Apolipoprotein AI amyloidosis: Difference between revisions

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==Classification==
==Classification==
Apolipoprotein AI amyloidosis is one of the subtypes of familial amyloidosis. Familiar amyloidosis may be classified according to the type of mutant protein into 6 subtypes:<ref name="Benson2003">{{cite journal|last1=Benson|first1=Merrill D|title=The hereditary amyloidoses|journal=Best Practice & Research Clinical Rheumatology|volume=17|issue=6|year=2003|pages=909–927|issn=15216942|doi=10.1016/j.berh.2003.09.001}}</ref><ref name="Benson20032">{{cite journal|last1=Benson|first1=Merrill D|title=The hereditary amyloidoses|journal=Best Practice & Research Clinical Rheumatology|volume=17|issue=6|year=2003|pages=909–927|issn=15216942|doi=10.1016/j.berh.2003.09.001}}</ref><ref>{{cite book | last = Scriver | first = Charles | title = The metabolic & molecular bases of inherited disease | publisher = McGraw-Hill | location = New York | year = 2001 | isbn = 978-0079130358 }}</ref>
Apolipoprotein AI amyloidosis is one of the subtypes of familial amyloidosis. Familiar amyloidosis may be classified according to the type of mutant protein into 7 subtypes:<ref name="Benson2003">{{cite journal|last1=Benson|first1=Merrill D|title=The hereditary amyloidoses|journal=Best Practice & Research Clinical Rheumatology|volume=17|issue=6|year=2003|pages=909–927|issn=15216942|doi=10.1016/j.berh.2003.09.001}}</ref><ref name="Benson20032">{{cite journal|last1=Benson|first1=Merrill D|title=The hereditary amyloidoses|journal=Best Practice & Research Clinical Rheumatology|volume=17|issue=6|year=2003|pages=909–927|issn=15216942|doi=10.1016/j.berh.2003.09.001}}</ref><ref>{{cite book | last = Scriver | first = Charles | title = The metabolic & molecular bases of inherited disease | publisher = McGraw-Hill | location = New York | year = 2001 | isbn = 978-0079130358 }}</ref>
* [[Transthyretin|Transthyretin (TTR)]]
* [[Transthyretin|Transthyretin (TTR)]]
* [[Apolipoprotein AI]]
* [[Apolipoprotein AI]]
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{{familytree/start}}
{{familytree/start}}
{{familytree | | | | | | | | | | | | | | A01 | | | | | | | | | | | | A01=genes involved in familial amyloidosis}}
{{familytree | | | | | | | | | | | | | | A01 | | | | | | | | | | | | A01=Genes involved in familial amyloidosis}}
{{familytree | | |,|-|-|-|v|-|-|-|v|-|-|-|+|-|-|-|v|-|-|-|v|-|-|-|.| | }}
{{familytree | | |,|-|-|-|v|-|-|-|v|-|-|-|+|-|-|-|v|-|-|-|v|-|-|-|.| | }}
{{familytree | | B10 | | B11 | | B12 | | B13 | | B14 | | B15 | | B16 |B10=Transthyretin (TTR)|B11=Apolipoprotein AI|B12=Gelsolin|B13=Lysozyme|B14=Cystatin C|B15=Fibrinogen Aa-chain|B16=Apolipoprotein AII}}  
{{familytree | | B10 | | B11 | | B12 | | B13 | | B14 | | B15 | | B16 |B10=Transthyretin (TTR)|B11=Apolipoprotein AI|B12=Gelsolin|B13=Lysozyme|B14=Cystatin C|B15=Fibrinogen Aa-chain|B16=Apolipoprotein AII}}  
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*Amyloid depositions also have glycosaminoglycans and serum amyloid P component (SAP) which alter the propensity for amyloid formation.<ref name="pmid8202534">{{cite journal |vauthors=Pepys MB, Rademacher TW, Amatayakul-Chantler S, Williams P, Noble GE, Hutchinson WL, Hawkins PN, Nelson SR, Gallimore JR, Herbert J |title=Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue=12 |pages=5602–6 |date=June 1994 |pmid=8202534 |pmc=44044 |doi=10.1073/pnas.91.12.5602 |url=}}</ref><ref name="pmid7868080">{{cite journal |vauthors=Tan SY, Pepys MB |title=Amyloidosis |journal=Histopathology |volume=25 |issue=5 |pages=403–14 |date=November 1994 |pmid=7868080 |doi=10.1111/j.1365-2559.1994.tb00001.x |url=}}</ref><ref name="pmid9256275">{{cite journal |vauthors=Botto M, Hawkins PN, Bickerstaff MC, Herbert J, Bygrave AE, McBride A, Hutchinson WL, Tennent GA, Walport MJ, Pepys MB |title=Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene |journal=Nat. Med. |volume=3 |issue=8 |pages=855–9 |date=August 1997 |pmid=9256275 |doi=10.1038/nm0897-855 |url=}}</ref>
*Amyloid depositions also have glycosaminoglycans and serum amyloid P component (SAP) which alter the propensity for amyloid formation.<ref name="pmid8202534">{{cite journal |vauthors=Pepys MB, Rademacher TW, Amatayakul-Chantler S, Williams P, Noble GE, Hutchinson WL, Hawkins PN, Nelson SR, Gallimore JR, Herbert J |title=Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue=12 |pages=5602–6 |date=June 1994 |pmid=8202534 |pmc=44044 |doi=10.1073/pnas.91.12.5602 |url=}}</ref><ref name="pmid7868080">{{cite journal |vauthors=Tan SY, Pepys MB |title=Amyloidosis |journal=Histopathology |volume=25 |issue=5 |pages=403–14 |date=November 1994 |pmid=7868080 |doi=10.1111/j.1365-2559.1994.tb00001.x |url=}}</ref><ref name="pmid9256275">{{cite journal |vauthors=Botto M, Hawkins PN, Bickerstaff MC, Herbert J, Bygrave AE, McBride A, Hutchinson WL, Tennent GA, Walport MJ, Pepys MB |title=Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene |journal=Nat. Med. |volume=3 |issue=8 |pages=855–9 |date=August 1997 |pmid=9256275 |doi=10.1038/nm0897-855 |url=}}</ref>
*[[Amyloid]] deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.<ref name="pmid267192342">{{cite journal |vauthors=Wechalekar AD, Gillmore JD, Hawkins PN |title=Systemic amyloidosis |journal=Lancet |volume=387 |issue=10038 |pages=2641–2654 |date=June 2016 |pmid=26719234 |doi=10.1016/S0140-6736(15)01274-X |url=}}</ref>
*[[Amyloid]] deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.<ref name="pmid267192342">{{cite journal |vauthors=Wechalekar AD, Gillmore JD, Hawkins PN |title=Systemic amyloidosis |journal=Lancet |volume=387 |issue=10038 |pages=2641–2654 |date=June 2016 |pmid=26719234 |doi=10.1016/S0140-6736(15)01274-X |url=}}</ref>
*Genetic mutations in different genes may lead to misfolding protein product.
*Genetic mutations in Apolipoprotein AI gene may lead to misfolding protein product.


