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Revision as of 15:09, 12 November 2019

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

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 "amyloid" as a 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 microscopy, explained the presence of non-branching fibrils with indeterminate length and variable width.^[2]^[1]

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:^[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 different genes may lead to misfolding protein product.

Genetics

Familial ATTR amyloidosis is transmitted in autosomal dominant pattern but it can have a heterogeneous nature of presentation.^[12]^[13]^[14]

Genes involved in the pathogenesis of Familial ATTR amyloidosis include:^[4]^[5]^[15]
- Transthyretin amyloidosis (ATTR)^[16]^[17]^[18]
  - 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)^[19]
  - 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)^[20]^[21]
  - 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)^[22]
  - 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)^[23]^[24]
  - Cystatin C is a serine protease inhibitor.
  - Leu68Gln mutation in its gene leads to cystatin C amyloidosis.
- Fibrinogen Aa-chain amyloidosis (A Fib)^[25]
  - 4 different mutations including Arg554Leu, Glu526Val, 4904delG, and 4897delT has been found to be associated with amyloidosis.
- Apolipoprotein AII amyloidosis (A ApoAII)^[26]
  - 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.

Causes

Common cause of Apolipoprotein AI amyloidosis is genetic mutation.^[22]^[4]^[5]^[27]

Differentiating Apolipoprotein AI amyloidosis from Other Diseases

Epidemiology and Demographics

Risk Factors

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].

OR

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

OR

Common risk factors in the development of [disease name] may be occupational, environmental, genetic, and viral.

Screening

There is insufficient evidence to recommend routine screening for [disease/malignancy].

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

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

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

The diagnosis of [disease name] is based on the [definition name] definition, which includes [criterion 1], [criterion 2], and [criterion 3].

OR

There are no established criteria for the diagnosis of [disease name].

History and Symptoms

The majority of patients with [disease name] are asymptomatic.

OR

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].

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].

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

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

[Test] is usually normal among patients with [disease name].

OR

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

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

OR

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

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

OR

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

There are no echocardiography/ultrasound findings associated with [disease name].

OR

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].

OR

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

There are no CT scan findings associated with [disease name].

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

There are no MRI findings associated with [disease name].

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

There are no other imaging findings associated with [disease name].

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

There are no other diagnostic studies associated with [disease name].

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

Medical Therapy

There is no treatment for [disease name]; the mainstay of therapy is supportive care.

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

Surgical intervention is not recommended for the management of [disease name].

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

There are no established measures for the primary prevention of [disease name].

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

There are no established measures for the secondary prevention of [disease name].

OR

Effective measures for the secondary prevention of [disease name] include [strategy 1], [strategy 2], and [strategy 3].

References

↑ ^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.
↑ ^4.0 ^4.1 ^4.2 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.
↑ ^5.0 ^5.1 ^5.2 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.
↑ Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.
↑ 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.
↑ 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.
↑ Tan SY, Pepys MB (November 1994). "Amyloidosis". Histopathology. 25 (5): 403–14. doi:10.1111/j.1365-2559.1994.tb00001.x. PMID 7868080.
↑ 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.
↑ 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.
↑ Hund E, Linke RP, Willig F, Grau A (February 2001). "Transthyretin-associated neuropathic amyloidosis. Pathogenesis and treatment". Neurology. 56 (4): 431–5. doi:10.1212/wnl.56.4.431. PMID 11261421.
↑ Gertz MA (June 2017). "Hereditary ATTR amyloidosis: burden of illness and diagnostic challenges". Am J Manag Care. 23 (7 Suppl): S107–S112. PMID 28978215.
↑ Invalid <ref> tag; no text was provided for refs named pmid116772762
↑ Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.
↑ Robbins J (1976). "Thyroxine-binding proteins". Prog. Clin. Biol. Res. 5: 331–55. PMID 61594.
↑ Westermark P, Sletten K, Johansson B, Cornwell GG (April 1990). "Fibril in senile systemic amyloidosis is derived from normal transthyretin". Proc. Natl. Acad. Sci. U.S.A. 87 (7): 2843–5. doi:10.1073/pnas.87.7.2843. PMC 53787. PMID 2320592.
↑ Holmgren G, Steen L, Ekstedt J, Groth CG, Ericzon BG, Eriksson S, Andersen O, Karlberg I, Nordén G, Nakazato M (September 1991). "Biochemical effect of liver transplantation in two Swedish patients with familial amyloidotic polyneuropathy (FAP-met30)". Clin. Genet. 40 (3): 242–6. doi:10.1111/j.1399-0004.1991.tb03085.x. PMID 1685359.
↑ 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.
↑ Maury CP, Kere J, Tolvanen R, de la Chapelle A (December 1990). "Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene". FEBS Lett. 276 (1–2): 75–7. doi:10.1016/0014-5793(90)80510-p. PMID 2176164.
↑ de la Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J (October 1992). "Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187". Nat. Genet. 2 (2): 157–60. doi:10.1038/ng1092-157. PMID 1338910.
↑ ^22.0 ^22.1 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.
↑ Gudmundsson G, Hallgrímsson J, Jónasson TA, Bjarnason O (1972). "Hereditary cerebral haemorrhage with amyloidosis". Brain. 95 (2): 387–404. doi:10.1093/brain/95.2.387. PMID 4655034.
↑ Ghiso J, Pons-Estel B, Frangione B (April 1986). "Hereditary cerebral amyloid angiopathy: the amyloid fibrils contain a protein which is a variant of cystatin C, an inhibitor of lysosomal cysteine proteases". Biochem. Biophys. Res. Commun. 136 (2): 548–54. doi:10.1016/0006-291x(86)90475-4. PMID 3707586.
↑ Uemichi T, Liepnieks JJ, Benson MD (February 1994). "Hereditary renal amyloidosis with a novel variant fibrinogen". J. Clin. Invest. 93 (2): 731–6. doi:10.1172/JCI117027. PMC 293912. PMID 8113408.
↑ Benson MD, Liepnieks JJ, Yazaki M, Yamashita T, Hamidi Asl K, Guenther B, Kluve-Beckerman B (March 2001). "A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene". Genomics. 72 (3): 272–7. doi:10.1006/geno.2000.6499. PMID 11401442.
↑ Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.

