Gelsolin related amyloidosis
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Ramyar Ghandriz MD[2]
Synonyms and keywords:Finnish type Hereditary Amyloidosis; Familial Amyloidosis of Finnish type (FAF); Gelsolin; Familial Amyloid Polyneuropathy IV; Meretoja's disease; hereditary amyloidosis; amyloid angiopathy
Overview
Gelsolin related amyloidosis is a sub group of familial amyloidosis and is also called familial amyloidosis of finnish type. it was first reported by Jouko Meretoja in 1969.It is thought that familial amyloidosis of Finnish type is caused by a monogenic mutation, which leads to misfolding of mutated gelsolin in the Golgi apparatus during cellular trafficking. Gelsolin coding area is around q32-34 of chromosome 9. Geloslin related amyloidosis is caused by a G654A or G654T mutation. These mutations cause compromising calcium ions binding to backbone of gelsolin protein.
Historical Perspective
- Gelsoline related amyloidosis was first reported by Jouko Meretoja in 1969.
- the patients studied had lattice dystrophy of the cornea and a cranial and peripheral neuropathy.[1]
Classification
- Gelsolin related amyloidosis is a sub group of familial amyloidosis and is also called familial amyloidosis of finnish type.[2]
Pathophysiology
- It is thought that familial amyloidosis of Finnish type is caused by a monogenic mutation, which leads to misfolding of mutated gelsolin in the Golgi apparatus during cellular trafficking.
- The fragments Which are cleaved are amyloidogenic themself.[3]
- The amyloid deposit is a protein product of the gelsolin gene.[4]
- Gelsolin gene is spliced to form cytoplasmic and secreted forms.[5]
- The amyloidic fractions are due to aberrant processing of secretd form, also known as plasma gelsolin.
- Gelsolin coding area is around q32-34 of chromosome 9.[6]
- One allele of mutant gene is enough for disease, it shows complete penetrence and autosomal dominant disease.
- Gelsoline related amyloidosis is a gain of toxic function mutation and disease.[7]
Causes
- Geloslin related amyloidosis is caused by a G654A or G654T mutation.
- This mutations cause compromising calcium ions binding to backbone of gelsolin protein.[8]
Differentiating Gelosline Related Amyloidosis from Other Diseases
Familial amyloidosis of finnish type (geloslin related amyloidosis) must be differentiated from other familial types by molecular analysis.[9]
- Existence of 5 KDa and 8 KDa fragments gelsolin amyloid fibril in electrophoresis.
Familial amyloidosis should be differentiated from the following systemic diseases:[10]
- Acute myocarditis
- Bechterew's Disease
- Bronchiectasis
- Carpal Tunnel Syndrome
- Collagen Vascular Disease
- Drug/toxic nephropathy
- Familial Mediterranean Fever
- Glomerulonephritis
- Hemodialysis Amyloidosis
- Interstitial lung diseases
- Leprosy
- Monoclonal gammopathies
- Multiple Myeloma
- Myocardial fibrosis
- Nephrotic Syndrome
- Osteomyelitis
- Peripheral neuropathy
- Restrictive cardiomyopathy
- Rheumatoid Arthritis
- Rheumatoid Polyarteritis
- Syphilis
- Systemic Lupus Erythematosus
- Tuberculosis
- Ulcerative colitis
- Vitamin deficiencies
Epidemiology and Demographics
- It is estimated that there is approximately 1000 carriers in Finland.
- Since the first report, many patients are seen all around the world.
- 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.[11][12][13][14][15][16][17][18][19][20]
Risk Factors
Incidence of non-hereditary gelsolin related amyloidosis is very low with the lack of established risk factors.[21]
Screening
There is insufficient evidence to recommend routine screening for gelsolin related amyloidosis.[22]
Natural History, Complications, and Prognosis
- In amyloidosis, insoluble fibrils of amyloid are deposited in the organs, causing organ dysfunction and eventually death.[23][24]
- Gelsolin related amyloidosis causes a specific kind of neuropathy, the Meretoja's syndrome.
- It is defined as lattice corneal dystrophy, and develops after the third decade of life.
