Induction of matrix metalloproteinase 1 gene expression is regulated by inflammation‐responsive transcription factor SAF‐1 in osteoarthritis

Ray, Alpana; Kuroki, Keiichi; Cook, James L.; Bal, B. Sonny; Kenter, Keith; Aust, Gabriela; Ray, Bimal K.

doi:10.1002/art.10706

Cited by 33 publications

(43 citation statements)

References 40 publications

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“…MMP-1 activity was increased in the synovial fluid of OA joints in horses (Brama et al, 2004). Overexpression of serum amyloid A-activating factor 1 in OA chondrocytes increased the expression of the MMP-1 promoter; thus, serum amyloid A-activating factor 1 may be a therapeutic target for controlling the overexpression of MMP-1 in OA (Ray et al, 2003). Increased MMP-3 can induce matrix degradation of articular cartilage in mature bovines (Lin et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Increased serum ADAMTS-4 in knee osteoarthritis: a potential indicator for the diagnosis of osteoarthritis in early stages

Li¹,

Du²,

Wang³

et al. 2014

Genet. Mol. Res.

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ABSTRACT. We compared serum levels of a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-4, ADAMTS-5, matrix metalloproteinase (MMP)-1, and MMP-3 in patients with different stages of knee osteoarthritis (OA), and investigated the clinical significance of diagnosing OA in early stages. OA patients were divided into 2 groups: early OA group (44 cases), intermediate and advanced OA group (26 cases). The healthy control group included 30 samples. ADAMTS-4, ADAMTS-5, MMP-1, and MMP-3 levels in the serum were tested using an enzyme-linked immunosorbent assay. A protein-protein interaction network was constructed by seeding the significantly expressed marker, followed by Gene Ontology enrichment analyses using Database for Annotation, Visualization and Integrated Discovery. ADAMTS-4 levels were significantly higher in patients at early stages of OA compared to intermediate or advanced OA and healthy controls. ADAMTS-5, MMP-1, and MMP-3 levels in intermediate and advanced-stage OA patients were significantly higher than those in early-stage OA patients and healthy controls. The proteinprotein interaction network showed that ADAMTS-4 participates in

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Section: Discussionmentioning

confidence: 99%

Increased serum ADAMTS-4 in knee osteoarthritis: a potential indicator for the diagnosis of osteoarthritis in early stages

Li¹,

Du²,

Wang³

et al. 2014

Genet. Mol. Res.

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“…A region of the MMP-1 promoter (Ϫ153 to ϩ3) known to respond to mitogenic signaling was employed (30). 24 h after the transfection, cell cultures were either treated or not treated with the ligand collagen.…”

Section: Ddr2 Y740f Mutation Induces Mmp-1 Promoter Activity and Stimmentioning

confidence: 99%

Tyrosine 740 Phosphorylation of Discoidin Domain Receptor 2 by Src Stimulates Intramolecular Autophosphorylation and Shc Signaling Complex Formation

