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Berlin Brandenburg

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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 01 October 2013, Vol.110(40), pp.16115-20
    Description: Systemic amyloid A (AA) amyloidosis is a serious complication of chronic inflammation. Serum AA protein (SAA), an acute phase plasma protein, is deposited extracellularly as insoluble amyloid fibrils that damage tissue structure and function. Clinical AA amyloidosis is typically preceded by many years of active inflammation before presenting, most commonly with renal involvement. Using dose-dependent, doxycycline-inducible transgenic expression of SAA in mice, we show that AA amyloid deposition can occur independently of inflammation and that the time before amyloid deposition is determined by the circulating SAA concentration. High level SAA expression induced amyloidosis in all mice after a short, slightly variable delay. SAA was rapidly incorporated into amyloid, acutely reducing circulating SAA concentrations by up to 90%. Prolonged modest SAA overexpression occasionally produced amyloidosis after long delays and primed most mice for explosive amyloidosis when SAA production subsequently increased. Endogenous priming and bulk amyloid deposition are thus separable events, each sensitive to plasma SAA concentration. Amyloid deposits slowly regressed with restoration of normal SAA production after doxycycline withdrawal. Reinduction of SAA overproduction revealed that, following amyloid regression, all mice were primed, especially for rapid glomerular amyloid deposition leading to renal failure, closely resembling the rapid onset of renal failure in clinical AA amyloidosis following acute exacerbation of inflammation. Clinical AA amyloidosis rarely involves the heart, but amyloidotic SAA transgenic mice consistently had minor cardiac amyloid deposits, enabling us to extend to the heart the demonstrable efficacy of our unique antibody therapy for elimination of visceral amyloid.
    Keywords: 3rs ; Disease Model ; Amyloid -- Metabolism ; Amyloidosis -- Physiopathology ; Inflammation -- Complications ; Serum Amyloid A Protein -- Metabolism
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 2
    Article
    Article
    BMJ Publishing Group Ltd and British Cardiovascular Society
    Language: English
    In: Heart, 11 November 2012, Vol.98(21), p.1546
    Description: Cardiac amyloidosis of transthyretin fibril protein (ATTR) type is an infiltrative cardiomyopathy characterised by ventricular wall thickening and diastolic heart failure. Increased access to cardiovascular magnetic resonance imaging has led to a marked increase in referrals to our centre of Caucasian patients with wild-type ATTR (senile systemic) amyloidosis and Afro-Caribbean patients with the hereditary ATTR V122I type. Both subtypes present predominantly as isolated cardiomyopathy. The differential diagnosis includes cardiac amyloid light-chain (AL) amyloidosis, which has a poorer prognosis and can be amenable to chemotherapy. We review here the clinical features of cardiac ATTR amyloidosis and describe the diagnostic tests to determine ATTR type. Correct diagnosis is ever more crucial given that several novel therapies for ATTR amyloidosis are on the near horizon.
    Keywords: Cardiac Amyloidosis ; Cardiovascular Mri ; Cardiomyopathy ; Valvular Disease ; Cardiac Function ; Cardiac Remodelling ; Interventional Cardiology ; Non-Coronary Intervention ; Percutaneous Valve Therapy ; Heart Failure ; Systolic Heart Failure ; Diastolic Dysfunction ; Myocardial Disease ; Cardiomyopathy Restrictive
    ISSN: 1355-6037
    ISSN: 13556037
    E-ISSN: 1468-201X
    E-ISSN: 1468201X
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  • 3
    Language: English
    In: The Lancet, 25 June 2016, Vol.387(10038), pp.2641-2654
    Description: Tissue deposition of protein fibrils causes a group of rare diseases called systemic amyloidoses. This Seminar focuses on changes in their epidemiology, the current approach to diagnosis, and advances in treatment. Systemic light chain (AL) amyloidosis is the most common of these conditions, but wild-type transthyretin cardiac amyloidosis (ATTRwt) is increasingly being diagnosed. Typing of amyloid fibrils, a critical determinant of therapy, has improved with the wide availability of laser capture and mass spectrometry from fixed histological tissue sections. Specific and accurate evaluation of cardiac amyloidosis is now possible using cardiac magnetic resonance imaging and cardiac repurposing of bone scintigraphy tracers. Survival in AL amyloidosis has improved markedly as novel chemotherapy agents have become available, but challenges remain in advanced disease. Early diagnosis, a key to better outcomes, still remains elusive. Broadening the amyloid-specific therapeutic landscape to include RNA inhibitors, fibril formation stabilisers and inhibitors, and immunotherapeutic targeting of amyloid deposits holds promise to transform outcomes in systemic amyloidoses.
