Apolipoprotein AI amyloidosis
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]
- Transthyretin (TTR)
- Apolipoprotein AI
- Apolipoprotein AII
- Fibrinogen Aa
- Lysozyme
- Gelsolin
- Cystatin C
| 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
Incidence
Mortality rate
- The mortality rate of systemic amyloidosis is approximately 100 per 100,000 deaths in developed countries.[16]
Age
- In familial amyloidosis, the mean age of presentation is:[17][18][12][13][19][20][21][22]
- Transthyretin (TTR): After 50 years of age
- The age of onset in TTR Val30Met variant of the disease in northern Portugal is in the early 30s
- Apolipoprotein AI: Third decade and older
- Apolipoprotein AII: Early adulthood
- Fibrinogen Aa: Fourth to fifth decade
- Lysozyme: Third to fourth decade
- Gelsolin: Late adulthood
- Cystatin C: Third to fourth decade
- Transthyretin (TTR): After 50 years of age
Race
- Hereditary amyloidosis subtypes include a substitution of an amino acid that is detected in approximately 4% of the african american population.[3]
Gender
- Men are more commonly affected by amyloidosis than women.[23]
Region
- Transthyretin-related hereditary amyloidosis is endemic in Portuguese locations Póvoa de Varzim and Vila do Conde (Caxinas), with more than 1000 affected people, coming from about 500 families, where 70% of the people develop the illness.[24][25][26][27][28][29][30][31][32][33][34]
- In northern Sweden, more specifically Piteå, Skellefteå and Umeå, 1.5% of the population has the mutated gene.
- There are many other populations in the world who exhibit the illness after having developed it independently.
- The majority of gelsolin related amyloidosis cases are reported in the United States, Japan, Portugal, England, Germany, Spain, France, Brazil, Sewden, Denmark, the Czech Republic, and Iran.
Risk Factors
- Common risk factors in the development of familial amyloidosis include:[23][3][17]
- Older age
- Male gender
- African american race
- Positive family history
Screening
There is insufficient evidence to recommend routine screening for 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 familial amyloidosis.[35]
- 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:
- Transthyretin (TTR)
- Apolipoprotein AI
- Apolipoprotein AII
- Fibrinogen Aa
- Biopsy of the affected organ is recommended for patients with limited organ involvement.[36]
- Biopsy from unaffected organs is more sensitive in patients with multi-organ involvement.
Diagnostic results
The following finding on performing tissue biopsy is confirmatory for familial amyloidosis:[37][38]
- Apple green birefringence of the tissue sample under polarized light with Congo red stain.
Sequence of Diagnostic Studies
The various investigations must be performed in the following order:
- History
- Although all the familial amyloidosis types are autosomal dominant, different degree of temperance makes it difficult to diagnose the disease based on family history.
- Physical examination
- Biopsy
Name of Diagnostic Criteria
There are no established criteria for the diagnosis of familial amyloidosis.
History and Symptoms
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.
- ↑ 3.0 3.1 3.2 Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
- ↑ 4.0 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.
- ↑ 5.0 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.
- ↑ 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.
- ↑ 12.0 12.1 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.
- ↑ 13.0 13.1 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.
- ↑ Scriver, Charles (2001). The metabolic & molecular bases of inherited disease. New York: McGraw-Hill. ISBN 978-0079130358.
- ↑ Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
- ↑ Pepys MB (2006). "Amyloidosis". Annu. Rev. Med. 57: 223–41. doi:10.1146/annurev.med.57.121304.131243. PMID 16409147.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 23.0 23.1 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.
- ↑ Quock TP, Yan T, Chang E, Guthrie S, Broder MS (May 2018). "Epidemiology of AL amyloidosis: a real-world study using US claims data". Blood Adv. 2 (10): 1046–1053. doi:10.1182/bloodadvances.2018016402. PMC 5965052. PMID 29748430.
- ↑ Ardalan, M. R.; Shoja, M. M. (2007). "Reply". Nephrology Dialysis Transplantation. 23 (3): 1071–1072. doi:10.1093/ndt/gfm586. ISSN 0931-0509.
- ↑ Suhr, Ole B (2019). "Commentary to Isabel Conceição et al. early diagnosis through targeted follow-up of identified carriers of TTR gene mutations". Amyloid. 26 (1): 1–2. doi:10.1080/13506129.2018.1558051. ISSN 1350-6129.
- ↑ Pihlamaa, Tiia; Rautio, Jorma; Kiuru-Enari, Sari; Suominen, Sinikka (2011). "Gelsolin Amyloidosis as a Cause of Early Aging and Progressive Bilateral Facial Paralysis". Plastic and Reconstructive Surgery. 127 (6): 2342–2351. doi:10.1097/PRS.0b013e318213a0a2. ISSN 0032-1052.
- ↑ Lachmann, Helen J.; Goodman, Hugh J.B.; Gilbertson, Janet A.; Gallimore, J. Ruth; Sabin, Caroline A.; Gillmore, Julian D.; Hawkins, Philip N. (2007). "Natural History and Outcome in Systemic AA Amyloidosis". New England Journal of Medicine. 356 (23): 2361–2371. doi:10.1056/NEJMoa070265. ISSN 0028-4793.
- ↑ Adam MP, Ardinger HH, Pagon RA, Wallace SE, Bean LJH, Stephens K; et al. (1993). "GeneReviews®". PMID 20301373.
- ↑ Ikeda, Etsuko; Yagi, Kiyohito; Kojima, Midori; Yagyuu, Takahiro; Ohshima, Akira; Sobajima, Satoshi; Tadokoro, Mika; Katsube, Yoshihiro; Isoda, Katsuhiro; Kondoh, Masuo; Kawase, Masaya; Go, Masahiro J; Adachi, Hisashi; Yokota, Yukiharu; Kirita, Tadaaki; Ohgushi, Hajime (2008). "Multipotent cells from the human third molar: feasibility of cell-based therapy for liver disease". Differentiation. 76 (5): 495–505. doi:10.1111/j.1432-0436.2007.00245.x. ISSN 0301-4681.
- ↑ Morley, S. K.; Freeman, M. P.; Tanskanen, E. I. (2007). "A comparison of the probability distribution of observed substorm magnitude with that predicted by a minimal substorm model". Annales Geophysicae. 25 (11): 2427–2437. doi:10.5194/angeo-25-2427-2007. ISSN 1432-0576.
- ↑ Contégal F, Bidot S, Thauvin C, Lévèque L, Soichot P, Gras P; et al. (2006). "[Finnish amyloid polyneuropathy in a French patient]". Rev Neurol (Paris). 162 (10): 997–1001. PMID 17028568.
- ↑ Makioka, Kouki; Yamazaki, Tsuneo; Fujita, Yukio; Takatama, Masamitsu; Nakazato, Yoichi; Okamoto, Koichi (2010). "Involvement of endoplasmic reticulum stress defined by activated unfolded protein response in multiple system atrophy". Journal of the Neurological Sciences. 297 (1–2): 60–65. doi:10.1016/j.jns.2010.06.019. ISSN 0022-510X.
- ↑ Planté-Bordeneuve, Violaine; Said, Gerard (2011). "Familial amyloid polyneuropathy". The Lancet Neurology. 10 (12): 1086–1097. doi:10.1016/S1474-4422(11)70246-0. ISSN 1474-4422.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.