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MMP8 — TGFB1

Text-mined interactions from Literome

Gallery et al., Microvasc Res 1999 (Pre-Eclampsia...) : Neither tumor necrosis factor-alpha nor transforming growth factor-beta , both thought to have significant roles in the control of placentation, affected MMP secretion
Meisser et al., Mol Hum Reprod 1999 : The aim of this study was to determine the effects of tumour necrosis factor alpha (TNF), interleukin-1 alpha (IL-1alpha), macrophage colony stimulating factor ( MCSF ) and transforming growth factor beta ( TGFbeta ) on the secretion of matrix metalloproteinases ( MMP ) , human chorionic gonadotrophin ( HCG ) and fetal fibronectin ( fFN ) by purified first trimester cytotrophoblastic cells (CTB) in vitro
Duivenvoorden et al., Clin Exp Metastasis 1999 (Bone Neoplasms) : MMP activity can be down-regulated by transforming growth factor beta1 ( TGF-beta1 ), a growth modulating factor, found in high concentrations in the bone ... Data presented in this paper support the hypothesis that TGF-beta1 can potentially disrupt the balance existing between osteoclast- and osteoblast derived MMP activity by inducing altered expression of matrix metalloproteinases and their tissue inhibitors derived from bone metastasizing cancer cells
Ma et al., Wound Repair Regen 1999 : In conclusion, these results indicate that mesothelial cells express MMP and TIMP mRNA and protein, and their expression is differentially regulated by transforming growth factor-beta1 , a mechanism that in part may influence the outcome of peritoneal tissue repair and adhesion formation
Nuttall et al., Endocrinology 2000 : There was no effect of these growth factors on gelatinase or TIMP-1, -2, and -3, nor was there an effect of transforming growth factor-beta on any MMP or TIMP examined
Palosaari et al., J Dent Res 2000 : The expression of MMP-8 in human odontoblasts and dental pulp cells is down-regulated by TGF-beta1
Parkin et al., Eur J Ophthalmol 2000 (Keratoconus) : It is known that platelet derived growth factor ( PDGF ) and transforming growth factor-beta ( TGF-beta ) are involved in the regulation of MMP activity and tissue inhibitor of metalloproteinase ( TIMP ) production in non-ocular tissues
Maeda et al., J Bone Miner Res 2001 : Taken together, the results of the current study show that matrix vesicles produced by growth plate chondrocytes contain MMP-3, that this enzyme is at least partially responsible for activation of small latent TGF-beta1 in the matrix, and that 1alpha,25 ( OH ) 2D3 regulates MMP release from matrix vesicles
Shek et al., Am J Pathol 2002 (Chronic Disease...) : We have examined MMP and TIMP synthesis by transformed cultured pancreatic stellate cells and their regulation by TGF-beta 1
Cotrim et al., J Periodontol 2002 (Gingival Overgrowth) : To determine the effect of TGF-beta1 on the expression of MMP and TIMP by human gingival fibroblasts under CsA treatment, human gingival fibroblast cultures were treated with sense oligonucleotides (SON) or antisense oligonucleotides ( AON )
Stawowy et al., Cardiovasc Res 2004 : We demonstrate that TGF-beta1 induces MMP-activity in CFBs, thereby facilitating CFBs motility
Munshi et al., J Biol Chem 2004 (Carcinoma, Squamous Cell...) : Because transforming growth factor-beta1 ( TGF-beta1 ) promotes tumor invasion in advanced squamous cell carcinomas, the role of TGF-beta1 in the regulation of MMP activity in a cellular model of invasive oral squamous cell carcinoma was examined
Vesey et al., Kidney Int 2005 (Calcium Signaling...) : These responses which are dependent on its protease activity appear not to be mediated by PAR-1 activation, the autocrine action of thrombin induced TGF-beta1 secretion, MMP activation , or EGF receptor transactivation
Wang et al., Proc Natl Acad Sci U S A 2005 (Emphysema) : Furthermore, exogenous TGF-beta1 potentially rescued emphysema-like phenotype and concomitantly reduced MMP expression in Fut8 ( -/- ) lung
Zhang et al., Zhonghua Fu Chan Ke Za Zhi 2006 (Ovarian Neoplasms) : Ovarian carcinoma cells activate HPMC through TGF-beta1 , which induces higher expressions of MMP of ovarian carcinoma cells
Wang et al., Arterioscler Thromb Vasc Biol 2006 : Thus, MMP-2 activated TGF-beta1 , and subsequently TbetaRII signaling, is a novel molecular mechanism for arterial aging
García-Alvarez et al., Sarcoidosis Vasc Diffuse Lung Dis 2006 (Pulmonary Fibrosis) : In lung fibroblasts, TGF-beta1 induced a strong upregulation of MT3-MMP , both at the gene and protein level
Krag et al., Nephrol Dial Transplant 2007 (Body Weight) : Moreover, high BG exaggerated TGF-beta1 induced changes in the BMT, MMP-2 and TIMP-1 expression and pERK1/2 staining
Zhang et al., Hepatogastroenterology 2007 (Disease Models, Animal...) : TGF-beta1 , MMP-2 and TIMP-1 mRNA in HSCs increased obviously during the course of hepatic fibrosis, and their levels were decreased after the treatment with IL-10 ( P < 0.05 )
Do et al., Mol Cancer Res 2008 (Neoplasm Metastasis...) : When cancer cells were cultured on plastic, TGF-beta1 , TGF-beta2, and TGF-beta3 induced pro-matrix metalloproteinase ( MMP ) secretion, loss of cell-cell junctions, down-regulation of E-cadherin, up-regulation of N-cadherin, and acquisition of a fibroblastoid phenotype, consistent with an epithelial-to-mesenchymal transition ... When cancer cells were cultured on a three-dimensional collagen matrix, TGF-beta1 , TGF-beta2, and TGF-beta3 stimulated both pro-MMP and active MMP secretion and invasion
Nilsson et al., Exp Cell Res 2009 (Breast Neoplasms...) : Inhibition of MMP activity restored TGF-beta1 levels, suggesting an involvement of MMP activities in the down-regulation of TGF-beta1 by tamoxifen
Edwards et al., Exp Gerontol 1996 : We conclude that the effects of TGF beta 1 on MMP and TIMP gene expression involve different cellular intermediaries, and suggest that altered composition or modification of TIE binding factors in aging cells may underlie the failure of TGF beta 1-mediated transcription repression
Uitto et al., Am J Pathol 1998 (Gingivitis...) : In these cells, MMP-13 expression at the mRNA and protein level was potently enhanced ( up to sixfold ) by tumor necrosis factor-alpha, transforming growth factor-beta(1) , and transforming growth factor-alpha and by keratinocyte growth factor in the presence of heparin