Effects of periodontal disease on the proteomic profile of the periodontal ligament
Main Author: | |
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Publication Date: | 2025 |
Other Authors: | , , , , , , , |
Format: | Article |
Language: | eng |
Source: | Repositório Institucional da UNESP |
Download full: | http://dx.doi.org/10.1016/j.jprot.2025.105384 https://hdl.handle.net/11449/300357 |
Summary: | Periodontal disease affects over 1 billion people globally. This study investigated how periodontitis affects the protein profile of the periodontal ligament (PDL) in rats. Eight Holtzman rats were divided into control and experimental periodontitis groups. The PDL was isolated using laser capture microdissection and protein extracts were analyzed by mass spectrometry. Data analysis utilized specialized software, and Gene Ontology enrichment analysis identified significant protein functions. The data are available via ProteomeXchange with identifier PXD055817. Proteins such as SerpinB1, C5, and Lgals3 were validated through immunohistochemistry, and their gene expression was examined in an in vitro human PDL cell line. This study identified 1326 proteins, with 156 unique to the control group, 294 unique to the periodontitis group, and 876 common to both groups. Enrichment analysis revealed that proteins associated with the regulation of enzyme activity and RNA binding were significantly represented in the periodontitis group. There were increased levels of SerpinB1, C5, and Lgals3 in the periodontitis group based on proteomic and immunohistochemical analyses. Furthermore, these targets showed increased gene expression in stimulated human PDL cells. This study provides insights into the periodontitis-related alterations in the protein composition of the PDL and PDL cells, identifying both novel and previously known disease-associated proteins. Significance: The periodontal ligament plays a crucial role in oral functions by providing structural support to the tooth. Due to the presence of undifferentiated mesenchymal cells, research into its regenerative capacity is ongoing. Pathological conditions can affect these functions and protein composition. Currently, there is a lack of comprehensive research specifically focusing on evaluating the periodontal ligament in both healthy and diseased states. This pioneering study screened for protein alterations and the mechanisms related to periodontitis. The possibility of using proteomic analysis to evaluate the protein alterations that occur in periodontitis, a disease with a high global incidence, could provide therapeutic targets and new biomarkers for future clinical studies. |
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Effects of periodontal disease on the proteomic profile of the periodontal ligamentC5Lgals3Periodontal ligamentPeriodontitisProteomicsSerpinB1Periodontal disease affects over 1 billion people globally. This study investigated how periodontitis affects the protein profile of the periodontal ligament (PDL) in rats. Eight Holtzman rats were divided into control and experimental periodontitis groups. The PDL was isolated using laser capture microdissection and protein extracts were analyzed by mass spectrometry. Data analysis utilized specialized software, and Gene Ontology enrichment analysis identified significant protein functions. The data are available via ProteomeXchange with identifier PXD055817. Proteins such as SerpinB1, C5, and Lgals3 were validated through immunohistochemistry, and their gene expression was examined in an in vitro human PDL cell line. This study identified 1326 proteins, with 156 unique to the control group, 294 unique to the periodontitis group, and 876 common to both groups. Enrichment analysis revealed that proteins associated with the regulation of enzyme activity and RNA binding were significantly represented in the periodontitis group. There were increased levels of SerpinB1, C5, and Lgals3 in the periodontitis group based on proteomic and immunohistochemical analyses. Furthermore, these targets showed increased gene expression in stimulated human PDL cells. This study provides insights into the periodontitis-related alterations in the protein composition of the PDL and PDL cells, identifying both novel and previously known disease-associated proteins. Significance: The periodontal ligament plays a crucial role in oral functions by providing structural support to the tooth. Due to the presence of undifferentiated mesenchymal cells, research into its regenerative capacity is ongoing. Pathological conditions can affect these functions and protein composition. Currently, there is a lack of comprehensive research specifically focusing on evaluating the periodontal ligament in both healthy and diseased states. This pioneering study screened for protein alterations and the mechanisms related to periodontitis. The possibility of using proteomic analysis to evaluate the protein alterations that occur in periodontitis, a disease with a high global incidence, could provide therapeutic targets and new biomarkers for future clinical studies.