url=}}</ref><ref name="pmid218384133">{{cite journal |vauthors=Kyle RA |title=Amyloidosis: a brief history |journal=Amyloid |volume=18 Suppl 1 |issue= |pages=6–7 |date=June 2011 |pmid=21838413 |doi=10.3109/13506129.2011.574354001 |url=}}</ref>
*In 1959, Cohen and Calkins used ultra-thin sections of amyloidotic tissues and assessed by [[Electron microscope|electron microscopic]] examination, explained the presence of non-branching [[Fibril|fibrils]] with indeterminate length and variable width.<ref name="pmid10940217">{{cite journal |vauthors=Sipe JD, Cohen AS |title=Review: history of the amyloid fibril |journal=J. Struct. Biol. |volume=130 |issue=2-3 |pages=88–98 |date=June 2000 |pmid=10940217 |doi=10.1006/jsbi.2000.4221 |url=}}</ref><ref name="pmid218384133">{{cite journal |vauthors=Kyle RA |title=Amyloidosis: a brief history |journal=Amyloid |volume=18 Suppl 1 |issue= |pages=6–7 |date=June 2011 |pmid=21838413 |doi=10.3109/13506129.2011.574354001 |url=}}</ref>


== Classification ==
== Classification ==


=== Amyloidosis may be classified based on [[precursor]] of amyloidogenic [[protein]] into different subtypes, include:<ref name="pmid25378951">{{cite journal |vauthors=Real de Asúa D, Costa R, Galván JM, Filigheddu MT, Trujillo D, Cadiñanos J |title=Systemic AA amyloidosis: epidemiology, diagnosis, and management |journal=Clin Epidemiol |volume=6 |issue= |pages=369–77 |date=2014 |pmid=25378951 |pmc=4218891 |doi=10.2147/CLEP.S39981 |url=}}</ref><ref name="pmid24998818">{{cite journal |vauthors=Misumi Y, Ando Y |title=[Classification of amyloidosis] |language=Japanese |journal=Brain Nerve |volume=66 |issue=7 |pages=731–7 |date=July 2014 |pmid=24998818 |doi= |url=}}</ref> ===
=== Amyloidosis may be classified based on [[precursor]] of amyloidogenic [[protein]] into different subtypes, include: ===
{| class="wikitable"
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! align="center" style="background:#4479BA; color: #FFFFFF;" + |Type
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=== Amyloidosis also may classified by their extension of organ involvement as below:<ref name="pmid21360109">{{cite journal |vauthors=Bilginer Y, Akpolat T, Ozen S |title=Renal amyloidosis in children |journal=Pediatr. Nephrol. |volume=26 |issue=8 |pages=1215–27 |date=August 2011 |pmid=21360109 |pmc=3119800 |doi=10.1007/s00467-011-1797-x |url=}}</ref><ref name="pmid28134587">{{cite journal |vauthors=Khoor A, Colby TV |title=Amyloidosis of the Lung |journal=Arch. Pathol. Lab. Med. |volume=141 |issue=2 |pages=247–254 |date=February 2017 |pmid=28134587 |doi=10.5858/arpa.2016-0102-RA |url=}}</ref> ===
=== Amyloidosis also may classified by their extension of organ involvement as below: ===
{| class="wikitable"
{| class="wikitable"
! align="center" style="background:#4479BA; color: #FFFFFF;" + |Classification
! align="center" style="background:#4479BA; color: #FFFFFF;" + |Classification
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== Pathophysiology ==
== 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.<ref name="pmid23979488">{{cite journal |vauthors=Gillmore JD, Hawkins PN |title=Pathophysiology and treatment of systemic amyloidosis |journal=Nat Rev Nephrol |volume=9 |issue=10 |pages=574–86 |date=October 2013 |pmid=23979488 |doi=10.1038/nrneph.2013.171 |url=}}</ref><ref name="pmid23227278">{{cite journal |vauthors=Baker KR, Rice L |title=The amyloidoses: clinical features, diagnosis and treatment |journal=Methodist Debakey Cardiovasc J |volume=8 |issue=3 |pages=3–7 |date=2012 |pmid=23227278 |pmc=3487569 |doi= |url=}}</ref>
*[[Amyloid]] is an abnormal insoluble [[extracellular]] [[protein]] that deposits in the different tissues and causes organic dysfunction and a wide variety of clinical syndromes.
*These abnormal [[Amyloid|amyloids]] derived from misfolding and aggregation of normally soluble [[Protein|proteins]].<ref name="pmid16409147">{{cite journal |vauthors=Pepys MB |title=Amyloidosis |journal=Annu. Rev. Med. |volume=57 |issue= |pages=223–41 |date=2006 |pmid=16409147 |doi=10.1146/annurev.med.57.121304.131243 |url=}}</ref>
*These abnormal [[Amyloid|amyloids]] derived from misfolding and aggregation of normally soluble [[Protein|proteins]].
