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Mass Spectrometry-Based Glycoproteomics and Prostate Cancer

Aberrant glycosylation has long been known to be associated with cancer, since it is involved in key mechanisms such as tumour onset, development and progression. This review will focus on protein glycosylation studies in cells, tissue, urine and serum in the context of prostate cancer. A dedicated...

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Detalles Bibliográficos
Autores principales: Gabriele, Caterina, Prestagiacomo, Licia E., Cuda, Giovanni, Gaspari, Marco
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8156230/
https://www.ncbi.nlm.nih.gov/pubmed/34069262
http://dx.doi.org/10.3390/ijms22105222
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author Gabriele, Caterina
Prestagiacomo, Licia E.
Cuda, Giovanni
Gaspari, Marco
author_facet Gabriele, Caterina
Prestagiacomo, Licia E.
Cuda, Giovanni
Gaspari, Marco
author_sort Gabriele, Caterina
collection PubMed
description Aberrant glycosylation has long been known to be associated with cancer, since it is involved in key mechanisms such as tumour onset, development and progression. This review will focus on protein glycosylation studies in cells, tissue, urine and serum in the context of prostate cancer. A dedicated section will cover the glycoforms of prostate specific antigen, the molecule that, despite some important limitations, is routinely tested for helping prostate cancer diagnosis. Our aim is to provide readers with an overview of mass spectrometry-based glycoproteomics of prostate cancer. From this perspective, the first part of this review will illustrate the main strategies for glycopeptide enrichment and mass spectrometric analysis. The molecular information obtained by glycoproteomic analysis performed by mass spectrometry has led to new insights into the mechanism linking aberrant glycosylation to cancer cell proliferation, migration and immunoescape.
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spelling pubmed-81562302021-05-28 Mass Spectrometry-Based Glycoproteomics and Prostate Cancer Gabriele, Caterina Prestagiacomo, Licia E. Cuda, Giovanni Gaspari, Marco Int J Mol Sci Review Aberrant glycosylation has long been known to be associated with cancer, since it is involved in key mechanisms such as tumour onset, development and progression. This review will focus on protein glycosylation studies in cells, tissue, urine and serum in the context of prostate cancer. A dedicated section will cover the glycoforms of prostate specific antigen, the molecule that, despite some important limitations, is routinely tested for helping prostate cancer diagnosis. Our aim is to provide readers with an overview of mass spectrometry-based glycoproteomics of prostate cancer. From this perspective, the first part of this review will illustrate the main strategies for glycopeptide enrichment and mass spectrometric analysis. The molecular information obtained by glycoproteomic analysis performed by mass spectrometry has led to new insights into the mechanism linking aberrant glycosylation to cancer cell proliferation, migration and immunoescape. MDPI 2021-05-14 /pmc/articles/PMC8156230/ /pubmed/34069262 http://dx.doi.org/10.3390/ijms22105222 Text en © 2021 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 Review
Gabriele, Caterina
Prestagiacomo, Licia E.
Cuda, Giovanni
Gaspari, Marco
Mass Spectrometry-Based Glycoproteomics and Prostate Cancer
title Mass Spectrometry-Based Glycoproteomics and Prostate Cancer
title_full Mass Spectrometry-Based Glycoproteomics and Prostate Cancer
title_fullStr Mass Spectrometry-Based Glycoproteomics and Prostate Cancer
title_full_unstemmed Mass Spectrometry-Based Glycoproteomics and Prostate Cancer
title_short Mass Spectrometry-Based Glycoproteomics and Prostate Cancer
title_sort mass spectrometry-based glycoproteomics and prostate cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8156230/
https://www.ncbi.nlm.nih.gov/pubmed/34069262
http://dx.doi.org/10.3390/ijms22105222
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