==Genetics==
===Genetics===
 
* Familial ATTR amyloidosis is transmitted in [[Autosome|autosomal]] [[Dominance relationship|dominant]] pattern but it can have a heterogeneous nature of presentation.<ref name="pmid11261421">{{cite journal |vauthors=Hund E, Linke RP, Willig F, Grau A |title=Transthyretin-associated neuropathic amyloidosis. Pathogenesis and treatment |journal=Neurology |volume=56 |issue=4 |pages=431–5 |date=February 2001 |pmid=11261421 |doi=10.1212/wnl.56.4.431 |url=}}</ref><ref name="pmid28978215">{{cite journal |vauthors=Gertz MA |title=Hereditary ATTR amyloidosis: burden of illness and diagnostic challenges |journal=Am J Manag Care |volume=23 |issue=7 Suppl |pages=S107–S112 |date=June 2017 |pmid=28978215 |doi= |url=}}</ref><ref name="pmid116772762" />
 
* Genes involved in the pathogenesis of Familial ATTR amyloidosis include:<ref name="Benson2003">{{cite journal|last1=Benson|first1=Merrill D|title=The hereditary amyloidoses|journal=Best Practice & Research Clinical Rheumatology|volume=17|issue=6|year=2003|pages=909–927|issn=15216942|doi=10.1016/j.berh.2003.09.001}}</ref><ref name="Benson20032">{{cite journal|last1=Benson|first1=Merrill D|title=The hereditary amyloidoses|journal=Best Practice & Research Clinical Rheumatology|volume=17|issue=6|year=2003|pages=909–927|issn=15216942|doi=10.1016/j.berh.2003.09.001}}</ref><ref>{{cite book | last = Scriver | first = Charles | title = The metabolic & molecular bases of inherited disease | publisher = McGraw-Hill | location = New York | year = 2001 | isbn = 978-0079130358 }}</ref>
**Transthyretin amyloidosis (ATTR)<ref name="pmid61594">{{cite journal |vauthors=Robbins J |title=Thyroxine-binding proteins |journal=Prog. Clin. Biol. Res. |volume=5 |issue= |pages=331–55 |date=1976 |pmid=61594 |doi= |url=}}</ref><ref name="pmid2320592">{{cite journal |vauthors=Westermark P, Sletten K, Johansson B, Cornwell GG |title=Fibril in senile systemic amyloidosis is derived from normal transthyretin |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue=7 |pages=2843–5 |date=April 1990 |pmid=2320592 |pmc=53787 |doi=10.1073/pnas.87.7.2843 |url=}}</ref><ref name="pmid1685359">{{cite journal |vauthors=Holmgren G, Steen L, Ekstedt J, Groth CG, Ericzon BG, Eriksson S, Andersen O, Karlberg I, Nordén G, Nakazato M |title=Biochemical effect of liver transplantation in two Swedish patients with familial amyloidotic polyneuropathy (FAP-met30) |journal=Clin. Genet. |volume=40 |issue=3 |pages=242–6 |date=September 1991 |pmid=1685359 |doi=10.1111/j.1399-0004.1991.tb03085.x |url=}}</ref>
***The most common type of familial amyloidosis.
***Single nucleotide substitution on transthyretin gene on chromosome 18 leads to nonfunctional transthyretin protein.
***Transthyretin protein is responsible for thyroid hormone and vitamin A transport and is produced by liver.
***We can find normal transthyretin protein deposition in aged individuals (senile cardiac amyloid).
***Mutant transthyretin protein accelerate the process of deposition and leads to early onset disease.
**Apolipoprotein AI amyloidosis (A ApoAI)<ref name="pmid9356442">{{cite journal |vauthors=Borhani DW, Rogers DP, Engler JA, Brouillette CG |title=Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue=23 |pages=12291–6 |date=November 1997 |pmid=9356442 |pmc=24911 |doi=10.1073/pnas.94.23.12291 |url=}}</ref>
***Single nucleotide substitutions in apolipoprotein AI gene.
***The underlying pathogenesis is incomplete degradation of this protein in body.
***The mode of inheritance in autosomal dominant with different penetrance.
****
**Gelsolin amyloidosis (A Gel)<ref name="pmid2176164">{{cite journal |vauthors=Maury CP, Kere J, Tolvanen R, de la Chapelle A |title=Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene |journal=FEBS Lett. |volume=276 |issue=1-2 |pages=75–7 |date=December 1990 |pmid=2176164 |doi=10.1016/0014-5793(90)80510-p |url=}}</ref><ref name="pmid1338910">{{cite journal |vauthors=de la Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J |title=Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187 |journal=Nat. Genet. |volume=2 |issue=2 |pages=157–60 |date=October 1992 |pmid=1338910 |doi=10.1038/ng1092-157 |url=}}</ref>
***Gelsolin protein is produced in skeletal muscle and macrophages.
***2 different mutations in gelsolin gene on chromosome 9 including Asp187Asn and Asp187Tyr leads to amyloid deposition and Gelsolin amyloidosis.
