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18 F-Florbetapir Binds Specifically to Myocardial Light Chain and Transthyretin Amyloid Deposits

18 F-Florbetapir Binds Specifically to Myocardial Light Chain and Transthyretin Amyloid Deposits Background— 18 F-florbetapir is a promising imaging biomarker for cardiac light chain amyloidosis (AL) and transthyretin amyloidosis (ATTR). Our aim, using human autopsy myocardial specimens, was to test the hypothesis that 18 F-florbetapir binds specifically to myocardial AL and ATTR amyloid deposits. Methods and Results— We studied myocardial sections from 30 subjects with autopsy-documented AL (n=10), ATTR (n=10), and nonamyloid controls (n=10) using 18 F-florbetapir and cold florbetapir compound and digital autoradiography. Total and nonspecific binding of 18 F-florbetapir was determined using the maximum signal intensity values. Specific binding of 18 F-florbetapir was calculated by subtracting nonspecific from total binding measurements (in decays per minute/mm 2 , DPM mm 2 ) and was compared with cardiac structure and function on echocardiography and the histological extent of amyloid deposits. Diffuse or focally increased 18 F-florbetapir uptake was noted in all AL and ATTR samples and in none of the control samples. Compared with control samples, mean 18 F-florbetapir–specific uptake was significantly higher in the amyloid samples (0.94±0.43 versus 2.00±0.58 DPM/mm 2 ; P <0.001), and in the AL compared with the ATTR samples (2.48±0.40 versus 1.52±0.22 DPM/mm 2 ; P <0.001). The samples from subjects with atypical echocardiographic features of amyloidosis showed quantitatively more intense 18 F-florbetapir–specific uptake compared with control samples (1.50±0.17 versus 0.94±0.43 DPM/mm 2 ; P =0.004), despite smaller amyloid extent than in subjects with typical echocardiograms. Conclusions— 18 F-florbetapir specifically binds to myocardial AL and ATTR deposits in humans and offers the potential to screen for the 2 most common types of myocardial amyloid. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Circulation: Cardiovascular Imaging Wolters Kluwer Health

18 F-Florbetapir Binds Specifically to Myocardial Light Chain and Transthyretin Amyloid Deposits

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Copyright
© 2015 American Heart Association, Inc.
Subject
11; 31; 32; 124; Original Articles; Molecular Imaging
ISSN
1941-9651
eISSN
1942-0080
DOI
10.1161/CIRCIMAGING.114.002954
pmid
26259579
Publisher site
See Article on Publisher Site

Abstract

Background— 18 F-florbetapir is a promising imaging biomarker for cardiac light chain amyloidosis (AL) and transthyretin amyloidosis (ATTR). Our aim, using human autopsy myocardial specimens, was to test the hypothesis that 18 F-florbetapir binds specifically to myocardial AL and ATTR amyloid deposits. Methods and Results— We studied myocardial sections from 30 subjects with autopsy-documented AL (n=10), ATTR (n=10), and nonamyloid controls (n=10) using 18 F-florbetapir and cold florbetapir compound and digital autoradiography. Total and nonspecific binding of 18 F-florbetapir was determined using the maximum signal intensity values. Specific binding of 18 F-florbetapir was calculated by subtracting nonspecific from total binding measurements (in decays per minute/mm 2 , DPM mm 2 ) and was compared with cardiac structure and function on echocardiography and the histological extent of amyloid deposits. Diffuse or focally increased 18 F-florbetapir uptake was noted in all AL and ATTR samples and in none of the control samples. Compared with control samples, mean 18 F-florbetapir–specific uptake was significantly higher in the amyloid samples (0.94±0.43 versus 2.00±0.58 DPM/mm 2 ; P <0.001), and in the AL compared with the ATTR samples (2.48±0.40 versus 1.52±0.22 DPM/mm 2 ; P <0.001). The samples from subjects with atypical echocardiographic features of amyloidosis showed quantitatively more intense 18 F-florbetapir–specific uptake compared with control samples (1.50±0.17 versus 0.94±0.43 DPM/mm 2 ; P =0.004), despite smaller amyloid extent than in subjects with typical echocardiograms. Conclusions— 18 F-florbetapir specifically binds to myocardial AL and ATTR deposits in humans and offers the potential to screen for the 2 most common types of myocardial amyloid.

Journal

Circulation: Cardiovascular Imaging – Wolters Kluwer Health

Published: Aug 1, 2015

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