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Journal ArticleDOI

Increased tissue inhibitor of metalloproteinase-1 expression and inhibition of gelatinase A activity in buccal mucosal fibroblasts by arecoline as possible mechanisms for oral submucous fibrosis

Yu-Chao Chang, +4 more
- 01 Feb 2002 - 
- Vol. 38, Iss: 2, pp 195-200
TLDR
It was found that arecoline acted not only as an inhibitor on gelatinolytic activity of MMP-2, but also a stimulator for TIMP-1 activity, which may contribute to the ECM components accumulation in the areca quid associated OSF.
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This article is published in Oral Oncology.The article was published on 2002-02-01. It has received 103 citations till now. The article focuses on the topics: Arecoline & Oral submucous fibrosis.

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Citations
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Journal ArticleDOI

Oral submucous fibrosis: review on aetiology and pathogenesis.

TL;DR: Current evidence implicates collagen-related genes in the susceptibility and pathogenesis of OSF and the individual mechanisms operating at various stages of the disease-initial, intermediate and advanced need further study in order to propose appropriate therapeutic interventions.
Journal ArticleDOI

Alert for an epidemic of oral cancer due to use of the betel quid substitutes gutkha and pan masala: a review of agents and causative mechanisms

TL;DR: Evidence that strongly supports causative mechanisms for genotoxicity and carcinogenicity of these substitute products, including gutkha and pan masala, are strongly implicated in the recent increase in the incidence of oral submucous fibrosis is reviewed.
Journal ArticleDOI

Molecular pathogenesis of oral submucous fibrosis--a collagen metabolic disorder.

TL;DR: The objectives of this review are to highlight the molecular events involved in the overproduction of insoluble collagen and decreased degradation of collagen occurring via exposure to BQ and stimulation of the TGF-beta pathway, and elucidate the cell signaling that is involved inThe etiopathogenesis of the disease process.
Journal ArticleDOI

Areca nut in pathogenesis of oral submucous fibrosis: revisited.

TL;DR: An overview on the role of areca nut in the pathogenesis and malignant potential of oral submucous fibrosis is given.
Journal ArticleDOI

Arecoline-induced myofibroblast transdifferentiation from human buccal mucosal fibroblasts is mediated by ZEB1

TL;DR: The data suggest that ZEB1 may participate in the pathogenesis of areca quid–associated OSF by activating the α‐SMA promoter and inducing myofibroblast transdifferentiation from BMFs.
References
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Journal ArticleDOI

Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.

TL;DR: This review describes the members of the matrixin family and discusses substrate specificity, domain structure and function, the activation of proMMPs, the regulation of matrixin activity by tissue inhibitors of metalloproteinases, and their pathophysiological implication.
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Matrix metalloproteinases and their inhibitors in connective tissue remodeling.

TL;DR: Latency is overcome by physical, chemical, and enzymatic treatments that separate the cysteine residue from the zinc Expression of the metalloproteinases is switched on by a variety of agents acting through regulatory elements of the gene, particularly the AP‐1 binding site.
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Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates.

TL;DR: A new technique is described for the electrophoretic analysis of plasminogen activators in sodium dodecyl sulfate-polyacrylamide gels containing copolymerized pl asminogen and gelatin, which can be used to detect as little as 1 mU of urokinase and effectively distinguishes between melanoma- and u rokinase-type plasmineg activators.
Journal Article

Tissue inhibitors of metalloproteinases: structure, regulation and biological functions.

TL;DR: The main aim of this article is to review recent literature on TIMPs with special emphasis on their biological activities and the possibility that they may have paradoxical roles in tumor progression.
Journal ArticleDOI

Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells A possible new growth factor in serum

TL;DR: Human tissue inhibitor of metalloproteinases‐1 (TIMP‐1), but not TIMP‐2, has potent growth‐promoting activity for a wide range of human and bovine cells, but TIMP-1 seems to be a new cell‐growth factor in serum and to stimulate the cells independently of its inhibitory activity.
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