**Lysozyme amyloidosis (A Lys)<ref name="pmid8464497">{{cite journal |vauthors=Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ |title=Human lysozyme gene mutations cause hereditary systemic amyloidosis |journal=Nature |volume=362 |issue=6420 |pages=553–7 |date=April 1993 |pmid=8464497 |doi=10.1038/362553a0 |url=}}</ref>
***4 different mutations on lysozyme gene including Ile56Thr, Asp67His, Trp64Arg, and Phe57Ile has been found to be associated with amyloidosis.
**Cystatin C amyloidosis (A Cys)<ref name="pmid4655034">{{cite journal |vauthors=Gudmundsson G, Hallgrímsson J, Jónasson TA, Bjarnason O |title=Hereditary cerebral haemorrhage with amyloidosis |journal=Brain |volume=95 |issue=2 |pages=387–404 |date=1972 |pmid=4655034 |doi=10.1093/brain/95.2.387 |url=}}</ref><ref name="pmid3707586">{{cite journal |vauthors=Ghiso J, Pons-Estel B, Frangione B |title=Hereditary cerebral amyloid angiopathy: the amyloid fibrils contain a protein which is a variant of cystatin C, an inhibitor of lysosomal cysteine proteases |journal=Biochem. Biophys. Res. Commun. |volume=136 |issue=2 |pages=548–54 |date=April 1986 |pmid=3707586 |doi=10.1016/0006-291x(86)90475-4 |url=}}</ref>
***Cystatin C is a serine protease inhibitor.
***Leu68Gln mutation in its gene leads to cystatin C amyloidosis.
**Fibrinogen Aa-chain amyloidosis (A Fib)<ref name="pmid8113408">{{cite journal |vauthors=Uemichi T, Liepnieks JJ, Benson MD |title=Hereditary renal amyloidosis with a novel variant fibrinogen |journal=J. Clin. Invest. |volume=93 |issue=2 |pages=731–6 |date=February 1994 |pmid=8113408 |pmc=293912 |doi=10.1172/JCI117027 |url=}}</ref>
***4 different mutations including Arg554Leu, Glu526Val, 4904delG, and 4897delT has been found to be associated with amyloidosis.
**Apolipoprotein AII amyloidosis (A ApoAII)<ref name="pmid11401442">{{cite journal |vauthors=Benson MD, Liepnieks JJ, Yazaki M, Yamashita T, Hamidi Asl K, Guenther B, Kluve-Beckerman B |title=A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene |journal=Genomics |volume=72 |issue=3 |pages=272–7 |date=March 2001 |pmid=11401442 |doi=10.1006/geno.2000.6499 |url=}}</ref>
***It was discovered recently.
***3 different mutations in the stop codon for the ApoAII gene including stop78Gly, stop78Ser, and stop78Arg has been found to be associated with amyloidosis.
***These mutations lead to an extra 21-amino acid at the carboxyl terminal end of the protein.


*Single nucleotide substitutions in apolipoprotein AI gene.<ref name="pmid9356442">{{cite journal |vauthors=Borhani DW, Rogers DP, Engler JA, Brouillette CG |title=Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue=23 |pages=12291–6 |date=November 1997 |pmid=9356442 |pmc=24911 |doi=10.1073/pnas.94.23.12291 |url=}}</ref>
*The underlying pathogenesis is incomplete degradation of this protein in body.
*The mode of inheritance in autosomal dominant with different penetrance.


==Causes==
==Causes==
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==Epidemiology and Demographics==
==Epidemiology and Demographics==


*The [[incidence]] of amyloidosis is approximately 1.2 per 100,000 individuals per year worldwide.<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>


==Risk Factors==
*The [[mortality rate]] of systemic amyloidosis is approximately 100 per 100,000 deaths in developed countries.<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>
There are no established risk factors for [disease name].
 
OR


The most potent risk factor in the development of [disease name] is [risk factor 1]. Other risk factors include [risk factor 2], [risk factor 3], and [risk factor 4].
* [[Apolipoprotein AI]] amyloidosis commonly affects individuals older than 30.


OR
*Hereditary amyloidosis subtypes include a substitution of an [[amino acid]] that is detected in approximately 4% of the african american population.<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>


Common risk factors in the development of [disease name] include [risk factor 1], [risk factor 2], [risk factor 3], and [risk factor 4].
*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>


OR
==Risk Factors==
 
*Common risk factors in the development of apolipoprotein AI amyloidosis include:<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><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><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>
Common risk factors in the development of [disease name] may be occupational, environmental, genetic, and viral.
**Older age
**Male gender
**African american race
**Positive family history


==Screening==
==Screening==
There is insufficient evidence to recommend routine screening for [disease/malignancy].
There is insufficient evidence to recommend routine screening for apolipoprotein AI amyloidosis.
 
OR
 
According to the [guideline name], screening for [disease name] is not recommended.
 
