Non-bacterial protein expression in periodontal pockets by proteome analysis
Objectives To compare the proteomic profile of inter‐proximal pocket tissues with inter‐proximal healthy tissues in the same subject to reveal proteins associated with periodontal disease in sites where periodontopathogenic bacteria were not detectable. Methods Twenty‐five healthy patients, with mod...
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Published in | Journal of clinical periodontology Vol. 40; no. 6; pp. 573 - 582 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Blackwell Publishing Ltd
01.06.2013
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Subjects | |
Online Access | Get full text |
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Summary: | Objectives
To compare the proteomic profile of inter‐proximal pocket tissues with inter‐proximal healthy tissues in the same subject to reveal proteins associated with periodontal disease in sites where periodontopathogenic bacteria were not detectable.
Methods
Twenty‐five healthy patients, with moderate‐to‐advanced chronic periodontitis and presenting with at least one intra‐bony defect next to a healthy inter‐proximal site were enrolled. The periodontal defects were treated with osseous resective surgery, and the flap design included both the periodontal pockets and the neighbouring inter‐proximal healthy sites. Pocket‐associated and healthy tissues were harvested for proteomic analyses.
Results
Fifteen proteins were differently expressed between pathological and healthy tissues. In particular, annexin A2, actin cytoplasmic 1, carbonic anhydrase 1 & 2; Ig kappa chain C region (two spots) and flavinreductase were overexpressed, whereas 14‐3‐3 protein sigma and zeta/delta, heat‐shock protein beta ‐1 (two spots), triosephosphateisomerase, peroxiredoxin‐1, fatty acid‐binding protein‐epidermal, and galectin‐7 were underexpressed in pathological tissue.
Conclusions
The unbalanced functional network of proteins involved could hinder adequate tissue response to pathogenic noxa. The study of periodontal pocket tissue proteomic profile would be crucial to better understand the pathogenesis of and the therapeutic strategies for periodontitis. |
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Bibliography: | istex:0550C877D0E583516C8A62C3265A72F988FA3DAC ArticleID:JCPE12050 Table S1. Main physiological functions of proteins found significantly unbalanced between healthy and pathological sites in the same subjects. ark:/67375/WNG-58FQVRX9-2 This study was funded by the authors' own institutions. The authors declare that they have no conflicts of interest. Conflict of interest and sources of funding statement ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
ISSN: | 0303-6979 1600-051X 1600-051X |
DOI: | 10.1111/jcpe.12050 |