- Diagnostic triad include[25] :
Diagnosis
Diagnostic Study of Choice
- Diagnostic studies for gelsolin related amyloidosis are the same as for amyloidosis.
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History and Symptoms
- Common symptoms of amyloidosis include abdominal pain, swelling, and enlarged tongue.
- Less common symptoms of amyloidosis include gastrointestinal bleeding, blood in urine, hoarseness and paresthesia.[27][28][29][30]
Physical Examination
- Physical examination findings of gelsolin related amyloidosis are the same as amyloidosis.
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Laboratory Findings
- Laboratory findings of gelsolin related amyloidosis are the same as amyloidosis.
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Electrocardiogram
- ECG findings of gelsolin related amyloidosis are the same as amyloidosis.
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X-ray
- X-ray findings of gelsolin related amyloidosis are the same as amyloidosis.
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Echocardiography or Ultrasound
- Echocardiographic findings of gelsolin related amyloidosis are the same as amyloidosis.
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CT scan
- CT scan findings of gelsolin related amyloidosis are the same as amyloidosis.
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MRI
- MRI findings of gelsolin related amyloidosis are the same as amyloidosis.
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Other Imaging Findings
- Other imaging findings of gelsolin related amyloidosis are the same as amyloidosis.
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Other Diagnostic Studies
- Other diagnostic studies of gelsolin related amyloidosis are the same as amyloidosis.
- For further information, click here.
Treatment
Medical Therapy
- Gelsolin related amyloidosis is typically discovered at an advanced stage.
- The initial treatment is aimed at preventing further organ damage and correcting the effects of organ failure.
- For a comprehensive guide on the treatment of amyloidosis, click here.
Surgery
- Cardiac transplant may need to be done for patients with cardiac amyloidosis.[31]
- Organ-specific transplant may need to be done, depending on the organ involved.[32]
Primary Prevention
There are no established measures for the primary prevention of gelsolin related amyloidosis.[33]
Secondary Prevention
There are no established measures for the secondary prevention of gelsolin related amyloidosis.[34]
References
- ↑ Meretoja J (1969). "Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms. A previously unrecognized heritable syndrome". Ann Clin Res. 1 (4): 314–24. PMID 4313418.
- ↑ Huff, Mary E; Balch, William E; Kelly, Jeffery W (2003). "Pathological and functional amyloid formation orchestrated by the secretory pathway". Current Opinion in Structural Biology. 13 (6): 674–682. doi:10.1016/j.sbi.2003.10.010. ISSN 0959-440X.
- ↑ Tanzi, Rudolph E.; Bertram, Lars (2005). "Twenty Years of the Alzheimer's Disease Amyloid Hypothesis: A Genetic Perspective". Cell. 120 (4): 545–555. doi:10.1016/j.cell.2005.02.008. ISSN 0092-8674.
- ↑ Maury, C P (1991). "Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin". Journal of Clinical Investigation. 87 (4): 1195–1199. doi:10.1172/JCI115118. ISSN 0021-9738.
- ↑ Haltia, Matti; Prelli, Frances; Ghiso, Jorge; Kiuru, Sari; Somer, Hannu; Palo, Jorma; Frangione, Blas (1990). "Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein". Biochemical and Biophysical Research Communications. 167 (3): 927–932. doi:10.1016/0006-291X(90)90612-Q. ISSN 0006-291X.
- ↑ Chen, C.-D. (2001). "Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2+ stabilization". The EMBO Journal. 20 (22): 6277–6287. doi:10.1093/emboj/20.22.6277. ISSN 1460-2075.
- ↑ Robinson, R. C.; Choe, S.; Burtnick, L. D. (2001). "The disintegration of a molecule: The role of gelsolin in FAF, familial amyloidosis (Finnish type)". Proceedings of the National Academy of Sciences. 98 (5): 2117–2118. doi:10.1073/pnas.051635098. ISSN 0027-8424.
- ↑ Kazmirski, Steven L.; Isaacson, Rivka L.; An, Chahm; Buckle, Ashley; Johnson, Christopher M.; Daggett, Valerie; Fersht, Alan R. (2002). "Loss of a metal-binding site in gelsolin leads to familial amyloidosis–Finnish type". Nature Structural Biology. 9 (2): 112–116. doi:10.1038/nsb745. ISSN 1072-8368.