OR
 
According to the [guideline name], screening for [disease name] by [test 1] is recommended every [duration] among patients with [condition 1], [condition 2], and [condition 3].


==Natural History, Complications, and Prognosis==
==Natural History, Complications, and Prognosis==
If left untreated, [#]% of patients with [disease name] may progress to develop [manifestation 1], [manifestation 2], and [manifestation 3].
OR
Common complications of [disease name] include [complication 1], [complication 2], and [complication 3].


OR
Prognosis is generally excellent/good/poor, and the 1/5/10-year mortality/survival rate of patients with [disease name] is approximately [#]%.


==Diagnosis==
==Diagnosis==
===Diagnostic Study of Choice===
===Diagnostic Study of Choice===
The diagnosis of [disease name] is made when at least [number] of the following [number] diagnostic criteria are met: [criterion 1], [criterion 2], [criterion 3], and [criterion 4].
OR
The diagnosis of [disease name] is based on the [criteria name] criteria, which include [criterion 1], [criterion 2], and [criterion 3].


OR
* Tissue biopsy with Congo red stain is the gold standard test for the diagnosis of apolipoprotein AI amyloidosis.<ref name="pmid12553428">{{cite journal |vauthors=Benson MD, Yazaki M, Magy N |title=Laboratory assessment of transthyretin amyloidosis |journal=Clin. Chem. Lab. Med. |volume=40 |issue=12 |pages=1262–5 |date=December 2002 |pmid=12553428 |doi=10.1515/CCLM.2002.218 |url=}}</ref>
* Biopsy tissue may be taken from an affected organ like kidney, or from subcutaneous fat or rectal mucosa.
* The rectal mucosa biopsy is more sensitive for apolipoprotein AI amyloidosis.
* Biopsy of the affected organ is recommended for patients with limited organ involvement.<ref name="pmid12479513">{{cite journal |vauthors=Andrews TR, Colon-Otero G, Calamia KT, Menke DM, Boylan KB, Kyle RA |title=Utility of subcutaneous fat aspiration for diagnosing amyloidosis in patients with isolated peripheral neuropathy |journal=Mayo Clin. Proc. |volume=77 |issue=12 |pages=1287–90 |date=December 2002 |pmid=12479513 |doi=10.4065/77.12.1287 |url=}}</ref>
* Biopsy from unaffected organs is more sensitive in patients with multi-organ involvement.
* The following finding on performing tissue biopsy is confirmatory for familial amyloidosis:<ref name="pmid13657054">{{cite journal |vauthors=COHEN AS, CALKINS E |title=Electron microscopic observations on a fibrous component in amyloid of diverse origins |journal=Nature |volume=183 |issue=4669 |pages=1202–3 |date=April 1959 |pmid=13657054 |doi=10.1038/1831202a0 |url=}}</ref><ref name="pmid11552976">{{cite journal |vauthors=Kyle RA |title=Amyloidosis: a convoluted story |journal=Br. J. Haematol. |volume=114 |issue=3 |pages=529–38 |date=September 2001 |pmid=11552976 |doi=10.1046/j.1365-2141.2001.02999.x |url=}}</ref>
** Apple green birefringence of the tissue sample under polarized light with Congo red stain.


The diagnosis of [disease name] is based on the [definition name] definition, which includes [criterion 1], [criterion 2], and [criterion 3].
* There are no established criteria for the diagnosis of familial amyloidosis.
 
OR
 
There are no established criteria for the diagnosis of [disease name].


===History and Symptoms===
===History and Symptoms===
The majority of patients with [disease name] are asymptomatic.


OR
* Patients with apolipoprotein AI amyloidosis may have a positive history of dyspnea, lethargy, weight loss, chest discomfort, fevers or [[chills]], night sweats, positive family history of amyloidosis, male gender, and african american race<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>


The hallmark of [disease name] is [finding]. A positive history of [finding 1] and [finding 2] is suggestive of [disease name]. The most common symptoms of [disease name] include [symptom 1], [symptom 2], and [symptom 3]. Common symptoms of [disease] include [symptom 1], [symptom 2], and [symptom 3]. Less common symptoms of [disease name] include [symptom 1], [symptom 2], and [symptom 3].
* Common [[symptoms]] of apolipoprotein AI amyloidosis include parasthesia, edema, cutaneous lesions, hoarseness, and cough<ref name="pmid4304452">{{cite journal |vauthors=Van Allen MW, Frohlich JA, Davis JR |title=Inherited predisposition to generalized amyloidosis. Clinical and pathological study of a family with neuropathy, nephropathy, and peptic ulcer |journal=Neurology |volume=19 |issue=1 |pages=10–25 |date=January 1969 |pmid=4304452 |doi=10.1212/wnl.19.1.10 |url=}}</ref><ref name="pmid10198255">{{cite journal |vauthors=Hamidi Asl K, Liepnieks JJ, Nakamura M, Parker F, Benson MD |title=A novel apolipoprotein A-1 variant, Arg173Pro, associated with cardiac and cutaneous amyloidosis |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue=2 |pages=584–8 |date=April 1999 |pmid=10198255 |doi=10.1006/bbrc.1999.0518 |url=}}</ref>


* Less common [[symptoms]] of apolipoprotein AI amyloidosis include hoarseness, gastrointestinal bleeding, diarrhea, paresthesias, gross [[hematuria]], and irritative [[urinary symptoms]]<ref name="pmid10228037">{{cite journal |vauthors=Hamidi Asl K, Liepnieks JJ, Nakamura M, Benson MD |title=Organ-specific (localized) synthesis of Ig light chain amyloid |journal=J. Immunol. |volume=162 |issue=9 |pages=5556–60 |date=May 1999 |pmid=10228037 |doi= |url=}}</ref>
===Physical Examination===
===Physical Examination===
Patients with [disease name] usually appear [general appearance]. Physical examination of patients with [disease name] is usually remarkable for [finding 1], [finding 2], and [finding 3].
[[Physical examination]] of patients with apolipoprotein AI amyloidosis is usually remarkable for sensory and motor neuropathy, edema, and cutaneous lesion.
 
