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Understanding the Complex World of Amyloid Disorders

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Understanding the Complex World of Amyloid Disorders: Where Does AA Amyloidosis Fit? Laura Obici, MD Amyloid Center – Biotechnology Research Laboratories University Hospital “San Matteo” Pavia, Italy Amyloid H&E Congo red staining under polarized light Courtesy of Professor CL Pirani. Electron microscopy showing 7.5–10 nm rigid, nonbranching amyloid fibrils Merlini G, Bellotti V. N Engl J Med. 2003;349:583-596. Amyloid Structural Features Congo red Courtesy of Professor Merlini. Atomic Force Microscopy of Amyloid Fibrils 600 400 200 0 200 400 600 0 nm Merlini G, Bellotti V. N Engl J Med. 2003;349:583-596. Relini A. et al, BBA 2004;1680:33-41. Merlini G, Bellotti V. N Engl J Med. 2003;349:583-596. Merlini G, Bellotti V. N Engl J Med. 2003;349:583-596. Amyloidoses Are Protein Misfolding Diseases Modified from Dobson C. Nature. 2003;426:884-890 Point Mutations Destabilize Lysozyme and Influence Amyloidogenicity T70N D67H 0.8 1.2 1 F57I W64R I56T Fraction Unfolded 0.6 0.4 0.2 0 -0.2 0 I56T T70N WT D67H 1 2 3 GdnHCl (M) 4 5 6 5 natural variants have been isolated: I56T, F57I, W64R, D67H, and T70N Esposito G, et al. J Biol Chem. 2003;278:25910-25918. b2 Microglobulin in Dialysis-related Amyloidosis Dialysis-related amyloidosis requires an increased concentration of free b2-microglobulin Proteolytic Remodeling Makes Proteins Amyloidogenic 100 (% b-aggregation per residue) 80 60 40 20 0 -20 0 5 10 15 20 25 30 35 40 45 Amino Acid Sequence Ab42 has a significantly higher aggregation propensity compared to Ab40 Nussbaum, RL, Ellis CE. N Engl J Med. 2003;348:1356-13564. Fernandez-Escammilla. A Nature Biotechnology. 2004;22:1302-1306. TANGO Score Fibrillogenesis Is a Nucleation-Dependent Process Merlini G, Bellotti V. N Engl J Med. 2003;349:583-596. Merlini G, Bellotti V. N Engl J Med. 2003;349:583-596. SAP Protects Amyloid Fibrils From Proteolysis B AAf + pronase AAf + 50 mg/l SAP + pronase AAf + 50 mg/l SAP + 7 nM MObDG + pronase 14 16 18 20 22 24 26 %125I released Emsley J, et al. Nature. 1994;367:338-345. Tennent GA, et al. PNAS. 1995;92:4299-4303 GAGs May Promote Amyloid Deposition • Heparan sulfate (HS) is a universal component of amyloid • HS can increase the b-sheet content of murine SAA1.1 and Ab • HS co-deposits both temporally and spatially with AA fibrils in spleen • Binding sites for HS have been identified for SAA, Ab, b2 microglobulin, immunoglobulin light chains • GAGs mimetics inhibit amyloid fibril formation Elimova E, et al. FASEB Journal. 2004;18:1749-1751. Conditions Associated With AA Amyloidosis Chronic Inflammatory Diseases Rheumatoid arthritis Psoriatic arthritis Chronic juvenile arthritis Ankylosing spondylitis Behcet’s syndrome Reiter’s syndrome Adult Still's disease Inflammatory bowel disease Hereditary periodic fevers Chronic Infections Tuberculosis Osteomyelitis Bronchiectasis Leprosy Pyelonephritis Decubitus ulcers Whipple’s disease Acne conglobata Neoplasia Hepatoma Renal carcinoma Castleman's disease Hodgkin's disease Adult hairy cell leukemia Waldenström's disease Common variable immunodeficiency Hypo/agammaglobulinemia Cystic fibrosis Hereditary Periodic Fevers FMF mode of inheritance age at onset length of the acess abdominal pain musculoskeletal chest pain rash