Label-Free Quantitative Proteomics Reveals Differentially Regulated Proteins in Experimental Gingivitis
We investigated the sequential protein expression in gingival crevicular fluid samples during the induction (I) and resolution (R) of experimental gingivitis. Periodontally and systemically healthy volunteers (n = 20) participated in a three-week experimental gingivitis protocol, followed by debride...
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Published in | Journal of proteome research Vol. 12; no. 2; pp. 657 - 678 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
01.02.2013
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Subjects | |
Online Access | Get full text |
ISSN | 1535-3893 1535-3907 1535-3907 |
DOI | 10.1021/pr300761e |
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Abstract | We investigated the sequential protein expression in gingival crevicular fluid samples during the induction (I) and resolution (R) of experimental gingivitis. Periodontally and systemically healthy volunteers (n = 20) participated in a three-week experimental gingivitis protocol, followed by debridement and two weeks of regular plaque control. Gingival crevicular fluid (GCF) samples were collected at baseline, Day 7, 14, and 21 (induction; I-phase), and at Day 21, 25, 30, and 35 (resolution; R-phase). Liquid chromatography–tandem mass spectrometry (LC–MS/MS) for label-free quantitative proteomics was applied. A total of 287 proteins were identified including 254 human, 14 bacterial, 12 fungal, and 7 yeast proteins. Ontology analysis revealed proteins primarily involved in cytoskeletal rearrangements, immune response, antimicrobial function, protein degradation, and DNA binding. There was considerable variation in the number of proteins identified, both among subjects and within subjects across time points. After pooling of samples between subjects at each time point, the levels of 59 proteins in the I-phase and 73 proteins in the R-phase were quantified longitudinally. Our data demonstrate that LC–MS/MS label-free quantitative proteomics is valuable in the assessment of the protein content of the GCF and can facilitate a better understanding of the molecular mechanisms involved in the induction and resolution of plaque-induced gingival inflammation in humans. |
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AbstractList | We investigated the sequential protein expression in gingival crevicular fluid samples during the induction (I) and resolution (R) of experimental gingivitis. Periodontally and systemically healthy volunteers (n = 20) participated in a three-week experimental gingivitis protocol, followed by debridement and two weeks of regular plaque control. Gingival crevicular fluid (GCF) samples were collected at baseline, Day 7, 14, and 21 (induction; I-phase), and at Day 21, 25, 30, and 35 (resolution; R-phase). Liquid chromatography–tandem mass spectrometry (LC–MS/MS) for label-free quantitative proteomics was applied. A total of 287 proteins were identified including 254 human, 14 bacterial, 12 fungal, and 7 yeast proteins. Ontology analysis revealed proteins primarily involved in cytoskeletal rearrangements, immune response, antimicrobial function, protein degradation, and DNA binding. There was considerable variation in the number of proteins identified, both among subjects and within subjects across time points. After pooling of samples between subjects at each time point, the levels of 59 proteins in the I-phase and 73 proteins in the R-phase were quantified longitudinally. Our data demonstrate that LC–MS/MS label-free quantitative proteomics is valuable in the assessment of the protein content of the GCF and can facilitate a better understanding of the molecular mechanisms involved in the induction and resolution of plaque-induced gingival inflammation in humans. We investigated the sequential protein expression in gingival crevicular fl uid samples during the induction (I) and resolution (R) of experimental gingivitis. Periodontally and systemically healthy volunteers ( n = 20) participated in a three-week experimental gingivitis protocol, followed by debridement and two weeks of regular plaque control. Gingival crevicular fl uid (GCF) samples were collected at baseline, Day 7, 14, and 21 (induction; I-phase), and at Day 21, 25, 30, and 35 (resolution; R-phase). Liquid chromatography − tandem mass spectrome- try (LC − MS/MS) for label-free quantitative proteomics was applied. A total of 287 proteins were identi fi ed including 254 human, 14 bacterial, 12 fungal, and 7 yeast proteins. Ontology analysis revealed proteins primarily involved in cytoskeletal rearrangements, immune response, antimicrobial function, protein degradation, and DNA binding. There was considerable variation in the number of proteins identi fi ed, both among subjects and within subjects across time points. After pooling of samples between subjects at each time point, the levels of 59 proteins in the I- phase and 73 proteins in the R-phase were quanti fi ed longitudinally. Our data demonstrate that LC − MS/MS label-free quantitative proteomics is valuable in the assessment of the protein content of the GCF and can facilitate a better understanding of the molecular mechanisms involved in the induction and resolution of plaque-induced gingival in fl ammation in humans We investigated the sequential protein expression in gingival crevicular fluid samples during the induction (I) and resolution (R) of experimental gingivitis. Periodontally