OR
 
Common physical examination findings of [disease name] include [finding 1], [finding 2], and [finding 3].
 
OR
 
The presence of [finding(s)] on physical examination is diagnostic of [disease name].
 
OR
 
The presence of [finding(s)] on physical examination is highly suggestive of [disease name].
 
===Laboratory Findings===
===Laboratory Findings===
An elevated/reduced concentration of serum/blood/urinary/CSF/other [lab test] is diagnostic of [disease name].
OR
Laboratory findings consistent with the diagnosis of [disease name] include [abnormal test 1], [abnormal test 2], and [abnormal test 3].


OR
* Common [[Test|tests]] that are abnormal in [[liver function tests]] including [[AST]], [[ALT]], total [[bilirubin]], alkaline phosphatase, and albumin.<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><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="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>


[Test] is usually normal among patients with [disease name].
* Common [[Test|tests]] that are abnormal in renal function [[Test|tests]] including serum creatinine, urinary [[protein]], glomerular filtration rate, and albumin to [[creatinine]] ratio in the [[urine]].


OR
* [[Cardiac biomarkers]] such as troponin and BNP and are the most important predictors of outcome in amyloidosis. They provide a quantitative assessment for [[Heart|cardiac]] damage and wall strain.
 
Some patients with [disease name] may have elevated/reduced concentration of [test], which is usually suggestive of [progression/complication].
 
OR
 
There are no diagnostic laboratory findings associated with [disease name].


===Electrocardiogram===
===Electrocardiogram===
There are no ECG findings associated with [disease name].


OR
* Findings on an ECG suggestive of apolipoprotein AI amyloidosis include low voltage in the limb leads, AV block, atrial fibrillation, heart block, and angina or infarction<ref name="pmid9290406">{{cite journal |vauthors=Dubrey SW, Cha K, Skinner M, LaValley M, Falk RH |title=Familial and primary (AL) cardiac amyloidosis: echocardiographically similar diseases with distinctly different clinical outcomes |journal=Heart |volume=78 |issue=1 |pages=74–82 |date=July 1997 |pmid=9290406 |pmc=484868 |doi=10.1136/hrt.78.1.74 |url=}}</ref><ref name="pmid16186440">{{cite journal |vauthors=Falk RH |title=Diagnosis and management of the cardiac amyloidoses |journal=Circulation |volume=112 |issue=13 |pages=2047–60 |date=September 2005 |pmid=16186440 |doi=10.1161/CIRCULATIONAHA.104.489187 |url=}}</ref>
 
An ECG may be helpful in the diagnosis of [disease name]. Findings on an ECG suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].


===X-ray===
===X-ray===
There are no x-ray findings associated with [disease name].


OR
* There are no x-ray findings associated with apolipoprotein AI amyloidosis.<br />
 
An x-ray may be helpful in the diagnosis of [disease name]. Findings on an x-ray suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].
 
OR
 
There are no x-ray findings associated with [disease name]. However, an x-ray may be helpful in the diagnosis of complications of [disease name], which include [complication 1], [complication 2], and [complication 3].


===Echocardiography or Ultrasound===
===Echocardiography or Ultrasound===
There are no echocardiography/ultrasound  findings associated with [disease name].
*Findings on echocardiography suggestive of apolipoprotein AI amyloidosis include:<ref name="pmid2647814">{{cite journal |vauthors=Klein AL, Hatle LK, Burstow DJ, Seward JB, Kyle RA, Bailey KR, Luscher TF, Gertz MA, Tajik AJ |title=Doppler characterization of left ventricular diastolic function in cardiac amyloidosis |journal=J. Am. Coll. Cardiol. |volume=13 |issue=5 |pages=1017–26 |date=April 1989 |pmid=2647814 |doi= |url=}}</ref><ref name="pmid26693331">{{cite journal |vauthors=Pantazis A, Vischer AS, Perez-Tome MC, Castelletti S |title=Diagnosis and management of hypertrophic cardiomyopathy |journal=Echo Res Pract |volume=2 |issue=1 |pages=R45–53 |date=March 2015 |pmid=26693331 |pmc=4676455 |doi=10.1530/ERP-15-0007 |url=}}</ref><ref name="pmid18192942">{{cite journal |vauthors=Eshaghian S, Kaul S, Shah PK |title=Cardiac amyloidosis: new insights into diagnosis and management |journal=Rev Cardiovasc Med |volume=8 |issue=4 |pages=189–99 |date=2007 |pmid=18192942 |doi= |url=}}</ref>
 
**Sparkling or speckled appearance of the [[left ventricular]] thickening
OR
**[[Hypertrophy (medical)|Hypertrophied]] [[right ventricle]]
 
**[[Diastolic dysfunction]] with restrictive filling pattern (in the advanced stages)
Echocardiography/ultrasound  may be helpful in the diagnosis of [disease name]. Findings on an echocardiography/ultrasound suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].
**Severe [[Atrial|atrial dilatation]]
 
**Thickening of the [[interatrial septum]]
OR
**[[Pericardial effusion]]
 
**Prominent [[Valves of the heart|valves]]
There are no echocardiography/ultrasound  findings associated with [disease name]. However, an echocardiography/ultrasound  may be helpful in the diagnosis of complications of [disease name], which include [complication 1], [complication 2], and [complication 3].


