Epidemiologic and Survival Trends in Amyloidosis, 1987–2019

Abstract

To the Editor: Amyloidosis is a group of rare disorders caused by deposition of misfolded proteins as insoluble fibrils, which leads to progressive multiorgan failure and death. 1 The past 30 years have seen remarkable advances in diagnostic imaging, more accurate identification of fibrils, and (in recent years) the first approved treatments. 2,3 We report here data on 11,006 patients who received a diagnosis of amyloidosis during the period from 1987 through October 2019. All data were obtained from the United Kingdom National Amyloidosis Centre database. The number of cases increased by 670% from the period 1987-1999 to the period 2010-2019 (Fig. 1A). Systemic light-chain (AL) amyloidosis remained the most common type and accounted for 55% of all cases (Fig. 1B). With the advances in therapies that target plasma cells, overall survival among patients with AL amyloidosis in-

Treating Protein Misfolding Diseases: Therapeutic Successes Against Systemic Amyloidoses

“…Indeed, cardiac amyloid deposits containing TTR can be detected in 12–25% of subjects older than 80 years at autopsy ( Cornwell et al., 1983 ; Tanskanen et al., 2008 ; Ueda et al., 2011 ). ATTRwt amyloidosis is an increasingly recognized cause of amyloid cardiomyopathy whose clinical detection has been conspicuously boosted by scintigraphy with bone tracers and increased awareness ( Ravichandran et al., 2020 ). Of note, scintigraphy with bone tracers enabled to detect ATTRwt amyloidosis in 14–16% of patients with severe symptomatic aortic stenosis listed for transcatheter aortic valve replacement ( Castano et al., 2017 ; Cavalcante et al., 2017 ; Scully et al., 2018 ; Scully et al., 2020 ).…”

Nuclear Imaging for the Diagnosis of Cardiac Amyloidosis in 2021

“…Systemic amyloidosis is a multisystem disorder characterized by the formation and deposition of mis-folded protein fibrils which can result in multi-organ failure and death [1,2]. This condition is associated with significant disease burden with increasing incidence and prevalence worldwide over the past decades [3][4][5]. Studies have shown that at least 20 out of one million UK residents are estimated to have systemic amyloidosis with 65% being light-chain (AL) amyloidosis.…”

“…Cardiac amyloidosis is defined as a group of disorders that involve the deposition of amyloid protein in the cardiac tissue, leading to myocardial dysfunction [10]. Due to the increasing awareness of the disease, improved life expectancy, and advancements in diagnostic pathways, cardiac amyloidosis is currently diagnosed more frequently than in the past, with AL and ATTR amyloidosis being the most common types [3]. One populationbased study focusing on Medicare beneficiaries in the United States revealed that between 2000 and 2012 the prevalence of cardiac amyloidosis increased from 8 to 17 cases per 100,000 person-year and the incidence increased from 18 to 55 cases per 100,000 personyear [11].…”

Wild-type transthyretin cardiac amyloidosis: When is a rare disease no longer a rare disease?

“…3 The recognition of the prevalence wild-type ATTR amyloidosis (wtATTR) changed over the last decade. 4 It was considered a rare clinical entity. Despite autopsy series showing that up to a quarter of all persons aged over 80 years may have ATTR amyloid deposits in the heart, 5 in the UK, less than 300 new cases were seen at the national referral centre in 2019.…”

“…Despite autopsy series showing that up to a quarter of all persons aged over 80 years may have ATTR amyloid deposits in the heart, 5 in the UK, less than 300 new cases were seen at the national referral centre in 2019. 4 Wider availability of cardiac MRI scanning has allowed for easier diagnosis of cardiac amyloidosis. In the last couple of years, availability of novel therapies that can stabilize the transthyretin molecule 6 or targeted agents that can block hepatic production of transthyretin 7,8 have been licenced for wtATTR and hereditary ATTR amyloidosis, respectively.…”