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Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis

Amyloidosis is associated with a number of rare diseases and is characterized by the deposition, in abdominothoracic organs and peripheral nerves, of extracellular protein fibrils, which leads to dysfunction and severe morbidity. Effective clinical evaluation and management of patients with systemic...

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Autores principales: Wall, Jonathan S., Kennel, Stephen J., Martin, Emily B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469514/
https://www.ncbi.nlm.nih.gov/pubmed/28654386
http://dx.doi.org/10.1177/1536012117708705
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author Wall, Jonathan S.
Kennel, Stephen J.
Martin, Emily B.
author_facet Wall, Jonathan S.
Kennel, Stephen J.
Martin, Emily B.
author_sort Wall, Jonathan S.
collection PubMed
description Amyloidosis is associated with a number of rare diseases and is characterized by the deposition, in abdominothoracic organs and peripheral nerves, of extracellular protein fibrils, which leads to dysfunction and severe morbidity. Effective clinical evaluation and management of patients with systemic amyloidosis are hampered by the lack of a noninvasive, quantitative method for detecting whole-body amyloid load. We have used a battery of assays including dual-energy SPECT imaging and comparative effectiveness studies in support of translation of a synthetic polybasic peptide, p5+14, as a novel radiotracer for visualization of amyloidosis by molecular imaging. These data provide support for a phase 1 positron emission tomography/computed tomography imaging trial of this reagent, labeled with iodine-124, in patients with all forms of systemic amyloidosis.
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spelling pubmed-54695142017-06-22 Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis Wall, Jonathan S. Kennel, Stephen J. Martin, Emily B. Mol Imaging Commentaries Amyloidosis is associated with a number of rare diseases and is characterized by the deposition, in abdominothoracic organs and peripheral nerves, of extracellular protein fibrils, which leads to dysfunction and severe morbidity. Effective clinical evaluation and management of patients with systemic amyloidosis are hampered by the lack of a noninvasive, quantitative method for detecting whole-body amyloid load. We have used a battery of assays including dual-energy SPECT imaging and comparative effectiveness studies in support of translation of a synthetic polybasic peptide, p5+14, as a novel radiotracer for visualization of amyloidosis by molecular imaging. These data provide support for a phase 1 positron emission tomography/computed tomography imaging trial of this reagent, labeled with iodine-124, in patients with all forms of systemic amyloidosis. SAGE Publications 2017-05-11 /pmc/articles/PMC5469514/ /pubmed/28654386 http://dx.doi.org/10.1177/1536012117708705 Text en © The Author(s) 2017 http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (http://www.creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage).
spellingShingle Commentaries
Wall, Jonathan S.
Kennel, Stephen J.
Martin, Emily B.
Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis
title Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis
title_full Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis
title_fullStr Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis
title_full_unstemmed Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis
title_short Dual-Energy SPECT and the Development of Peptide p5+14 for Imaging Amyloidosis
title_sort dual-energy spect and the development of peptide p5+14 for imaging amyloidosis
topic Commentaries
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469514/
https://www.ncbi.nlm.nih.gov/pubmed/28654386
http://dx.doi.org/10.1177/1536012117708705
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