===CT scan===
===CT scan===
There are no CT scan findings associated with [disease name].
<br />
 
OR
 
[Location] CT scan may be helpful in the diagnosis of [disease name]. Findings on CT scan suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].
 
OR
 
There are no CT scan findings associated with [disease name]. However, a CT scan may be helpful in the diagnosis of complications of [disease name], which include [complication 1], [complication 2], and [complication 3].


===MRI===
===MRI===
There are no MRI findings associated with [disease name].
<br />
 
OR
 
[Location] MRI may be helpful in the diagnosis of [disease name]. Findings on MRI suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].
 
OR
 
There are no MRI findings associated with [disease name]. However, a MRI may be helpful in the diagnosis of complications of [disease name], which include [complication 1], [complication 2], and [complication 3].


===Other Imaging Findings===
===Other Imaging Findings===
There are no other imaging findings associated with [disease name].
There are no other imaging findings associated with apolipoprotein AI amyloidosis.<br />
 
OR
 
[Imaging modality] may be helpful in the diagnosis of [disease name]. Findings on an [imaging modality] suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].


===Other Diagnostic Studies===
===Other Diagnostic Studies===
There are no other diagnostic studies associated with [disease name].
There are no other diagnostic studies associated with apolipoprotein AI amyloidosis.<br />
 
OR
 
[Diagnostic study] may be helpful in the diagnosis of [disease name]. Findings suggestive of/diagnostic of [disease name] include [finding 1], [finding 2], and [finding 3].
 
OR
 
Other diagnostic studies for [disease name] include [diagnostic study 1], which demonstrates [finding 1], [finding 2], and [finding 3], and [diagnostic study 2], which demonstrates [finding 1], [finding 2], and [finding 3].


==Treatment==
==Treatment==
===Medical Therapy===
===Medical Therapy===
There is no treatment for [disease name]; the mainstay of therapy is supportive care.
There is no medical therapy for apolipoprotein AI amyloidosis. The mainstay of therapy is supportive care.<br />
 
OR
 
Supportive therapy for [disease name] includes [therapy 1], [therapy 2], and [therapy 3].
 
OR
 
The majority of cases of [disease name] are self-limited and require only supportive care.
 
OR
 
[Disease name] is a medical emergency and requires prompt treatment.
 
OR
 
The mainstay of treatment for [disease name] is [therapy].
 
OR
 
The optimal therapy for [malignancy name] depends on the stage at diagnosis.
 
OR
 
[Therapy] is recommended among all patients who develop [disease name].
 
OR
 
Pharmacologic medical therapy is recommended among patients with [disease subclass 1], [disease subclass 2], and [disease subclass 3].
 
OR
 
Pharmacologic medical therapies for [disease name] include (either) [therapy 1], [therapy 2], and/or [therapy 3].
 
OR
 
Empiric therapy for [disease name] depends on [disease factor 1] and [disease factor 2].
 
OR
 
Patients with [disease subclass 1] are treated with [therapy 1], whereas patients with [disease subclass 2] are treated with [therapy 2].


===Surgery===
===Surgery===
Surgical intervention is not recommended for the management of [disease name].
*[[Cardiac transplantation|Cardiac transplant]] may need to be done for patients with cardiac amyloidosis.<ref name="pmid23227279">{{cite journal| author=Estep JD, Bhimaraj A, Cordero-Reyes AM, Bruckner B, Loebe M, Torre-Amione G| title=Heart transplantation and end-stage cardiac amyloidosis: a review and approach to evaluation and management. | journal=Methodist Debakey Cardiovasc J | year= 2012 | volume= 8 | issue= 3 | pages= 8-16 | pmid=23227279 | doi= | pmc=3487570 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=23227279  }} </ref>
 
*[[Organ transplant|Organ-specific transplant]] may need to be done, depending on the [[Organ (anatomy)|organ]] involved.
OR
 
Surgery is not the first-line treatment option for patients with [disease name]. Surgery is usually reserved for patients with either [indication 1], [indication 2], and [indication 3]
 
OR
 
The mainstay of treatment for [disease name] is medical therapy. Surgery is usually reserved for patients with either [indication 1], [indication 2], and/or [indication 3].
 
OR
 
The feasibility of surgery depends on the stage of [malignancy] at diagnosis.
 
OR
 
Surgery is the mainstay of treatment for [disease or malignancy].


===Primary Prevention===
===Primary Prevention===
There are no established measures for the primary prevention of [disease name].
There is no role for primaryprevention in apolipoprotein AI amyloidosis.
 
OR
 
There are no available vaccines against [disease name].
 
OR
 
Effective measures for the primary prevention of [disease name] include [measure1], [measure2], and [measure3].
 
OR
 
[Vaccine name] vaccine is recommended for [patient population] to prevent [disease name]. Other primary prevention strategies include [strategy 1], [strategy 2], and [strategy 3].


===Secondary Prevention===
===Secondary Prevention===
There are no established measures for the secondary prevention of [disease name].
There is no role for secondary prevention in apolipoprotein AI amyloidosis.
 
OR
 
Effective measures for the secondary prevention of [disease name] include [strategy 1], [strategy 2], and [strategy 3].


==References==
==References==

Latest revision as of 17:03, 13 November 2019

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Fahimeh Shojaei, M.D.