Template:WikiDoc Sources

[pmid218384133-1] 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.

[pmid10940217-2] 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.

[pmid11677276-3] Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.

[Benson2003-4] 4.0 ^4.1 ^4.2 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.

[Benson20032-5] 5.0 ^5.1 ^5.2 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.

[pmid26719234-7] 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.

[pmid8202534-8] 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.

[pmid7868080-9] Tan SY, Pepys MB (November 1994). "Amyloidosis". Histopathology. 25 (5): 403–14. doi:10.1111/j.1365-2559.1994.tb00001.x. PMID 7868080.

[pmid9256275-10] 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.

[pmid267192342-11] 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.

[pmid11261421-12] Hund E, Linke RP, Willig F, Grau A (February 2001). "Transthyretin-associated neuropathic amyloidosis. Pathogenesis and treatment". Neurology. 56 (4): 431–5. doi:10.1212/wnl.56.4.431. PMID 11261421.

[pmid28978215-13] Gertz MA (June 2017). "Hereditary ATTR amyloidosis: burden of illness and diagnostic challenges". Am J Manag Care. 23 (7 Suppl): S107–S112. PMID 28978215.

[pmid116772762-14] Invalid <ref> tag; no text was provided for refs named pmid116772762

[15] Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.

[pmid61594-16] Robbins J (1976). "Thyroxine-binding proteins". Prog. Clin. Biol. Res. 5: 331–55. PMID 61594.

[pmid2320592-17] Westermark P, Sletten K, Johansson B, Cornwell GG (April 1990). "Fibril in senile systemic amyloidosis is derived from normal transthyretin". Proc. Natl. Acad. Sci. U.S.A. 87 (7): 2843–5. doi:10.1073/pnas.87.7.2843. PMC 53787. PMID 2320592.

[pmid1685359-18] Holmgren G, Steen L, Ekstedt J, Groth CG, Ericzon BG, Eriksson S, Andersen O, Karlberg I, Nordén G, Nakazato M (September 1991). "Biochemical effect of liver transplantation in two Swedish patients with familial amyloidotic polyneuropathy (FAP-met30)". Clin. Genet. 40 (3): 242–6. doi:10.1111/j.1399-0004.1991.tb03085.x. PMID 1685359.

[pmid9356442-19] 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.

[pmid2176164-20] Maury CP, Kere J, Tolvanen R, de la Chapelle A (December 1990). "Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene". FEBS Lett. 276 (1–2): 75–7. doi:10.1016/0014-5793(90)80510-p. PMID 2176164.

[pmid1338910-21] Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J (October 1992). "Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187". Nat. Genet. 2 (2): 157–60. doi:10.1038/ng1092-157. PMID 1338910.

[pmid8464497-22] 22.0 ^22.1 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.

