Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry

Glioblastoma (GBM) is the most aggressive brain tumor, and different efforts have been employed in the search for new drugs and therapeutic protocols for GBM. A label-free, mass spectrometry–based quantitative proteomics has been developed to identify and characterize proteins that are differentiall...

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Main Authors: Aline Menezes, Yara Martins, Fábio Nogueira, Denise De Abreu Pereira, Katia Carneiro
Format: Article
Language:English
Published: Bio-protocol LLC 2025-02-01
Series:Bio-Protocol
Online Access:https://bio-protocol.org/en/bpdetail?id=5197&type=0
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author Aline Menezes
Yara Martins
Fábio Nogueira
Denise De Abreu Pereira
Katia Carneiro
author_facet Aline Menezes
Yara Martins
Fábio Nogueira
Denise De Abreu Pereira
Katia Carneiro
author_sort Aline Menezes
collection DOAJ
description Glioblastoma (GBM) is the most aggressive brain tumor, and different efforts have been employed in the search for new drugs and therapeutic protocols for GBM. A label-free, mass spectrometry–based quantitative proteomics has been developed to identify and characterize proteins that are differentially expressed in GBM to gain a better understanding of the interactions and functions that lead to the pathological state focusing on the extracellular matrix (ECM). The main challenge in GBM research has been to identify novel molecular therapeutic targets and accurate diagnostic/prognostic biomarkers. To better investigate the GBM secretome upon in vitro treatment with histone deacetylase inhibitor (iHDAC), we employed a high-throughput label-free methodology of protein identification and quantification based on mass spectrometry followed by in silico studies. Our analysis revealed significant changes in the ECM protein profile, particularly those associated with the angiogenic matrisome. Proteins such as decorin, ADAM10, ADAM12, and ADAM15 were differentially regulated upon in silico analysis. In contrast, key angiogenesis markers such as VEGF and ECM proteins like fibronectin and integrins did not display significant changes. These results suggest that iHDAC inhibitors may modulate or suppress tumor behavior growth by targeting ECM proteins’ secretion rather than directly inhibiting angiogenesis.
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institution Kabale University
issn 2331-8325
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spelling doaj-art-c6041d20d05f4f9fa674a0e32fb664162025-02-07T08:16:46ZengBio-protocol LLCBio-Protocol2331-83252025-02-0115310.21769/BioProtoc.5197Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass SpectrometryAline Menezes0Yara Martins1Fábio Nogueira2Denise De Abreu Pereira3Katia Carneiro4Instituto de Ciências Biomédicas e Programa de Pós-graduação em Medicina (Anatomia Patológica), Universidade Federal do Rio de Janeiro, Rio de Janeiro, BrazilLaboratório de Biomedicina do Cérebro, Instituto Estadual do Cérebro Paulo Niemeyer, -IEC, Rio de Janeiro, BrazilLaboratório de Proteômica, LADETEC, Instituto de Química, Universidade Federal do Rio de Janeiro - UFRJ, Rio de Janeiro, BrazilCentro de Medicina de Precisão, Instituto Carlos Chagas Filho, Universidade Federal do Rio de Janeiro - UFRJ, Rio de Janeiro, BrazilLaboratório de Proteômica, LADETEC, Instituto de Química, Universidade Federal do Rio de Janeiro - UFRJ, Rio de Janeiro, BrazilCentro de Medicina de Precisão, Instituto Carlos Chagas Filho, Universidade Federal do Rio de Janeiro - UFRJ, Rio de Janeiro, BrazilPrograma de Oncobiologia Celular e Molecular, Coordenação de Pesquisa e Inivação, Instituto Nacional do Câncer- INCA, Rio de Janeiro, BrazilInstituto de Ciências Biomédicas e Programa de Pós-graduação em Medicina (Anatomia Patológica), Universidade Federal do Rio de Janeiro, Rio de Janeiro, BrazilGlioblastoma (GBM) is the most aggressive brain tumor, and different efforts have been employed in the search for new drugs and therapeutic protocols for GBM. A label-free, mass spectrometry–based quantitative proteomics has been developed to identify and characterize proteins that are differentially expressed in GBM to gain a better understanding of the interactions and functions that lead to the pathological state focusing on the extracellular matrix (ECM). The main challenge in GBM research has been to identify novel molecular therapeutic targets and accurate diagnostic/prognostic biomarkers. To better investigate the GBM secretome upon in vitro treatment with histone deacetylase inhibitor (iHDAC), we employed a high-throughput label-free methodology of protein identification and quantification based on mass spectrometry followed by in silico studies. Our analysis revealed significant changes in the ECM protein profile, particularly those associated with the angiogenic matrisome. Proteins such as decorin, ADAM10, ADAM12, and ADAM15 were differentially regulated upon in silico analysis. In contrast, key angiogenesis markers such as VEGF and ECM proteins like fibronectin and integrins did not display significant changes. These results suggest that iHDAC inhibitors may modulate or suppress tumor behavior growth by targeting ECM proteins’ secretion rather than directly inhibiting angiogenesis.https://bio-protocol.org/en/bpdetail?id=5197&type=0
spellingShingle Aline Menezes
Yara Martins
Fábio Nogueira
Denise De Abreu Pereira
Katia Carneiro
Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry
Bio-Protocol
title Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry
title_full Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry
title_fullStr Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry
title_full_unstemmed Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry
title_short Profiling the Secretome of Glioblastoma Cells Under Histone Deacetylase Inhibition Using Mass Spectrometry
title_sort profiling the secretome of glioblastoma cells under histone deacetylase inhibition using mass spectrometry
url https://bio-protocol.org/en/bpdetail?id=5197&type=0
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