Synonyms and keywords:

Overview

Historical Perspective

Classification

Apolipoprotein AI amyloidosis is one of the subtypes of familial amyloidosis. Familiar amyloidosis may be classified according to the type of mutant protein into 7 subtypes:[4][5][6]

 
 
 
 
 
 
 
 
 
 
 
 
 
Genes involved in familial amyloidosis
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
Transthyretin (TTR)
 
Apolipoprotein AI
 
Gelsolin
 
Lysozyme
 
Cystatin C
 
Fibrinogen Aa-chain
 
Apolipoprotein AII


Pathophysiology

Pathogenesis

  • It is understood that amyloidosis is the result of deposition of Amyloid.[7]
  • Amyloid is an abnormal insoluble extracellular protein which may cause organic dysfunction and a wide variety of clinical syndromes.
  • These abnormal amyloids are derived from misfolding and aggregation of normally soluble proteins.
  • Amyloid depositions also have glycosaminoglycans and serum amyloid P component (SAP) which alter the propensity for amyloid formation.[8][9][10]
  • Amyloid deposition can disrupt tissue structure of involved organ and consequently leads to organ failure.[11]
  • Genetic mutations in Apolipoprotein AI gene may lead to misfolding protein product.

Genetics

  • Single nucleotide substitutions in apolipoprotein AI gene.[12]
  • The underlying pathogenesis is incomplete degradation of this protein in body.
  • The mode of inheritance in autosomal dominant with different penetrance.

Causes

Common cause of Apolipoprotein AI amyloidosis is genetic mutation.[13][4][5][14]

Differentiating Apolipoprotein AI amyloidosis from Other Diseases

Epidemiology and Demographics

  • The incidence of amyloidosis is approximately 1.2 per 100,000 individuals per year worldwide.[15]
  • The mortality rate of systemic amyloidosis is approximately 100 per 100,000 deaths in developed countries.[16]
  • Hereditary amyloidosis subtypes include a substitution of an amino acid that is detected in approximately 4% of the african american population.[3]
  • Men are more commonly affected by amyloidosis than women.[17]

Risk Factors

  • Common risk factors in the development of apolipoprotein AI amyloidosis include:[17][3][18]
    • Older age
    • Male gender
    • African american race
    • Positive family history

Screening

There is insufficient evidence to recommend routine screening for apolipoprotein AI amyloidosis.

Natural History, Complications, and Prognosis

Diagnosis

Diagnostic Study of Choice

  • Tissue biopsy with Congo red stain is the gold standard test for the diagnosis of apolipoprotein AI amyloidosis.[19]
  • Biopsy tissue may be taken from an affected organ like kidney, or from subcutaneous fat or rectal mucosa.
  • The rectal mucosa biopsy is more sensitive for apolipoprotein AI amyloidosis.
  • Biopsy of the affected organ is recommended for patients with limited organ involvement.[20]
  • Biopsy from unaffected organs is more sensitive in patients with multi-organ involvement.
  • The following finding on performing tissue biopsy is confirmatory for familial amyloidosis:[21][22]
    • Apple green birefringence of the tissue sample under polarized light with Congo red stain.
  • There are no established criteria for the diagnosis of familial amyloidosis.

History and Symptoms

  • Patients with apolipoprotein AI amyloidosis may have a positive history of dyspnea, lethargy, weight loss, chest discomfort, fevers or chills, night sweats, positive family history of amyloidosis, male gender, and african american race[23]
  • Common symptoms of apolipoprotein AI amyloidosis include parasthesia, edema, cutaneous lesions, hoarseness, and cough[24][25]

Physical Examination

Physical examination of patients with apolipoprotein AI amyloidosis is usually remarkable for sensory and motor neuropathy, edema, and cutaneous lesion.

Laboratory Findings

  • Common tests that are abnormal in renal function tests including serum creatinine, urinary protein, glomerular filtration rate, and albumin to creatinine ratio in the urine.
  • Cardiac biomarkers such as troponin and BNP and are the most important predictors of outcome in amyloidosis. They provide a quantitative assessment for cardiac damage and wall strain.

Electrocardiogram

  • Findings on an ECG suggestive of apolipoprotein AI amyloidosis include low voltage in the limb leads, AV block, atrial fibrillation, heart block, and angina or infarction[30][31]

X-ray

  • There are no x-ray findings associated with apolipoprotein AI amyloidosis.

Echocardiography or Ultrasound

CT scan


MRI


Other Imaging Findings

There are no other imaging findings associated with apolipoprotein AI amyloidosis.

Other Diagnostic Studies

There are no other diagnostic studies associated with apolipoprotein AI amyloidosis.

Treatment

Medical Therapy

There is no medical therapy for apolipoprotein AI amyloidosis. The mainstay of therapy is supportive care.

Surgery

Primary Prevention

There is no role for primaryprevention in apolipoprotein AI amyloidosis.

Secondary Prevention

There is no role for secondary prevention in apolipoprotein AI amyloidosis.