and systemically healthy volunteers (n = 20) participated in a three-week experimental gingivitis protocol, followed by debridement and two weeks of regular plaque control. Gingival crevicular fluid (GCF) samples were collected at baseline, Day 7, 14, and 21 (induction; I-phase), and at Day 21, 25, 30, and 35 (resolution; R-phase). Liquid chromatography-tandem mass spectrometry (LC-MS/MS) for label-free quantitative proteomics was applied. A total of 287 proteins were identified including 254 human, 14 bacterial, 12 fungal, and 7 yeast proteins. Ontology analysis revealed proteins primarily involved in cytoskeletal rearrangements, immune response, antimicrobial function, protein degradation, and DNA binding. There was considerable variation in the number of proteins identified, both among subjects and within subjects across time points. After pooling of samples between subjects at each time point, the levels of 59 proteins in the I-phase and 73 proteins in the R-phase were quantified longitudinally. Our data demonstrate that LC-MS/MS label-free quantitative proteomics is valuable in the assessment of the protein content of the GCF and can facilitate a better understanding of the molecular mechanisms involved in the induction and resolution of plaque-induced gingival inflammation in humans.We investigated the sequential protein expression in gingival crevicular fluid samples during the induction (I) and resolution (R) of experimental gingivitis. Periodontally and systemically healthy volunteers (n = 20) participated in a three-week experimental gingivitis protocol, followed by debridement and two weeks of regular plaque control. Gingival crevicular fluid (GCF) samples were collected at baseline, Day 7, 14, and 21 (induction; I-phase), and at Day 21, 25, 30, and 35 (resolution; R-phase). Liquid chromatography-tandem mass spectrometry (LC-MS/MS) for label-free quantitative proteomics was applied. A total of 287 proteins were identified including 254 human, 14 bacterial, 12 fungal, and 7 yeast proteins. Ontology analysis revealed proteins primarily involved in cytoskeletal rearrangements, immune response, antimicrobial function, protein degradation, and DNA binding. There was considerable variation in the number of proteins identified, both among subjects and within subjects across time points. After pooling of samples between subjects at each time point, the levels of 59 proteins in the I-phase and 73 proteins in the R-phase were quantified longitudinally. Our data demonstrate that LC-MS/MS label-free quantitative proteomics is valuable in the assessment of the protein content of the GCF and can facilitate a better understanding of the molecular mechanisms involved in the induction and resolution of plaque-induced gingival inflammation in humans. |
Author | Jönsson, Daniel Ramberg, Per Wahlander, Åsa Grossman, Jonas Papapanou, Panos N Barnes, Virginia Monsul Bostanci, Nagihan |
AuthorAffiliation | The Sahlgrenska Academy at Göteborg University Colgate-Palmolive Technology Center Columbia University College of Dental Medicine Functional Genomics Center University of Zurich |
AuthorAffiliation_xml | – name: Colgate-Palmolive Technology Center – name: The Sahlgrenska Academy at Göteborg University – name: University of Zurich – name: Functional Genomics Center – name: Columbia University College of Dental Medicine |
Author_xml | – sequence: 1 givenname: Nagihan surname: Bostanci fullname: Bostanci, Nagihan – sequence: 2 givenname: Per surname: Ramberg fullname: Ramberg, Per – sequence: 3 givenname: Åsa surname: Wahlander fullname: Wahlander, Åsa – sequence: 4 givenname: Jonas surname: Grossman fullname: Grossman, Jonas – sequence: 5 givenname: Daniel surname: Jönsson fullname: Jönsson, Daniel – sequence: 6 givenname: Virginia Monsul surname: Barnes fullname: Barnes, Virginia Monsul – sequence: 7 givenname: Panos N surname: Papapanou fullname: Papapanou, Panos N email: pp192@columbia.edu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23244068$$D View this record in MEDLINE/PubMed https://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-15584$$DView record from Swedish Publication Index https://gup.ub.gu.se/publication/174524$$DView record from Swedish Publication Index |
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Snippet | We investigated the sequential protein expression in gingival crevicular fluid samples during the induction (I) and resolution (R) of experimental gingivitis.... We investigated the sequential protein expression in gingival crevicular fl uid samples during the induction (I) and resolution (R) of experimental gingivitis.... |
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SubjectTerms | Adult Bacterial Proteins - analysis biomarker Chromatography, Liquid cytoskeleton debridement DNA Female Fungal Proteins - analysis Gene Expression Regulation gingival crevicular fluid Gingival Crevicular Fluid - chemistry Gingival Crevicular Fluid - microbiology gingivitis Gingivitis - genetics Gingivitis - metabolism Gingivitis - microbiology Humans immune response inflammation liquid chromatography Male Odontologi Odontology pathogenesis periodontal disease protein content protein degradation protein synthesis proteins proteome Proteome - analysis proteomics Salivary Proteins and Peptides - analysis Tandem Mass Spectrometry yeasts |
Title | Label-Free Quantitative Proteomics Reveals Differentially Regulated Proteins in Experimental Gingivitis |
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