*[[Amyloid]] deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.<ref name="pmid26155101">{{cite journal |vauthors=Jerzykowska S, Cymerys M, Gil LA, Balcerzak A, Pupek-Musialik D, Komarnicki MA |title=Primary systemic amyloidosis as a real diagnostic challenge - case study |journal=Cent Eur J Immunol |volume=39 |issue=1 |pages=61–6 |date=2014 |pmid=26155101 |pmc=4439975 |doi=10.5114/ceji.2014.42126 |url=}}</ref>
*[[Amyloid]] deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.
===Systemic Amyloidosis===
===Systemic Amyloidosis===
*In systemic amyloidosis, [[amyloid]] gradually accumulate and [[amyloid]] deposition is widespread in the viscera, [[blood vessel]] walls, and in the different [[Connective tissue|connective tissues]].<ref name="pmid23227278">{{cite journal |vauthors=Baker KR, Rice L |title=The amyloidoses: clinical features, diagnosis and treatment |journal=Methodist Debakey Cardiovasc J |volume=8 |issue=3 |pages=3–7 |date=2012 |pmid=23227278 |pmc=3487569 |doi= |url=}}</ref><ref name="pmid16409147">{{cite journal |vauthors=Pepys MB |title=Amyloidosis |journal=Annu. Rev. Med. |volume=57 |issue= |pages=223–41 |date=2006 |pmid=16409147 |doi=10.1146/annurev.med.57.121304.131243 |url=}}</ref>
*In systemic amyloidosis, [[amyloid]] gradually accumulate and [[amyloid]] deposition is widespread in the viscera, [[blood vessel]] walls, and in the different [[Connective tissue|connective tissues]].<ref name="pmid23227278">{{cite journal |vauthors=Baker KR, Rice L |title=The amyloidoses: clinical features, diagnosis and treatment |journal=Methodist Debakey Cardiovasc J |volume=8 |issue=3 |pages=3–7 |date=2012 |pmid=23227278 |pmc=3487569 |doi= |url=}}</ref><ref name="pmid16409147">{{cite journal |vauthors=Pepys MB |title=Amyloidosis |journal=Annu. Rev. Med. |volume=57 |issue= |pages=223–41 |date=2006 |pmid=16409147 |doi=10.1146/annurev.med.57.121304.131243 |url=}}</ref>
====Primary Amyloidosis (AL)====
====Primary Amyloidosis (AL)====
*[[AL amyloidosis|Primary (AL) amyloidosis)]] is the most common type of amyloidosis. It results from aggregation and deposition of monoclonal [[Immunoglobulin|immunoglobulin (Ig)]] [[Light chain|light chains]] that usually produced by [[plasma cell]] clones.
*[[AL amyloidosis|Primary (AL) amyloidosis)]] is the most common type of amyloidosis. It results from aggregation and deposition of monoclonal [[Immunoglobulin|immunoglobulin (Ig)]] [[Light chain|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]] [[Fibril|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>
*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]] [[Fibril|fibrils]].
*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]].
*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:
**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
**[[Hematology|Haematological]] response to treatment
**[[Hematology|Haematological]] response to treatment
*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>
*The median [[Survival analysis|survival]] of patients with [[AL amyloidosis]] is aproximately 3.8 years.
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)====
*[[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>
*[[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>
*[[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>
*[[AA amyloidosis|Secondary or reactive amyloidosis (AA)]] is approximately 45% of all systemic amyloidosis.
*[[Pathogenesis]] of [[AA amyloidosis|secondary amyloidosis]] is multifactorial that include:
*[[Pathogenesis]] of [[AA amyloidosis|secondary amyloidosis]] is multifactorial that include:
**[[Primary structure]] of the [[precursor]] protein
**[[Primary structure]] of the [[precursor]] protein
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====Hereditary Amyloidosis====
====Hereditary Amyloidosis====
*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 (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:
**[[Transthyretin|Transthyretin (TTR)]] (most common [[inherited]] [[mutation]])
**[[Transthyretin|Transthyretin (TTR)]] (most common [[inherited]] [[mutation]])
**[[Fibrinogen]]
**[[Fibrinogen]]
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**[[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]].
*Some [[Neurodegenerative disease|neurodegenerative disorders]] such as [[Parkinson's disease]], [[Alzheimer's disease|Alzheimer]], and [[Huntington's disease]] may occur in localised amyloidosis.
*Some [[Neurodegenerative disease|neurodegenerative disorders]] such as [[Parkinson's disease]], [[Alzheimer's disease|Alzheimer]], and [[Huntington's disease]] may occur in localised amyloidosis.