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Deutsche ForschungsgemeinschaftDepartment of Diagnosis and Surgery School of Dentistry at Araraquara São Paulo State University - UNESP, AraraquaraDepartment of Prosthodontics and Periodontics Division of Periodontics Piracicaba Dental School University of Campinas – UNICAMP, PiracicabaDental School Centro Universitário N. Sra do Patrocínio – CEUNSP ItuDepartment of Genetics Evolution Microbiology and Immunology Institute of Biology University of Campinas – UNICAMP, CampinasADA Forsyth InstituteDental School São Leopoldo Mandic Department of Research, CampinasLaboratory of Oral Microbiology Department of Periodontology University of BernDepartment of Periodontology and Operative Dentistry University Medical Center of the Johannes Gutenberg UniversityDepartment of Diagnosis and Surgery School of Dentistry at Araraquara São Paulo State University - UNESP, AraraquaraDeutsche Forschungsgemeinschaft: 1593/5-1FAPESP: 2014/20715-7FAPESP: 2017/07137-2FAPESP: 2018/23599-9Universidade Estadual Paulista (UNESP)Universidade Estadual de Campinas (UNICAMP)ItuADA Forsyth InstituteSão Leopoldo MandicUniversity of BernUniversity Medical Center of the Johannes Gutenberg UniversityLopes, Maria Eduarda Scordamaia [UNESP]Marcantonio, Camila Chierici [UNESP]Salmon, Cristiane RibeiroMofatto, Luciana SoutoNociti Junior, Francisco HumbertoEick, SigrunDeschner, JamesCirelli, Joni Augusto [UNESP]Nogueira, Andressa Vilas Boas [UNESP]2025-04-29T18:49:25Z2025-04-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.jprot.2025.105384Journal of Proteomics, v. 314.1876-77371874-3919https://hdl.handle.net/11449/30035710.1016/j.jprot.2025.1053842-s2.0-85216011457Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Proteomicsinfo:eu-repo/semantics/openAccess2025-05-01T05:50:04Zoai:repositorio.unesp.br:11449/300357Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462025-05-01T05:50:04Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
title |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
spellingShingle |
Effects of periodontal disease on the proteomic profile of the periodontal ligament Lopes, Maria Eduarda Scordamaia [UNESP] C5 Lgals3 Periodontal ligament Periodontitis Proteomics SerpinB1 |
title_short |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
title_full |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
title_fullStr |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
title_full_unstemmed |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
title_sort |
Effects of periodontal disease on the proteomic profile of the periodontal ligament |
author |
Lopes, Maria Eduarda Scordamaia [UNESP] |
author_facet |
Lopes, Maria Eduarda Scordamaia [UNESP] Marcantonio, Camila Chierici [UNESP] Salmon, Cristiane Ribeiro Mofatto, Luciana Souto Nociti Junior, Francisco Humberto Eick, Sigrun Deschner, James Cirelli, Joni Augusto [UNESP] Nogueira, Andressa Vilas Boas [UNESP] |
author_role |
author |
author2 |
Marcantonio, Camila Chierici [UNESP] Salmon, Cristiane Ribeiro Mofatto, Luciana Souto Nociti Junior, Francisco Humberto Eick, Sigrun Deschner, James Cirelli, Joni Augusto [UNESP] Nogueira, Andressa Vilas Boas [UNESP] |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Universidade Estadual de Campinas (UNICAMP) Itu ADA Forsyth Institute São Leopoldo Mandic University of Bern University Medical Center of the Johannes Gutenberg University |
dc.contributor.author.fl_str_mv |
Lopes, Maria Eduarda Scordamaia [UNESP] Marcantonio, Camila Chierici [UNESP] Salmon, Cristiane Ribeiro Mofatto, Luciana Souto Nociti Junior, Francisco Humberto Eick, Sigrun Deschner, James Cirelli, Joni Augusto [UNESP] Nogueira, Andressa Vilas Boas [UNESP] |
dc.subject.por.fl_str_mv |
C5 Lgals3 Periodontal ligament Periodontitis Proteomics SerpinB1 |
topic |
C5 Lgals3 Periodontal ligament Periodontitis Proteomics SerpinB1 |
description |
Periodontal disease affects over 1 billion people globally. This study investigated how periodontitis affects the protein profile of the periodontal ligament (PDL) in rats. Eight Holtzman rats were divided into control and experimental periodontitis groups. The PDL was isolated using laser capture microdissection and protein extracts were analyzed by mass spectrometry. Data analysis utilized specialized software, and Gene Ontology enrichment analysis identified significant protein functions. The data are available via ProteomeXchange with identifier PXD055817. Proteins such as SerpinB1, C5, and Lgals3 were validated through immunohistochemistry, and their gene expression was examined in an in vitro human PDL cell line. This study identified 1326 proteins, with 156 unique to the control group, 294 unique to the periodontitis group, and 876 common to both groups. Enrichment analysis revealed that proteins associated with the regulation of enzyme activity and RNA binding were significantly represented in the periodontitis group. There were increased levels of SerpinB1, C5, and Lgals3 in the periodontitis group based on proteomic and immunohistochemical analyses. Furthermore, these targets showed increased gene expression in stimulated human PDL cells. This study provides insights into the periodontitis-related alterations in the protein composition of the PDL and PDL cells, identifying both novel and previously known disease-associated proteins. Significance: The periodontal ligament plays a crucial role in oral functions by providing structural support to the tooth. Due to the presence of undifferentiated mesenchymal cells, research into its regenerative capacity is ongoing. Pathological conditions can affect these functions and protein composition. Currently, there is a lack of comprehensive research specifically focusing on evaluating the periodontal ligament in both healthy and diseased states. This pioneering study screened for protein alterations and the mechanisms related to periodontitis. The possibility of using proteomic analysis to evaluate the protein alterations that occur in periodontitis, a disease with a high global incidence, could provide therapeutic targets and new biomarkers for future clinical studies. |
publishDate |
2025 |
dc.date.none.fl_str_mv |
2025-04-29T18:49:25Z 2025-04-15 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.jprot.2025.105384 Journal of Proteomics, v. 314. 1876-7737 1874-3919 https://hdl.handle.net/11449/300357 10.1016/j.jprot.2025.105384 2-s2.0-85216011457 |
url |
http://dx.doi.org/10.1016/j.jprot.2025.105384 https://hdl.handle.net/11449/300357 |
identifier_str_mv |
Journal of Proteomics, v. 314. 1876-7737 1874-3919 10.1016/j.jprot.2025.105384 2-s2.0-85216011457 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Proteomics |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
repositoriounesp@unesp.br |
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1834482485145108480 |