Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis
Follicular lymphoma (FL) represents the major subtype of indolent B-cell non-Hodgkin lymphomas (B-NHLs) and results from the malignant transformation of mature B-cells in lymphoid organs. Although gene expression and genomic studies have identified multiple disease driving gene aberrations, only a f...
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MDPI AG
2021-02-01
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| Series: | Cancers |
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| author | Kamila Duś-Szachniewicz Grzegorz Rymkiewicz Anil Kumar Agrawal Paweł Kołodziej Jacek R. Wiśniewski |
| author_facet | Kamila Duś-Szachniewicz Grzegorz Rymkiewicz Anil Kumar Agrawal Paweł Kołodziej Jacek R. Wiśniewski |
| author_sort | Kamila Duś-Szachniewicz |
| collection | DOAJ |
| description | Follicular lymphoma (FL) represents the major subtype of indolent B-cell non-Hodgkin lymphomas (B-NHLs) and results from the malignant transformation of mature B-cells in lymphoid organs. Although gene expression and genomic studies have identified multiple disease driving gene aberrations, only a few proteomic studies focused on the protein level. The present work aimed to examine the proteomic profiles of follicular lymphoma vs. normal B-cells obtained by fine-needle aspiration biopsy (FNAB) to gain deep insight into the most perturbed pathway of FL. The cells of interest were purified by magnetic-activated cell sorting (MACS). High-throughput proteomic profiling was performed using liquid chromatography-tandem mass spectrometry (LC-MS/MS) and allowed to identify of 6724 proteins in at least 75% of each group of samples. The ‘Total Protein Approach’ (TPA) was applied to the absolute quantification of proteins in this study. We identified 1186 differentially abundant proteins (DAPs) between FL and control samples, causing an extensive remodeling of several molecular pathways, including the B-cell receptor signaling pathway, cellular adhesion molecules, and PPAR pathway. Additionally, the construction of protein–protein interactions networks (PPINs) and identification of hub proteins allowed us to indicate the key player proteins for FL pathology. Finally, ICAM1, CD9, and CD79B protein expression was validated in an independent cohort by flow cytometry (FCM), and the results were consistent with the mass spectrometry (MS) data. |
| first_indexed | 2024-03-09T05:34:07Z |
| format | Article |
| id | doaj.art-0a86c97bb55b491cba9aafb37e2cf5a8 |
| institution | Directory Open Access Journal |
| issn | 2072-6694 |
| language | English |
| last_indexed | 2024-03-09T05:34:07Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cancers |
| spelling | doaj.art-0a86c97bb55b491cba9aafb37e2cf5a82023-12-03T12:29:56ZengMDPI AGCancers2072-66942021-02-0113463010.3390/cancers13040630Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the LymphomagenesisKamila Duś-Szachniewicz0Grzegorz Rymkiewicz1Anil Kumar Agrawal2Paweł Kołodziej3Jacek R. Wiśniewski4Department of Pathology, Wrocław Medical University, Marcinkowskiego 1, 50-368 Wrocław, PolandFlow Cytometry Laboratory, Department of Pathology and Laboratory Diagnostics, Maria Skłodowska-Curie National Research Institute of Oncology, Roentgen 5, 02-781 Warsaw, Poland2nd Department of General and Oncological Surgery, Wrocław Medical University, Borowska 213, 50-556 Wrocław, PolandDivision of Pathology, Sokołowski Hospital Wałbrzych, Sokołowskiego 4, 58-309 Wałbrzych, PolandBiochemical Proteomics Group, Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, GermanyFollicular lymphoma (FL) represents the major subtype of indolent B-cell non-Hodgkin lymphomas (B-NHLs) and results from the malignant transformation of mature B-cells in lymphoid organs. Although gene expression and genomic studies have identified multiple disease driving gene aberrations, only a few proteomic studies focused on the protein level. The present work aimed to examine the proteomic profiles of follicular lymphoma vs. normal B-cells obtained by fine-needle aspiration biopsy (FNAB) to gain deep insight into the most perturbed pathway of FL. The cells of interest were purified by magnetic-activated cell sorting (MACS). High-throughput proteomic profiling was performed using liquid chromatography-tandem mass spectrometry (LC-MS/MS) and allowed to identify of 6724 proteins in at least 75% of each group of samples. The ‘Total Protein Approach’ (TPA) was applied to the absolute quantification of proteins in this study. We identified 1186 differentially abundant proteins (DAPs) between FL and control samples, causing an extensive remodeling of several molecular pathways, including the B-cell receptor signaling pathway, cellular adhesion molecules, and PPAR pathway. Additionally, the construction of protein–protein interactions networks (PPINs) and identification of hub proteins allowed us to indicate the key player proteins for FL pathology. Finally, ICAM1, CD9, and CD79B protein expression was validated in an independent cohort by flow cytometry (FCM), and the results were consistent with the mass spectrometry (MS) data.https://www.mdpi.com/2072-6694/13/4/630follicular lymphoma (FL)label-free quantitative proteomicsprotein-protein interaction network (PPIN)differentially abundant proteins (DAPs)hub proteinscellular adhesion molecules (CAMs) |
| spellingShingle | Kamila Duś-Szachniewicz Grzegorz Rymkiewicz Anil Kumar Agrawal Paweł Kołodziej Jacek R. Wiśniewski Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis Cancers follicular lymphoma (FL) label-free quantitative proteomics protein-protein interaction network (PPIN) differentially abundant proteins (DAPs) hub proteins cellular adhesion molecules (CAMs) |
| title | Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis |
| title_full | Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis |
| title_fullStr | Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis |
| title_full_unstemmed | Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis |
| title_short | Large-Scale Proteomic Analysis of Follicular Lymphoma Reveals Extensive Remodeling of Cell Adhesion Pathway and Identifies Hub Proteins Related to the Lymphomagenesis |
| title_sort | large scale proteomic analysis of follicular lymphoma reveals extensive remodeling of cell adhesion pathway and identifies hub proteins related to the lymphomagenesis |
| topic | follicular lymphoma (FL) label-free quantitative proteomics protein-protein interaction network (PPIN) differentially abundant proteins (DAPs) hub proteins cellular adhesion molecules (CAMs) |
| url | https://www.mdpi.com/2072-6694/13/4/630 |
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