- ↑ Engel, W. K.; Askanas, V. (2005). "Inclusion-body myositis: Clinical, diagnostic, and pathologic aspects". Neurology. 66 (Issue 1, Supplement 1): S20–S29. doi:10.1212/01.wnl.0000192260.33106.bb. ISSN 0028-3878.
- ↑ Ando, Yukio; Coelho, Teresa; Berk, John L; Cruz, Márcia Waddington; Ericzon, Bo-Göran; Ikeda, Shu-ichi; Lewis, W David; Obici, Laura; Planté-Bordeneuve, Violaine; Rapezzi, Claudio; Said, Gerard; Salvi, Fabrizio (2013). "Guideline of transthyretin-related hereditary amyloidosis for clinicians". Orphanet Journal of Rare Diseases. 8 (1): 31. doi:10.1186/1750-1172-8-31. ISSN 1750-1172.
- ↑ 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.
- ↑ Hammarstrom, P. (2003). "Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics". Science. 299 (5607): 713–716. doi:10.1126/science.1079589. ISSN 0036-8075.
- ↑ Shin, Susan C.; Robinson-Papp, Jessica (2012). "Amyloid Neuropathies". Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine. 79 (6): 733–748. doi:10.1002/msj.21352. ISSN 0027-2507.
- ↑ Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
- ↑ Khan MF, Falk RH (November 2001). "Amyloidosis". Postgrad Med J. 77 (913): 686–93. PMC 1742163. PMID 11677276.
- ↑ Boysen, G; Galassi, G; Kamieniecka, Z; Schlaeger, J; Trojaborg, W (1979). "Familial amyloidosis with cranial neuropathy and corneal lattice dystrophy". Journal of Neurology, Neurosurgery & Psychiatry. 42 (11): 1020–1030. doi:10.1136/jnnp.42.11.1020. ISSN 0022-3050.
- ↑ 26.0 26.1 Huerva V, Soldevila J, Matias-Guiu X (2014). "Recurrent Amyloid Material in Grafts Used in Patients with Lattice Corneal Dystrophy 2 (Meretoja's Syndrome)". Med Hypothesis Discov Innov Ophthalmol. 3 (3): 99–100. PMC 4348492. PMID 25741526.
- ↑ 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.
- ↑ Baker KR, Rice L (2012). "The amyloidoses: clinical features, diagnosis and treatment". Methodist Debakey Cardiovasc J. 8 (3): 3–7. PMC 3487569. PMID 23227278.
- ↑ Lim AY, Lee JH, Jung KS, Gwag HB, Kim DH, Kim SJ, Lee GY, Kim JS, Kim HJ, Lee SY, Lee JE, Jeon ES, Kim K (July 2015). "Clinical features and outcomes of systemic amyloidosis with gastrointestinal involvement: a single-center experience". Korean J. Intern. Med. 30 (4): 496–505. doi:10.3904/kjim.2015.30.4.496. PMC 4497337. PMID 26161016.
- ↑ 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.
- ↑ 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.
- ↑ Kennedy TL, Patel NM (June 2000). "Surgical management of localized amyloidosis". Laryngoscope. 110 (6): 918–23. doi:10.1097/00005537-200006000-00005. PMID 10852504.
- ↑ Bonì, Francesco; Milani, Mario; Porcari, Riccardo; Barbiroli, Alberto; Ricagno, Stefano; de Rosa, Matteo (2016). "Molecular basis of a novel renal amyloidosis due to N184K gelsolin variant". Scientific Reports. 6 (1). doi:10.1038/srep33463. ISSN 2045-2322.
- ↑ Solomon, James P.; Bourgault, Steve; Powers, Evan T.; Kelly, Jeffery W. (2011). "Heparin Binds 8 kDa Gelsolin Cross-β-Sheet Oligomers and Accelerates Amyloidogenesis by Hastening Fibril Extension". Biochemistry. 50 (13): 2486–2498. doi:10.1021/bi101905n. ISSN 0006-2960.