[pmid4655034-23] Gudmundsson G, Hallgrímsson J, Jónasson TA, Bjarnason O (1972). "Hereditary cerebral haemorrhage with amyloidosis". Brain. 95 (2): 387–404. doi:10.1093/brain/95.2.387. PMID 4655034.

[pmid3707586-24] Ghiso J, Pons-Estel B, Frangione B (April 1986). "Hereditary cerebral amyloid angiopathy: the amyloid fibrils contain a protein which is a variant of cystatin C, an inhibitor of lysosomal cysteine proteases". Biochem. Biophys. Res. Commun. 136 (2): 548–54. doi:10.1016/0006-291x(86)90475-4. PMID 3707586.

[pmid8113408-25] Uemichi T, Liepnieks JJ, Benson MD (February 1994). "Hereditary renal amyloidosis with a novel variant fibrinogen". J. Clin. Invest. 93 (2): 731–6. doi:10.1172/JCI117027. PMC 293912. PMID 8113408.

[pmid11401442-26] Benson MD, Liepnieks JJ, Yazaki M, Yamashita T, Hamidi Asl K, Guenther B, Kluve-Beckerman B (March 2001). "A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene". Genomics. 72 (3): 272–7. doi:10.1006/geno.2000.6499. PMID 11401442.

[27] Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.

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@@ Line 9: / Line 9: @@
 ==Historical Perspective==
-<br />
+* In 1639, Nicolaus Fontanus [[Autopsy|autopsied]] a young man who had [[ascites]], [[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 1854, Rudolph Virchow introduced the term "amyloid" as a [[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 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 1959, Cohen and Calkins used ultrathin sections of amyloidotic [[Tissue (biology)|tissues]] and assessed by [[electron microscopy]], explained the presence of non-branching 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==
-<br />
+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>
+* [[Transthyretin|Transthyretin (TTR)]]
+* [[Apolipoprotein AI]]
+* Apolipoprotein AII
+* [[Fibrinogen A alpha-chain associated amyloidosis|Fibrinogen Aa]]
+* [[Lysozyme]]
+* [[Gelsolin]]
+* [[Cystatin C]]
-==Pathophysiology==
+{{familytree/start}}
-<br />
+{{familytree | | | | | | | | | | | | | | A01 | | | | | | | | | | | | A01=genes involved in familial amyloidosis}}
+{{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/end}}
-==Causes==
-<br />
-==Differentiating Apolipoprotein AI amyloidosis from Other Diseases==
-<br />
-==Epidemiology and Demographics==
+==Pathophysiology==
-The incidence/prevalence of [disease name] is approximately [number range] per 100,000 individuals worldwide.
+===Pathogenesis===
+*It is understood that amyloidosis is the result of deposition of [[Amyloid]].<ref name="pmid26719234">{{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 is an abnormal insoluble [[extracellular]] [[protein]] which may cause organic dysfunction and a wide variety of clinical syndromes.
+*These abnormal [[Amyloid|amyloids]] are derived from misfolding and aggregation of normally soluble [[Protein|proteins]].
+*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>
+*Genetic mutations in different genes may lead to misfolding protein product.
-OR
+==Genetics==
-In [year], the incidence/prevalence of [disease name] was estimated to be [number range] cases per 100,000 individuals worldwide.
+* 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" />
-OR
+* 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.
-In [year], the incidence of [disease name] is approximately [number range] per 100,000 individuals with a case-fatality rate of [number range]%.
+==Causes==
+Common cause of Apolipoprotein AI amyloidosis is genetic mutation.<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><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>
+==Differentiating Apolipoprotein AI amyloidosis from Other Diseases==
-Patients of all age groups may develop [disease name].
-OR
+==Epidemiology and Demographics==
-The incidence of [disease name] increases with age; the median age at diagnosis is [#] years.
-OR
-[Disease name] commonly affects individuals younger than/older than [number of years] years of age.
-OR
-[Chronic disease name] is usually first diagnosed among [age group].
-OR
-[Acute disease name] commonly affects [age group].
-There is no racial predilection to [disease name].
-OR
-[Disease name] usually affects individuals of the [race 1] race. [Race 2] individuals are less likely to develop [disease name].
-[Disease name] affects men and women equally.
-OR
-[Gender 1] are more commonly affected by [disease name] than [gender 2]. The [gender 1] to [gender 2] ratio is approximately [number > 1] to 1.
-The majority of [disease name] cases are reported in [geographical region].
-OR
-[Disease name] is a common/rare disease that tends to affect [patient population 1] and [patient population 2].
 ==Risk Factors==