Nicotine increases the collagen‐degrading ability of human gingival fibroblasts

Zhou, Jiejie; Olson, Byron L.; Windsor, L. Jack

doi:10.1111/j.1600-0765.2006.00937.x

Cited by 47 publications

(63 citation statements)

References 43 publications

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“…Specific inhibitors of gelatinases (MMP-2 and MMP-9), stromelysins (MMP-3), had only a mild effect on sEndoglin release, whereas a collagenase inhibitor (MMP-13) did not affect sEndoglin levels at all. This indicated that these classes of MMPs were probably not involved in the shedding process and suggested membrane-type MMPs to be the primary endoglin shedding candidates because they are inhibited by these broad-spectrum inhibitors (29).…”

Section: Resultsmentioning

confidence: 99%

Matrix Metalloproteinase-14 (MT1-MMP)–Mediated Endoglin Shedding Inhibits Tumor Angiogenesis

et al. 2010

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Endoglin is a transforming growth factor-β coreceptor with a crucial role in angiogenesis. A soluble form of endoglin is present in the circulation, but the role of soluble endoglin (sEndoglin) is poorly understood. In addition, the endoglin shedding mechanism is not known. Therefore, we examined the role of sEndoglin in tumor angiogenesis and the mechanism by which the extracellular domain of endoglin is released from the membrane. In colorectal cancer specimens, we observed high endothelial endoglin protein expression, accompanied with slightly lower sEndoglin levels in the circulation, compared with healthy controls. In vitro analysis using endothelial sprouting assays revealed that sEndoglin reduced spontaneous and vascular endothelial growth factorinduced endothelial sprouting. Human umbilical vascular endothelial cells were found to secrete high levels of sEndoglin. Endoglin shedding was inhibited by matrix metalloproteinase (MMP) inhibitors and MMP

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Section: Resultsmentioning

confidence: 99%

Matrix Metalloproteinase-14 (MT1-MMP)–Mediated Endoglin Shedding Inhibits Tumor Angiogenesis

et al. 2010

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“…The direction of collagen fibers may have an affect on periodontal tissue resistance due to affecting the adhesiveness to root surface (22,34). Zhou et al (42) reported nicotine and P. gingivalis had an additive effect on human gingival fibroblast-mediated collagen degradation and these findings help to explain why smoking is a major factor contributing to the initiation and/or exacerbation of periodontal diseases. In the current study, before being incubated in the culture of the smoking patient, EMD granules were seen in their globular structure but the rareness of the web structure and the globules were less than in the non-smoking patient, and the collagen fibers gave a tight packaged thick fiber view.…”

Section: Resultsmentioning

confidence: 95%

Effect of Smoking on Attachment of Human Periodontal Ligament Cells to Periodontally Involved Root Surfaces Following Enamel Matrix Derivative Application

Kesim

KILIÇ

Özdamar

et al. 2012

Biotechnology & Biotechnological Equipment

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“…With respect to the oral cavity, isolated nicotine has been implicated in affecting gingival fibroblast cell viability 4 tissue remodeling, 5 cell adhesion and migration 6 and myofibroblast transition.…”

Section: Introductionmentioning

confidence: 99%

Effects of Cotinine on Human Gingival Fibroblast Migration

Wheater¹,

Mouabbi²

2015

Dent Open J

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Nicotine has a deleterious impact on gingival fibroblast cell viability, adhesion, and migration. Less is known regarding the effect of cotinine, the main metabolite of nicotine, on such processes. The objective of this study was to determine if cotinine affects the adhesion or migration of Human Gingival Fibroblasts (HGF) in culture. HGF were treated with nicotine or cotinine at several concentrations and dose-response cytotoxicity was determined by MTT assay. The effects of nicotine and cotinine on HGF adhesion were measured colorimetrically and cell migration was determined using the scratch wound assay. The number of HGF oriented parallel to the wound edge at 24 hours was counted using phase contrast images. Data were analyzed using ANOVA and Dunnet's multiple comparison post-test. At the highest concentrations of cotinine (640 ng/ml) and nicotine (400 µg/ml) both HGF survival and cell adhesion were significantly inhibited (p<0.01). By scratch wound assay HGF migration from the wound edge at 24 hours was significantly inhibited by 320 ng/ml (p<0.001) and 640 ng/ml (p<0.001) cotinine, and by 400 µg/ml (p<0.01) nicotine. HGF migration was significantly inhibited by 80 ng/ml (p<0.05), 320 ng/ml (p<0.01) and 640 ng/ml (p<0.001) cotinine and by 100 µg/ml (p<0.01), 200 µg/ml (p<0.01) and 400 µg/ml (p<0.001) nicotine at 48 hours. Significantly more HGF were oriented parallel to wound edge with pre treatment of 10 ng/ml cotinine or 50 µg/ml nicotine before wounding (p<0.001). In HGF exposed to nicotine (400 µg/ml) or cotinine (640 ng/ml), cell survival, cell adhesion, and migration were significantly decreased, but cell polarity was not affected. These concentrations are within ranges of serum levels in smokers, providing evidence that multiple cellular aspects of wound healing are compromised in tobacco users.

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Nicotine increases the collagen‐degrading ability of human gingival fibroblasts

Abstract: Nicotine increased human gingival fibroblast-mediated collagen degradation, in part through the activation of membrane-associated MMPs. Nicotine and P. gingivalis had an additive effect on human gingival fibroblast-mediated collagen degradation.

Cited by 47 publications

References 43 publications

Matrix Metalloproteinase-14 (MT1-MMP)–Mediated Endoglin Shedding Inhibits Tumor Angiogenesis

Matrix Metalloproteinase-14 (MT1-MMP)–Mediated Endoglin Shedding Inhibits Tumor Angiogenesis

Effect of Smoking on Attachment of Human Periodontal Ligament Cells to Periodontally Involved Root Surfaces Following Enamel Matrix Derivative Application

Effects of Cotinine on Human Gingival Fibroblast Migration

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