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*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-rays|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
*
==Epidemiology and Demographics==
===Incidence===
*The incidence of amyloidosis is approximately 1.2 per 100,000 individuals per year worldwide.<ref name="pmid1167727622">{{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>
===Prevalence===
*The incidence/prevalence of [disease name] is approximately [number range] per 100,000 individuals worldwide.
*In [year], the incidence/prevalence of [disease name] was estimated to be [number range] cases per 100,000 individuals worldwide.
*The prevalence of [disease/malignancy] is estimated to be [number] cases annually.
===Mortality rate===
*The mortality rate of systemic amyloidosis is approximately 100 per 100,000 deaths in developed countries.<ref name="pmid164091472">{{cite journal |vauthors=Pepys MB |title=Amyloidosis |journal=Annu. Rev. Med. |volume=57 |issue= |pages=223–41 |date=2006 |pmid=16409147 |doi=10.1146/annurev.med.57.121304.131243 |url=}}</ref>
=== Age===
*In amyloidosis, the mean age of presentation is 55-60 years.<ref name="pmid214940832">{{cite journal |vauthors=Shin YM |title=Hepatic amyloidosis |journal=Korean J Hepatol |volume=17 |issue=1 |pages=80–3 |date=March 2011 |pmid=21494083 |pmc=3304630 |doi=10.3350/kjhep.2011.17.1.80 |url=}}</ref>
===Race===
*Hereditary amyloidosis subtypes include a substitution of an amino acid that is detected in approximately 4% of the black population.<ref name="pmid116772763">{{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>
*[Disease name] usually affects individuals of the [race 1] race. [Race 2] individuals are less likely to develop [disease name].
===Gender ===
*Men are more commonly affected by amyloidosis than women.<ref name="pmid21494083">{{cite journal |vauthors=Shin YM |title=Hepatic amyloidosis |journal=Korean J Hepatol |volume=17 |issue=1 |pages=80–3 |date=March 2011 |pmid=21494083 |pmc=3304630 |doi=10.3350/kjhep.2011.17.1.80 |url=}}</ref>
==Case Studies==
==Case Studies==
[[Amyloidosis case study one|Case #1]]
[[Amyloidosis case study one|Case #1]]

Revision as of 14:51, 24 October 2019

Amyloidosis Microchapters

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• Secondary amyloidosis
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• Gelsolin related amyloidosis
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• Leucocyte cell-derived chemotaxin 2 related amyloidosis
• Fibrinogen A alpha-chain associated amyloidosis

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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