recessive <20 years 1-4 days very common (serositis) monoarthritis pleuritis, often unilateral rare (<5%) crysipelaslike on lower limbs pericarditis, scrotal attacks, splenomegaly recessive childhood 3-7 days very common athralgias unusual very common (>90%) or several types: maculopapular, papular headache cervical lymph nodes hepatosplenomegaly HIDS variable often more than 1 up to several weeks common myalgias yes common crysipelas-like including upper limbs orbital edema TRAPS dominant M-W_FCAS/CINCA dominant childhood neonatal variable rare arthritis/destruction no urticaria/crythema other signs deadness-cold sensitivity/dysmorphy papillitis amyloids treatment chromosomal locus gene Protein yes colchicine 16p13.3 MEFV Ma renostrin/pyrin yes none effective TNF inhibitors? 12q44 MVK Mevalonate yes Steroids TNF inhibitors? 12p13 TNFRSFIA Type 1 TNF receptor (55p) yes Steroids interleukin-1 inhibitor? 1q44 CIASI cryopyrin Grateau G. Rheumatology (Oxford). 2004;43:410-415. Serum Amyloid A Is a Polymorphic Protein SAA1 Type I acute phase reactants SAA2 SAAP3 not expressed in humans SAA 4 constitutive SAA1 SAA1.1 SAA1.2 SAA1.3 SAA1.4 SAA1.5 In mice only SAA1.1 is deposited as AA-amyloid In human SAA genotype may influence susceptibility to AA Röcken C, Shakespeare. Virchows Arch. 2002;440:111-22. Husby G, et al. Amyloid. 1994;1:119-147. Yamada T. Clin Chem Lab Med. 1999;37:381-388. Sipe J. Amyloid. 2000;7:10-12. AA Amyloidogenesis Tissue injury, infections IL-1, IL-6, TNF- SAA1 (>70%) and SAA2 Plasma concentration changes from HDL-SAA 3–10 mg/L  100–1000 mg/L Specific receptors on macrophages (spleen, liver, kidney) SAA released from HDL AA fibrils Modified from Röcken C, Shakespeare A. Virchows Arch. 2002;440:111-122. Presenting Clinical Features in AA Amyloidosis Feature Proteinuria/renal insufficiency Diarrhea/obstipation/malabsorption Goiter Neuropathy/carpal tunnel syndrome Hepatomegaly Lymphadenopathy Cardiac % 91 22 9 3 5 2 1-2 Modified from Gertz, Kyle. Medicine. 1991;70:246. AL Amyloidosis IF anti l Kidney (74%) Heart (58%) Bone marrow plasma cell clone synthesizing amyloidogenic light chain No of organs involved: 1 (31%) >1 (69%) Liver (28%) GI (8%) Updated and adapted from N Engl J Med. 2003;349:583-596. Diagnosis Should Not Rely Only on Clinical Grounds • 60-year old woman • Nephrotic syndrome and slowly progressing renal failure over the past 4 yrs • Renal biopsy: amyloidosis • Proteinuria (11.8 g/24 h) • Serum creatinine 2.87 mg/dL • Serum high resolution IF: IgGk • SAA 71.1 mg/L (r.r.: <6.4) • IL-6 80 pg/mL (r.r. <3.12) • No known inflammatory diseases • DNA analysis for familial and hered. periodic fever s.: negative • June 2003, progressive renal failure (serum creatinine 2.3 mg/dL) U S IF anti-k IF anti-g U S U S Plasma-cell-Type Castleman’s disease with IL-6 release and increased SAA synthesis Plasma-cell-type Castleman’s disease (H & E) Amyloid in the lymph node, green birefringence in polarized light University of Pavia and University Hospital San Matteo Biotechnology Research Laboratories Giampaolo Merlini Vittorio Bellotti Vittorio Perfetti Laura Obici Giovanni Palladini Monica Stoppini Irene Zorzoli Palma Mangione Sabrina Marciano Sofia Giorgetti Alessia Andreola Simona Casarini Simona Donadei Milena Quaglia Francesca Lavatelli Valentina Navazza Sara Marini Alberto Bovera

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