Scintigraphic and echocardiographic evaluation of patients with cardiac transthyretin amyloidosis and first-degree relatives

Abstract Funding Acknowledgements Type of funding sources: Other. Main source(s): Pfizer Research Grant (ID#57165999) Background Misfolding transthyretin (TTR) is the source two distinct forms amyloidosis (ATTR): acquired or wild-type (ATTRwt) and hereditary (ATTRm), which transmitted in an autosomal dominant inheritance with a variable penetrance. Types gene mutations display genetic ethnic variability. Purpose The aim this prospective study was to assess TTR variants, echocardiographic parameters regional left ventricle 99mTc-DPD uptake among patients ATTR first-degree relatives. Methods We present data based on evaluation first 25 (13 (52%) females), including 10 (40%) index (age 66.4 ± 13 years) 15 (60%) relatives who were studied between June 2020 February 2021. Analysis included clinical data, free light chain blood immunoglobulins urine immunofixation, transthoracic echocardiography (TTE) global longitudinal strain (GLS) analysis, single-photon emission computed tomography (SPECT) 3,3-disphono-1,2-propanodicarboxylic acid (DPD), testing by amplicon-based next-generation sequencing approach, selected cases cardiac soft tissue biopsy. Results Overall, 6 diagnosed ATTRm 4 ATTRwt presenting mixed, neuropathic phenotype. There detected following types variants - Phe53Leu, Ala101Val, Glu112Lys, Glu109Lys. Nine out amyloid cardiomyopathy (CA) grade 2-3 tracer SPECT symptomatic heart failure (NYHA 2.2 1.1; NT-proBNP value 2224 2799 pg/ml). In both there either focal diffuse pattern evaluated technique. TTE marked (LV) hypertrophy maximum wall thickness 22 5 mm LV mass 382 111 g/m2. All CA had abnormal (GLS, -14.5 5%) diastolic dysfunction (EA 1.56 0.76, E/E’ 16 11). None expressed scintigraphy. Phe53Leu variant, them presented decreased GLS value. Conclusions Patients hypertrophy, value, scintigraphy increased However, some pathogenic variant