In 1639, Nicolaus Fontanus autopsied a young man who had ascitis, jaundice, liver abscess and splenomegaly and his report has been the first description of amyloidosis. and in 1959, Cohen and Calkins assessed an ultra-thin sections of amyloidotic tissues by electron microscopic examination. Amyloidosis may be classified based on precursor of amyloidogenic protein into different subtypes, include AL amyloidosis (Light chains of immunoglobulines), AA amyloidosis (Serum amyloid A protein), AF amyloidosis (Mutant transthyretin, A1-apolipoprotein, gelsolin, fibrinogen, etc.), ATTRwt amyloidosis (Wild-type transthyretin), and AH amyloidosis (ß2-microglobulin). Amyloidosis also may classified by their extension of organ involvement as systemic amyloidosis (primary amyloidosis, secondary amyloidosis, hereditary amyloidosis) and Organ-specific amyloidosis (cardiac amyloidosis, hepatic amyloidosis, renal amyloidosis, etc.). Amyloid is an abnormal insoluble extracellular protein that deposits in the different tissues and causes organic dysfunction. These abnormal amyloids derived from misfolding and aggregation of normally soluble proteins. In systemic amyloidosis, amyloid gradually accumulate and amyloid deposition is widespread in the viscera, blood vessel walls, and in the different connective tissues. In organ-specific amyloidoses, amyloid deposition occurs only in the origin organ or tissue of precursor protein. In microscopy pathology of amyloidosis, amyloid is detectable as typical green birefringence under polarized light after Congo red staining, linear non-branching fibrils, distinct X-ray diffraction pattern consistent with Pauling's model of a cross-beta fibril.

Historical Perspective

Classification

Amyloidosis may be classified based on precursor of amyloidogenic protein into different subtypes, include:

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 extension of organ involvement as below:

Classification subtypes Causes Important clinical findings
Systemic amyloidosis Primary amyloidosis (AL)
Secondary amyloidosis (AA)
Hereditary amyloidosis
Organ-specific amyloidosis Renal amyloidosis
Cardiac amyloidosis
Hepatic amyloidosis
Amyloid neuropathy
Gastrointestinal amyloidosis

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.
  • These abnormal amyloids derived from misfolding and aggregation of normally soluble proteins.
  • Amyloid deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.

Systemic Amyloidosis

Primary Amyloidosis (AL)

For more information about primary amyloidosis click here.

Secondary Amyloidosis (AA)

For more information about secondary amyloidosis click here.

Hereditary Amyloidosis

Organ-specific Amyloidosis

Microscopic Pathology

In microscopy pathology of amyloidosis, amyloid is detectable as:[6][5]

  • 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

Epidemiology and Demographics

Incidence

  • The incidence of amyloidosis is approximately 1.2 per 100,000 individuals per year worldwide.[7]

Prevalence

  • The incidence/prevalence of [disease name] is approximately [number range] per 100,000 individuals worldwide.
  • In [year], the incidence/prevalence of [disease name] was estimated to be [number range] cases per 100,000 individuals worldwide.
  • The prevalence of [disease/malignancy] is estimated to be [number] cases annually.

Mortality rate

  • The mortality rate of systemic amyloidosis is approximately 100 per 100,000 deaths in developed countries.[8]

Age

  • In amyloidosis, the mean age of presentation is 55-60 years.[9]

Race

  • Hereditary amyloidosis subtypes include a substitution of an amino acid that is detected in approximately 4% of the black population.[10]
  • [Disease name] usually affects individuals of the [race 1] race. [Race 2] individuals are less likely to develop [disease name].

Gender

  • Men are more commonly affected by amyloidosis than women.[11]

Case Studies

Case #1

  1. ↑ 1.0 1.1 Kyle RA (June 2011). "Amyloidosis: a brief history". Amyloid. 18 Suppl 1: 6–7. doi:10.3109/13506129.2011.574354001. PMID 21838413.
  2. ↑ 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.
  3. ↑ Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
  4. ↑ Pepys MB (2006). "Amyloidosis". Annu. Rev. Med. 57: 223–41. doi:10.1146/annurev.med.57.121304.131243. PMID 16409147.
  5. ↑ 5.0 5.1 5.2 Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
  6. ↑ 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.
  7. ↑ Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
  8. ↑ Pepys MB (2006). "Amyloidosis". Annu. Rev. Med. 57: 223–41. doi:10.1146/annurev.med.57.121304.131243. PMID 16409147.
  9. ↑ Shin YM (March 2011). "Hepatic amyloidosis". Korean J Hepatol. 17 (1): 80–3. doi:10.3350/kjhep.2011.17.1.80. PMC 3304630. PMID 21494083.
  10. ↑ Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
  11. ↑ Shin YM (March 2011). "Hepatic amyloidosis". Korean J Hepatol. 17 (1): 80–3. doi:10.3350/kjhep.2011.17.1.80. PMC 3304630. PMID 21494083.
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