    Keywords: Medicine
    ISSN: 0140-6736
    E-ISSN: 1474-547X
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  • 4
    Language: English
    In: Journal of the American College of Cardiology, 27 March 2012, Vol.59(13), pp.E993-E993
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/S0735-1097(12)60994-2 Byline: Jason Dungu, Mark S. O'Donnell, Philip N. Hawkins, Lisa J. Anderson Author Affiliation: St George's University of London, London, United Kingdom, UK National Amyloidosis Centre, London, United Kingdom Article Note: (footnote) ACC Moderated Poster Contributions McCormick Place South, Hall A Monday, March 26, 2012, 11:00 a.m.-Noon Session Title: What's New in Cardiac Amyloidosis and Dilated Cardiomyopathy Abstract Category: 14. Heart Failure: Clinical Presentation Number: 1218-250
    Keywords: Medicine
    ISSN: 0735-1097
    E-ISSN: 1558-3597
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  • 5
    Language: English
    In: Arthritis and rheumatism, February 2011, Vol.63(2), pp.314-24
    Keywords: Autoimmune Diseases -- Immunology ; Autoimmunity -- Immunology ; Immunity, Innate -- Immunology ; Interleukin-1beta -- Immunology
    E-ISSN: 1529-0131
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  • 6
    In: Kidney International, 2014
    Description: Amyloidosis results from protein misfolding, and ongoing amyloid deposition can ultimately lead to organ failure and death. Historically, this is a group of diseases with limited treatment options and frequently poor prognosis. However, there are now 'targeted' therapeutics emerging in the form of stabilizers of the precursor protein, inhibitors of fibrillogenesis, fibril disruptors, and blockers of protein translation, transcription, and immunotherapy. We review many of these approaches that are currently being assessed in clinical trials.
    Keywords: Molecular Targeted Therapy ; Amyloidosis -- Drug Therapy ; Prealbumin -- Metabolism;
    ISSN: 0085-2538
    E-ISSN: 15231755
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  • 7
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 28 January 2014, Vol.111(4), pp.1539-44
    Description: The Ser52Pro variant of transthyretin (TTR) produces aggressive, highly penetrant, autosomal-dominant systemic amyloidosis in persons heterozygous for the causative mutation. Together with a minor quantity of full-length wild-type and variant TTR, the main component of the ex vivo fibrils was the residue 49-127 fragment of the TTR variant, the portion of the TTR sequence that previously has been reported to be the principal constituent of type A, cardiac amyloid fibrils formed from wild-type TTR and other TTR variants [Bergstrom J, et al. (2005) J Pathol 206(2):224-232]. This specific truncation of Ser52Pro TTR was generated readily in vitro by limited proteolysis. In physiological conditions and under agitation the residue 49-127 proteolytic fragment rapidly and completely self-aggregates into typical amyloid fibrils. The remarkable susceptibility to such cleavage is likely caused by localized destabilization of the β-turn linking strands C and D caused by loss of the wild-type hydrogen-bonding network between the side chains of residues Ser52, Glu54, Ser50, and a water molecule, as revealed by the high-resolution crystallographic structure of Ser52Pro TTR. We thus provide a structural basis for the recently hypothesized, crucial pathogenic role of proteolytic cleavage in TTR amyloid fibrillogenesis. Binding of the natural ligands thyroxine or retinol-binding protein (RBP) by Ser52Pro variant TTR stabilizes the native tetrameric assembly, but neither protected the variant from proteolysis. However, binding of RBP, but not thyroxine, inhibited subsequent fibrillogenesis.
    Keywords: Misfolding ; Protein Aggregation ; Amyloid -- Metabolism ; Prealbumin -- Metabolism ; Proline -- Metabolism ; Serine -- Metabolism
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 8
    Language: English
    In: Journal of the American College of Cardiology, 27 March 2012, Vol.59(13), pp.E1574-E1574
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/S0735-1097(12)61575-7 Byline: Jason Dungu, Oswaldo Valencia, Aigul Baltabaeva, Tarek FT Antonios, Philip N. Hawkins, Lisa J. Anderson Author Affiliation: St George's University of London, London, United Kingdom, UK National Amyloidosis Centre, London, United Kingdom Article Note: (footnote) ACC Moderated Poster Contributions McCormick Place South, Hall A Sunday, March 25, 2012, 11:00 a.m.-Noon Session Title: Pericardial/Myocardial Disease IV Abstract Category: 12. Pericardial/Myocardial Disease Presentation Number: 1126-119
    Keywords: Medicine
    ISSN: 0735-1097
    E-ISSN: 1558-3597
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  • 9
    Language: English
    In: Journal of the American College of Cardiology, 09 October 2018, Vol.72(15), pp.1881-1881
    Keywords: Medicine
    ISSN: 0735-1097
    E-ISSN: 1558-3597
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  • 10
    Article
    Article
    Language: English
    In: Orphanet Journal of Rare Diseases, 2015, Vol.10(Suppl 1), p.I10
    Keywords: Medicine;
    ISSN: 1750-1172
    Source: CrossRef
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