Preliminary experience of <sup>99m</sup>Tc‐Aprotinin scintigraphy in amyloidosis

Han, Sai; Chong, Victor; Murray, T; McDonagh, Theresa A.; Hunter, John; Poon, F. W.; Gray, H. W.; Neilly, J. B.

doi:10.1111/j.1600-0609.2007.00963.x

Cited by 46 publications

(36 citation statements)

References 11 publications

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“…But, it is not widely available, shows limited signal in the heart, and is not used clinically due to concerns of bovine spongiform encephalitis (as it is produced from bovine lungs). 14 Intense uptake of bone imaging agents, 99m Technetium-3,3-diphosphono-1,2-propanodicarboxylic acid ( 99m Tc-DPD) and 99m Tc-pyrophosphate( 99m Tc-PYP), is accurate to diagnose cardiac ATTR amyloidosis likely due to high calcium levels in the amyloid deposits. 1516 99m Tc-DPD and 99m Tc-PYP are widely available and intense radiotracer uptake is highly specific for diagnosing cardiac ATTR amyloidosis.…”

Section: Discussionmentioning

confidence: 99%

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

Park

Padera

Belanger

et al. 2015

Circ: Cardiovascular Imaging

109

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Background 18F-florbetapir is a promising imaging biomarker for light chain (AL) and transthyretin (ATTR) cardiac amyloidosis. Our aim, using human autopsy myocardial specimens, was to test the hypothesis that 18F-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 non-amyloid controls (N = 10), using 18F-florbetapir and cold florbetapir compound and digital autoradiography. Total and non-specific binding of 18F-florbetapir was determined using the maximum signal intensity values. Specific binding of 18F-florbetapir was calculated by subtracting non-specific from total binding measurements (in decays per minute/mm2, DPM mm2), and was compared to cardiac structure and function on echocardiography and the histological extent of amyloid deposits. Diffuse or focally increased 18F-florbetapir uptake was noted in all AL and ATTR samples and in none of the control samples. Compared to control samples, mean 18F-florbetapir specific uptake was significantly higher in the amyloid samples (0.94 ± 0.43 vs. 2.00 ± 0.58 DPM/mm2, p < 0.001), and in the AL compared to the ATTR samples (2.48 ± 0.40 vs. 1.52 ± 0.22 DPM/mm2, p < 0.001). The samples from subjects with atypical echocardiographic features of amyloidosis showed quantitatively more intense 18F-florbetapir specific uptake compared to control samples (1.50 ± 0.17 vs. 0.94 ± 0.43 DPM/mm2, p = 0.004), despite smaller amyloid extent than in subjects with typical echocardiograms. Conclusions 18F-florbetapir specifically binds to myocardial AL and ATTR deposits in humans and offers the potential to screen for the two most common types of myocardial amyloid.

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Section: Discussionmentioning

confidence: 99%

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

Park

Padera

Belanger

et al. 2015

Circ: Cardiovascular Imaging

109

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“…It provides images of amyloid load that can be used to compliment routine diagnosis by histochemical analysis of tissue biopsies, aid in prognostication, and document response to therapy (24,25). Although 123 I-SAP scintigraphy is the most common imaging technique for the detection of amyloid in the peripheral organs, other methods using 99m Tc-aprotinin and 99m Tc-3,3-diphosphon-1,2-propanodicarboxylic acid for imaging cardiac amyloid and ATTR, respectively, are also available (26)(27)(28)(29)(30). These methods are rarely used, however, because of the nonspecific nature of the interaction.…”

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confidence: 99%

In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides

Wall

Richey²,

Stuckey

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

106

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Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ.

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“…These are especially helpful in non-AL amyloidosis, where cardiac biomarkers for the detection of early disease might not be as sensitive as in AL amyloidosis. In addition to providing diagnostic information about the extent of cardiac involvement, in some cases, they can also inform about the amyloid burden of extracardiac organs [107].…”

Section: Nuclear Imagingmentioning

confidence: 99%

Improving strategies for the diagnosis of cardiac amyloidosis

Kourelis

Gertz

2015

Expert Review of Cardiovascular Therapy

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Amyloidosis refers to a group of rare but potentially fatal, protein misfolding diseases. The heart is frequently involved in the most common types, that is, immunoglobulin light chain and transthyretin amyloidosis and is the single most important predictor of patient outcomes. A major limitation in improving patient outcomes, in addition to developing novel therapeutics, is the late diagnosis of the disease. Once suspected, an organ for biopsy should be targeted and the amyloid type should be identified by mass spectrometry. An endomyocardial biopsy should be offered if cardiac involvement is in doubt. Echocardiography, MRI and nuclear imaging can provide valuable diagnostic and prognostic information and can secure the diagnosis if amyloid has been identified in an extracardiac tissue.

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Preliminary experience of ^99mTc‐Aprotinin scintigraphy in amyloidosis

Abstract: 99mTc-Aprotinin imaging may be a useful non-invasive method for the assessment of the presence and extent of extra-abdominal amyloid, particularly cardiac amyloidosis. It has little role in diagnosis of amyloidosis involving the oro-facial and abdominal structures.

Cited by 46 publications

References 11 publications

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

In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides

Improving strategies for the diagnosis of cardiac amyloidosis

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Preliminary experience of 99mTc‐Aprotinin scintigraphy in amyloidosis

Abstract: 99mTc-Aprotinin imaging may be a useful non-invasive method for the assessment of the presence and extent of extra-abdominal amyloid, particularly cardiac amyloidosis. It has little role in diagnosis of amyloidosis involving the oro-facial and abdominal structures.

Cited by 46 publications

References 11 publications

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

In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides

Improving strategies for the diagnosis of cardiac amyloidosis

Contact Info

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Resources

About

Preliminary experience of ^99mTc‐Aprotinin scintigraphy in amyloidosis

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