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The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?

AL amyloidosis is caused by the misfolding of immunoglobulin light chains leading to an impaired function of tissues and organs in which they accumulate. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system wide. To fill this gap, w...

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Autores principales: Di Silvestre, Dario, Brambilla, Francesca, Lavatelli, Francesca, Chirivì, Maila, Canetti, Diana, Bearzi, Claudia, Rizzi, Roberto, Bijzet, Johan, Hazenberg, Bouke P. C., Bellotti, Vittorio, Gillmore, Julian D., Mauri, Pierluigi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10000381/
https://www.ncbi.nlm.nih.gov/pubmed/36899835
http://dx.doi.org/10.3390/cells12050699
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author Di Silvestre, Dario
Brambilla, Francesca
Lavatelli, Francesca
Chirivì, Maila
Canetti, Diana
Bearzi, Claudia
Rizzi, Roberto
Bijzet, Johan
Hazenberg, Bouke P. C.
Bellotti, Vittorio
Gillmore, Julian D.
Mauri, Pierluigi
author_facet Di Silvestre, Dario
Brambilla, Francesca
Lavatelli, Francesca
Chirivì, Maila
Canetti, Diana
Bearzi, Claudia
Rizzi, Roberto
Bijzet, Johan
Hazenberg, Bouke P. C.
Bellotti, Vittorio
Gillmore, Julian D.
Mauri, Pierluigi
author_sort Di Silvestre, Dario
collection PubMed
description AL amyloidosis is caused by the misfolding of immunoglobulin light chains leading to an impaired function of tissues and organs in which they accumulate. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system wide. To fill this gap, we evaluated proteome changes in the abdominal subcutaneous adipose tissue of patients affected by the AL isotypes κ and λ. Through our retrospective analysis based on graph theory, we have herein deduced new insights representing a step forward from the pioneering proteomic investigations previously published by our group. ECM/cytoskeleton, oxidative stress and proteostasis were confirmed as leading processes. In this scenario, some proteins, including glutathione peroxidase 1 (GPX1), tubulins and the TRiC complex, were classified as biologically and topologically relevant. These and other results overlap with those already reported for other amyloidoses, supporting the hypothesis that amyloidogenic proteins could induce similar mechanisms independently of the main fibril precursor and of the target tissues/organs. Of course, further studies based on larger patient cohorts and different tissues/organs will be essential, which would be a key point that would allow for a more robust selection of the main molecular players and a more accurate correlation with clinical aspects.
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spelling pubmed-100003812023-03-11 The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis? Di Silvestre, Dario Brambilla, Francesca Lavatelli, Francesca Chirivì, Maila Canetti, Diana Bearzi, Claudia Rizzi, Roberto Bijzet, Johan Hazenberg, Bouke P. C. Bellotti, Vittorio Gillmore, Julian D. Mauri, Pierluigi Cells Article AL amyloidosis is caused by the misfolding of immunoglobulin light chains leading to an impaired function of tissues and organs in which they accumulate. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system wide. To fill this gap, we evaluated proteome changes in the abdominal subcutaneous adipose tissue of patients affected by the AL isotypes κ and λ. Through our retrospective analysis based on graph theory, we have herein deduced new insights representing a step forward from the pioneering proteomic investigations previously published by our group. ECM/cytoskeleton, oxidative stress and proteostasis were confirmed as leading processes. In this scenario, some proteins, including glutathione peroxidase 1 (GPX1), tubulins and the TRiC complex, were classified as biologically and topologically relevant. These and other results overlap with those already reported for other amyloidoses, supporting the hypothesis that amyloidogenic proteins could induce similar mechanisms independently of the main fibril precursor and of the target tissues/organs. Of course, further studies based on larger patient cohorts and different tissues/organs will be essential, which would be a key point that would allow for a more robust selection of the main molecular players and a more accurate correlation with clinical aspects. MDPI 2023-02-22 /pmc/articles/PMC10000381/ /pubmed/36899835 http://dx.doi.org/10.3390/cells12050699 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Di Silvestre, Dario
Brambilla, Francesca
Lavatelli, Francesca
Chirivì, Maila
Canetti, Diana
Bearzi, Claudia
Rizzi, Roberto
Bijzet, Johan
Hazenberg, Bouke P. C.
Bellotti, Vittorio
Gillmore, Julian D.
Mauri, Pierluigi
The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
title The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
title_full The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
title_fullStr The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
title_full_unstemmed The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
title_short The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
title_sort protein network in subcutaneous fat biopsies from patients with al amyloidosis: more than diagnosis?
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10000381/
https://www.ncbi.nlm.nih.gov/pubmed/36899835
http://dx.doi.org/10.3390/cells12050699
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