Expression of extracellular matrix metalloproteinase inducer glycosylation and caveolin-1 in healthy and inflamed human gingiva

Background and Objective Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin‐1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin‐1 expression in healt...

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Published inJournal of periodontal research Vol. 49; no. 2; pp. 197 - 204
Main Authors Wang, J., Yang, D., Li, C., Shang, S., Xiang, J.
Format Journal Article
LanguageEnglish
Published United States Blackwell Publishing Ltd 01.04.2014
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ISSN0022-3484
1600-0765
1600-0765
DOI10.1111/jre.12095

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Abstract Background and Objective Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin‐1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin‐1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin‐1 expression, and assessed how this interaction influenced MMP‐1 production. Material and Methods Gingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis (chronic periodontitis) subjects. EMMPRIN, caveolin‐1 and MMP‐1 expressions were analyzed by immunohistochemistry. EMMPRIN and caveolin‐1 co‐localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin‐1, active MMP‐1 and proMMP‐1 expression was assessed by Western blot. Results EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast‐like cells. Strong caveolin‐1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin‐1 co‐localization in gingival epithelium, endothelial and fibroblast‐like cells. Compared with healthy subjects, the chronic periodontitis group had increased high‐glycoform EMMPRIN (HG‐EMMPRIN) and active MMP‐1 expression (p < 0.05). Active MMP‐1 and proMMP‐1 protein levels were positively correlated with HG‐EMMPRIN levels (p < 0.05). Conclusion EMMPRIN and caveolin‐1 colocalize in periodontal tissues. The increased active MMP‐1 and proMMP‐1 production may be associated with elevated HG‐EMMPRIN levels.
AbstractList Background and Objective Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin‐1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin‐1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin‐1 expression, and assessed how this interaction influenced MMP‐1 production. Material and Methods Gingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis (chronic periodontitis) subjects. EMMPRIN, caveolin‐1 and MMP‐1 expressions were analyzed by immunohistochemistry. EMMPRIN and caveolin‐1 co‐localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin‐1, active MMP‐1 and proMMP‐1 expression was assessed by Western blot. Results EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast‐like cells. Strong caveolin‐1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin‐1 co‐localization in gingival epithelium, endothelial and fibroblast‐like cells. Compared with healthy subjects, the chronic periodontitis group had increased high‐glycoform EMMPRIN (HG‐EMMPRIN) and active MMP‐1 expression (p < 0.05). Active MMP‐1 and proMMP‐1 protein levels were positively correlated with HG‐EMMPRIN levels (p < 0.05). Conclusion EMMPRIN and caveolin‐1 colocalize in periodontal tissues. The increased active MMP‐1 and proMMP‐1 production may be associated with elevated HG‐EMMPRIN levels.
Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin-1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin-1 expression, and assessed how this interaction influenced MMP-1 production. Gingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis (chronic periodontitis) subjects. EMMPRIN, caveolin-1 and MMP-1 expressions were analyzed by immunohistochemistry. EMMPRIN and caveolin-1 co-localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin-1, active MMP-1 and proMMP-1 expression was assessed by Western blot. EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast-like cells. Strong caveolin-1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin-1 co-localization in gingival epithelium, endothelial and fibroblast-like cells. Compared with healthy subjects, the chronic periodontitis group had increased high-glycoform EMMPRIN (HG-EMMPRIN) and active MMP-1 expression (p < 0.05). Active MMP-1 and proMMP-1 protein levels were positively correlated with HG-EMMPRIN levels (p < 0.05). EMMPRIN and caveolin-1 colocalize in periodontal tissues. The increased active MMP-1 and proMMP-1 production may be associated with elevated HG-EMMPRIN levels.
Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin-1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin-1 expression, and assessed how this interaction influenced MMP-1 production.BACKGROUND AND OBJECTIVEGlycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin-1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin-1 expression, and assessed how this interaction influenced MMP-1 production.Gingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis (chronic periodontitis) subjects. EMMPRIN, caveolin-1 and MMP-1 expressions were analyzed by immunohistochemistry. EMMPRIN and caveolin-1 co-localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin-1, active MMP-1 and proMMP-1 expression was assessed by Western blot.MATERIAL AND METHODSGingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis (chronic periodontitis) subjects. EMMPRIN, caveolin-1 and MMP-1 expressions were analyzed by immunohistochemistry. EMMPRIN and caveolin-1 co-localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin-1, active MMP-1 and proMMP-1 expression was assessed by Western blot.EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast-like cells. Strong caveolin-1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin-1 co-localization in gingival epithelium, endothelial and fibroblast-like cells. Compared with healthy subjects, the chronic periodontitis group had increased high-glycoform EMMPRIN (HG-EMMPRIN) and active MMP-1 expression (p < 0.05). Active MMP-1 and proMMP-1 protein levels were positively correlated with HG-EMMPRIN levels (p < 0.05).RESULTSEMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast-like cells. Strong caveolin-1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin-1 co-localization in gingival epithelium, endothelial and fibroblast-like cells. Compared with healthy subjects, the chronic periodontitis group had increased high-glycoform EMMPRIN (HG-EMMPRIN) and active MMP-1 expression (p < 0.05). Active MMP-1 and proMMP-1 protein levels were positively correlated with HG-EMMPRIN levels (p < 0.05).EMMPRIN and caveolin-1 colocalize in periodontal tissues. The increased active MMP-1 and proMMP-1 production may be associated with elevated HG-EMMPRIN levels.CONCLUSIONEMMPRIN and caveolin-1 colocalize in periodontal tissues. The increased active MMP-1 and proMMP-1 production may be associated with elevated HG-EMMPRIN levels.
Background and Objective Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its ability to induce matrix metalloproteinases (MMPs) production. This study investigated EMMPRIN glycosylation and caveolin-1 expression in healthy and inflamed human gingival tissues, analyzed the relationship between EMMPRIN glycosylation and caveolin-1 expression, and assessed how this interaction influenced MMP-1 production. Material and Methods Gingival tissues were collected from 10 healthy subjects and 15 chronic periodontitis (chronic periodontitis) subjects. EMMPRIN, caveolin-1 and MMP-1 expressions were analyzed by immunohistochemistry. EMMPRIN and caveolin-1 co-localization was detected by immunofluorescence. EMMPRIN glycosylation, caveolin-1, active MMP-1 and proMMP-1 expression was assessed by Western blot. Results EMMPRIN was expressed in gingival epithelial cells, inflammatory cells, endothelial and fibroblast-like cells. Strong caveolin-1 immunoreactivity was detected in gingival epithelial and endothelial cells. Double immunofluorescence studies revealed EMMPRIN and caveolin-1 co-localization in gingival epithelium, endothelial and fibroblast-like cells. Compared with healthy subjects, the chronic periodontitis group had increased high-glycoform EMMPRIN (HG-EMMPRIN) and active MMP-1 expression (p < 0.05). Active MMP-1 and proMMP-1 protein levels were positively correlated with HG-EMMPRIN levels (p < 0.05). Conclusion EMMPRIN and caveolin-1 colocalize in periodontal tissues. The increased active MMP-1 and proMMP-1 production may be associated with elevated HG-EMMPRIN levels.
Author Li, C.
Xiang, J.
Wang, J.
Yang, D.
Shang, S.
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Keywords Caveolin-1
EMMPRIN
glycosylation
MMP-1
periodontitis
Language English
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Snippet Background and Objective Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin‐1 and influences its...
Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its ability to induce matrix...
Background and Objective Glycosylated extracellular matrix metalloproteinase inducer (EMMPRIN) is specifically associated with caveolin-1 and influences its...
SourceID proquest
pubmed
wiley
istex
SourceType Aggregation Database
Index Database
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StartPage 197
SubjectTerms Adolescent
Adult
Basigin - analysis
Caveolin 1 - analysis
Caveolin-1
Chronic Periodontitis - metabolism
Chronic Periodontitis - pathology
Dental Plaque Index
EMMPRIN
Endothelial Cells - chemistry
Endothelium, Vascular - chemistry
Epithelial Cells - chemistry
Female
Fibroblasts - chemistry
Gingiva - chemistry
Gingiva - cytology
Glycosylation
Humans
Male
Matrix Metalloproteinase 1 - analysis
Middle Aged
MMP-1
Periodontal Attachment Loss - classification
Periodontal Index
Periodontal Pocket - classification
periodontitis
Young Adult
Title Expression of extracellular matrix metalloproteinase inducer glycosylation and caveolin-1 in healthy and inflamed human gingiva
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https://www.ncbi.nlm.nih.gov/pubmed/23647605
https://www.proquest.com/docview/1508425029
https://www.proquest.com/docview/1891867687
Volume 49
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