References

  1. ↑ 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. ↑ 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.
  3. ↑ 3.0 3.1 3.2 Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
  4. ↑ 4.0 4.1 Benson, Merrill D (2003). "The hereditary amyloidoses". Best Practice & Research Clinical Rheumatology. 17 (6): 909–927. doi:10.1016/j.berh.2003.09.001. ISSN 1521-6942.
  5. ↑ 5.0 5.1 Benson, Merrill D (2003). "The hereditary amyloidoses". Best Practice & Research Clinical Rheumatology. 17 (6): 909–927. doi:10.1016/j.berh.2003.09.001. ISSN 1521-6942.
  6. ↑ Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.
  7. ↑ Wechalekar AD, Gillmore JD, Hawkins PN (June 2016). "Systemic amyloidosis". Lancet. 387 (10038): 2641–2654. doi:10.1016/S0140-6736(15)01274-X. PMID 26719234.
  8. ↑ Pepys MB, Rademacher TW, Amatayakul-Chantler S, Williams P, Noble GE, Hutchinson WL, Hawkins PN, Nelson SR, Gallimore JR, Herbert J (June 1994). "Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure". Proc. Natl. Acad. Sci. U.S.A. 91 (12): 5602–6. doi:10.1073/pnas.91.12.5602. PMC 44044. PMID 8202534.
  9. ↑ Tan SY, Pepys MB (November 1994). "Amyloidosis". Histopathology. 25 (5): 403–14. doi:10.1111/j.1365-2559.1994.tb00001.x. PMID 7868080.
  10. ↑ Botto M, Hawkins PN, Bickerstaff MC, Herbert J, Bygrave AE, McBride A, Hutchinson WL, Tennent GA, Walport MJ, Pepys MB (August 1997). "Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene". Nat. Med. 3 (8): 855–9. doi:10.1038/nm0897-855. PMID 9256275.
  11. ↑ Wechalekar AD, Gillmore JD, Hawkins PN (June 2016). "Systemic amyloidosis". Lancet. 387 (10038): 2641–2654. doi:10.1016/S0140-6736(15)01274-X. PMID 26719234.
  12. ↑ Borhani DW, Rogers DP, Engler JA, Brouillette CG (November 1997). "Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation". Proc. Natl. Acad. Sci. U.S.A. 94 (23): 12291–6. doi:10.1073/pnas.94.23.12291. PMC 24911. PMID 9356442.
  13. ↑ Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ (April 1993). "Human lysozyme gene mutations cause hereditary systemic amyloidosis". Nature. 362 (6420): 553–7. doi:10.1038/362553a0. PMID 8464497.
  14. ↑ Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.
  15. ↑ Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
  16. ↑ Pepys MB (2006). "Amyloidosis". Annu. Rev. Med. 57: 223–41. doi:10.1146/annurev.med.57.121304.131243. PMID 16409147.
  17. ↑ 17.0 17.1 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.
  18. ↑ 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.
  19. ↑ Benson MD, Yazaki M, Magy N (December 2002). "Laboratory assessment of transthyretin amyloidosis". Clin. Chem. Lab. Med. 40 (12): 1262–5. doi:10.1515/CCLM.2002.218. PMID 12553428.
  20. ↑ Andrews TR, Colon-Otero G, Calamia KT, Menke DM, Boylan KB, Kyle RA (December 2002). "Utility of subcutaneous fat aspiration for diagnosing amyloidosis in patients with isolated peripheral neuropathy". Mayo Clin. Proc. 77 (12): 1287–90. doi:10.4065/77.12.1287. PMID 12479513.
  21. ↑ COHEN AS, CALKINS E (April 1959). "Electron microscopic observations on a fibrous component in amyloid of diverse origins". Nature. 183 (4669): 1202–3. doi:10.1038/1831202a0. PMID 13657054.
  22. ↑ Kyle RA (September 2001). "Amyloidosis: a convoluted story". Br. J. Haematol. 114 (3): 529–38. doi:10.1046/j.1365-2141.2001.02999.x. PMID 11552976.
  23. ↑ 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.
  24. ↑ Van Allen MW, Frohlich JA, Davis JR (January 1969). "Inherited predisposition to generalized amyloidosis. Clinical and pathological study of a family with neuropathy, nephropathy, and peptic ulcer". Neurology. 19 (1): 10–25. doi:10.1212/wnl.19.1.10. PMID 4304452.
  25. ↑ Hamidi Asl K, Liepnieks JJ, Nakamura M, Parker F, Benson MD (April 1999). "A novel apolipoprotein A-1 variant, Arg173Pro, associated with cardiac and cutaneous amyloidosis". Biochem. Biophys. Res. Commun. 257 (2): 584–8. doi:10.1006/bbrc.1999.0518. PMID 10198255.
  26. ↑ Hamidi Asl K, Liepnieks JJ, Nakamura M, Benson MD (May 1999). "Organ-specific (localized) synthesis of Ig light chain amyloid". J. Immunol. 162 (9): 5556–60. PMID 10228037.
  27. ↑ 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.
  28. ↑ Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
  29. ↑ 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.
  30. ↑ Dubrey SW, Cha K, Skinner M, LaValley M, Falk RH (July 1997). "Familial and primary (AL) cardiac amyloidosis: echocardiographically similar diseases with distinctly different clinical outcomes". Heart. 78 (1): 74–82. doi:10.1136/hrt.78.1.74. PMC 484868. PMID 9290406.
  31. ↑ Falk RH (September 2005). "Diagnosis and management of the cardiac amyloidoses". Circulation. 112 (13): 2047–60. doi:10.1161/CIRCULATIONAHA.104.489187. PMID 16186440.
  32. ↑ Klein AL, Hatle LK, Burstow DJ, Seward JB, Kyle RA, Bailey KR, Luscher TF, Gertz MA, Tajik AJ (April 1989). "Doppler characterization of left ventricular diastolic function in cardiac amyloidosis". J. Am. Coll. Cardiol. 13 (5): 1017–26. PMID 2647814.
  33. ↑ Pantazis A, Vischer AS, Perez-Tome MC, Castelletti S (March 2015). "Diagnosis and management of hypertrophic cardiomyopathy". Echo Res Pract. 2 (1): R45–53. doi:10.1530/ERP-15-0007. PMC 4676455. PMID 26693331.
  34. ↑ Eshaghian S, Kaul S, Shah PK (2007). "Cardiac amyloidosis: new insights into diagnosis and management". Rev Cardiovasc Med. 8 (4): 189–99. PMID 18192942.
  35. ↑ Estep JD, Bhimaraj A, Cordero-Reyes AM, Bruckner B, Loebe M, Torre-Amione G (2012). "Heart transplantation and end-stage cardiac amyloidosis: a review and approach to evaluation and management". Methodist Debakey Cardiovasc J. 8 (3): 8–16. PMC 3487570. PMID 23227279.


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