Matrix metalloproteinase 10 promotion of collagenolysis via procollagenase activation: Implications for cartilage degradation in arthritis

Barksby, H. E.; Milner, Jennifer M; Patterson, Angela; Peake, Nicholas; Wang, Hui; Robson, Timothy; Lakey, Rachel; Middleton, Jim; Cawston, Tim E.; Richards, Carl D.; Rowan, Andrew D.

doi:10.1002/art.22167

Cited by 109 publications

(107 citation statements)

References 51 publications

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“…MMP10 deficiency in a K-Rasmediated lung cancer model leads to a decrease in tumor burden compared with controls (Regala et al 2011). In addition, MMP10 has also been associated with inflammatory disease, such as arthritis (Barksby et al 2006). Here we show that pharmacological blockers of MMPs in vivo delay the development of the preneoplastic lesions caused by c-fos expression, likely due to inhibition of MMP10, the only MMP/ADAM up-regulated upon c-Fos expression.…”

Section: Discussionmentioning

confidence: 99%

Inflammation-mediated skin tumorigenesis induced by epidermal c-Fos

et al. 2013

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Skin squamous cell carcinomas (SCCs) are the second most prevalent skin cancers. Chronic skin inflammation has been associated with the development of SCCs, but the contribution of skin inflammation to SCC development remains largely unknown. In this study, we demonstrate that inducible expression of c-fos in the epidermis of adult mice is sufficient to promote inflammation-mediated epidermal hyperplasia, leading to the development of preneoplastic lesions. Interestingly, c-Fos transcriptionally controls mmp10 and s100a7a15 expression in keratinocytes, subsequently leading to CD4 T-cell recruitment to the skin, thereby promoting epidermal hyperplasia that is likely induced by CD4 T-cell-derived IL-22. Combining inducible c-fos expression in the epidermis with a single dose of the carcinogen 7,12-dimethylbenz(a)anthracene (DMBA) leads to the development of highly invasive SCCs, which are prevented by using the anti-inflammatory drug sulindac. Moreover, human SCCs display a correlation between c-FOS expression and elevated levels of MMP10 and S100A15 proteins as well as CD4 T-cell infiltration. Our studies demonstrate a bidirectional cross-talk between premalignant keratinocytes and infiltrating CD4 T cells in SCC development. Therefore, targeting inflammation along with the newly identified targets, such as MMP10 and S100A15, represents promising therapeutic strategies to treat SCCs.

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Section: Discussionmentioning

confidence: 99%

Inflammation-mediated skin tumorigenesis induced by epidermal c-Fos

et al. 2013

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“…Recently, Frederick and colleagues (25) reported that MMP-10 contributes to anchorage-independent growth of NSCLC through a PKCι-dependent pathway. Importantly, both MMP-3 and MMP-10 can activate latent MMP-1 (26)(27)(28). Consequently, CEBPB promotes collagenolytic activity both at the level of MMP-1 gene activation and enzymatic activity.…”

Section: Discussionmentioning

confidence: 99%

CCAAT Enhancer Binding Protein-β Regulates Matrix Metalloproteinase-1 Expression in Interleukin-1β–Stimulated A549 Lung Carcinoma Cells

Armstrong¹,

Phelps²,

Vincenti³

2009

Molecular Cancer Research

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Matrix metalloproteinase-1 (MMP-1) is an inflammationinducible neutral protease that mediates extracellular matrix remodeling and promotes tumor invasion. In this study, we examined the activation of MMP-1 gene expression in A549 lung carcinoma cells stimulated with the inflammatory cytokine interleukin-1β (IL-1β). We found that MMP-1 mRNA levels were maximal following 16 hours of IL-1β stimulation and that this correlated with the expression of the transcription factor CCAAT enhancer-binding protein-β (CEBPB). Knockdown of CEBPB expression with short hairpin RNA abrogated the expression of MMP-1, MMP-3, and MMP-10 in IL-1β-stimulated A549 cells. An established CEBP element in the MMP-1 promoter was found to be required for basal and IL-1β-induced transcription. Electrophoresis mobility shift assays showed that CEBPB binds to this promoter element maximally 16 hours after IL-1β stimulation. DNA affinity chromatography studies showed that the LAP1, LAP2, and LIP isoforms of CEBPB bind to the IL-1β-responsive CEBPB site in the MMP-1 promoter. Exogenous expression of the LAP1 and LAP2 isoforms stimulated the MMP-1 promoter, whereas LIP had no effect. Phosphorylation of CEBPB at Thr 235 peaked at 16 hours in IL-1β-stimulated cells. The MEK inhibitor U0126 inhibited this phosphorylation and reduced MMP-1 gene induction. These studies establish CEBPB as an important mediator of metalloproteinase gene activation during inflammatory responses in lung cancer cells and highlight the different regulatory roles of CEBPB isoforms. (Mol Cancer Res 2009;7(9):1517-24)

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“…Inflammatory stimuli induce its release by synovial fibroblasts, whereas treatment with pro-catabolic elements stimulates expression by articular chondrocytes (Barksby et al, 2006). The physiopathological relevance of MMP-10 has been associated to vascular development, atherothrombosis , skin wound healing and cell migration, since it is primarily found at the front of the migrating epithelial 'tongue' (Madlener and Werner, 1997) and it has been observed in migrating enterocytes in inflammatory bowel disease Vaalamo et al, 1998).…”

Section: Biological Aspectsmentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

204

209

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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Matrix metalloproteinase 10 promotion of collagenolysis via procollagenase activation: Implications for cartilage degradation in arthritis

Cited by 109 publications

References 51 publications

Inflammation-mediated skin tumorigenesis induced by epidermal c-Fos

Inflammation-mediated skin tumorigenesis induced by epidermal c-Fos

CCAAT Enhancer Binding Protein-β Regulates Matrix Metalloproteinase-1 Expression in Interleukin-1β–Stimulated A549 Lung Carcinoma Cells

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

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