Yang

Kim

et al. 2005

Journal of Biological Chemistry

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DDR2 is a receptor tyrosine kinase whose activating ligands are various collagens. DDR2-mediated cellular signaling has been shown to require Src activity. However, the precise mechanism underlying the Src dependence of DDR2 signaling is unknown. Here, using baculoviral co-expression of the DDR2 cytosolic domain and Src, we show that Src targets three tyrosine residues (Tyr-736, Tyr-740, and Tyr-741) in the activation loop of DDR2 for phosphorylation. This phosphorylation by Src stimulates DDR2 cisautophosphorylation of additional tyrosine residues. In vitro Shc binding assays demonstrate that phosphotyrosines resulting from DDR2 autophosphorylation are involved in Shc binding to the DDR2 cytosolic domain. Mutating tyrosine 740 of DDR2 to phenylalanine stimulates autophosphorylation of DDR2 to an extent similar to that resulting from Src phosphorylation of DDR2. In addition, the DDR2 Y740F mutant protein displays collagenindependent, constitutively activated signaling. These findings suggest that tyrosine 740 inhibits DDR2 autophosphorylation. Collectively, our findings are consistent with the following mechanism for Src-dependent DDR2 activation and signaling: 1) ligand binding promotes phosphorylation of Tyr-740 in the DDR2 activation loop by Src; 2) Tyr-740 phosphorylation stimulates intramolecular autophosphorylation of DDR2; 3) DDR2 autophosphorylation generates cytosolic domain phosphotyrosines that promote the formation of DDR2 cytosolic domain-Shc signaling complexes. The discoidin domain receptor (DDR)2 family, including DDR1 and DDR2, belongs to receptor tyrosine kinases (RTKs) family. Its extracellular part, containing the so-called discoidin domain, binds to various collagen proteins as their activating ligands (1-3), and its intracellular part possesses a domain of tyrosine kinase, which shares ϳ50% sequence homology with that of the Trk family of neurotrophin receptors as well as with insulin receptor (4 -6).Involvement of DDR proteins in the proliferation of various cell types has been reported. Increased DDR1 expression is observed in keratinocytes of the skin and smooth muscle cells around blood vessels when the tissues are injured (7,8). DDR1 is also expressed in monocyte-derived cells where it is believed to play a role in collagen binding and cell differentiation (9, 10). DDR2 expression is observed in mesenchymal cells and is involved in bone growth (11). During liver fibrosis, induction and activation of DDR2 occur in liver stellate cells, and its tyrosine kinase activity is necessary for the proliferation of stellate cells and for the increase of collagen and MMP-2 synthesis (12, 13). In rheumatoid arthritis, DDR2 induction is also observed in activated synovial fibroblasts and is thought to stimulate the growth of these cells and MMP-1 synthesis (14). In addition, the induction of DDR proteins is implicated in breast and ovarian cancer, and is correlated with metastasis (15, 16).Autophosphorylation of the cytosolic domain of RTKs is typically a critical event for the activation of RTK-med...

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“…A prominent characteristic of rheumatoid arthritis is an increase in the numbers of synovial fibroblasts, which produce proinflammatory cytokines and matrix metalloproteinases (MMPs) that erode bone and destroy cartilage (1,2). In recent studies, serum amyloid A-activating factor 1 (SAF-1) an inflammation-responsive transcription factor, was identified as a critical regulator of MMP-1 gene induction in chondrocytes and synovial fibroblast cells (3). SAF-1 belongs to a family of zinc finger proteins, and its human and mouse homologues are identified as MAZ (4) and Pur-1 (5), respectively.…”

Section: R Heumatoid Arthritis (Ra)mentioning

confidence: 99%

“…Although it is suggested that a modest increase in SAF-1 activity during chronic inflammation would increase the expression of its target genes (12), relatively little is known about the cellular consequences if this protein is significantly overproduced. Indeed, significant overexpression of SAF-1 has recently been seen in osteoarthritic cartilage tissue (3). To examine this, we overexpressed SAF-1 in the cells and monitored their fate.…”

Section: R Heumatoid Arthritis (Ra)mentioning

confidence: 99%

Overexpression of Serum Amyloid A-Activating Factor 1 Inhibits Cell Proliferation by the Induction of Cyclin-Dependent Protein Kinase Inhibitor p21WAF-1/Cip-1/Sdi-1 Expression

Ray

Shakya

Kumar

et al. 2004

The Journal of Immunology

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Inflammation-responsive transcription factor, serum amyloid A-activating factor 1 (SAF-1), has been shown to regulate several genes, including serum amyloid A, γ-fibrinogen, and matrix metalloproteinase 1, whose abnormal expression is associated with the pathogenesis of arthritis, atherosclerosis, and amyloidosis. Prolonged high level expression of SAF-1 in cultured cells failed to produce any stable cell line that overexpresses SAF-1. To test the fate of SAF-1-overexpressing cells, the cells were monitored for growth and morphological changes over time. The cells that were programmed to overproduce SAF-1 were found to undergo growth arrest and reduce DNA synthesis within 3 days after transfection. These cells undergo marked morphological changes from typical fibroblasts to round morphology and gradually cease to exist. Microarray analysis for cell cycle-specific genes in SAF1-transfected cells identified several candidate genes whose expression levels were altered during SAF-1 overexpression. Cdk inhibitor protein p21 was significantly affected by SAF-1; its expression level was highly induced by cellular conditions where SAF-1 is abundant. The increased level of p21 in the cell drives it to a growth arrest mode, a condition previously found to be controlled by p53. In this study we provide evidence that, similar to p53, SAF-1 is able to activate p21 gene expression by promoting transcription directly via its interaction with the p21 promoter. Together these data indicate that SAF-1 controls cell cycle progression via p21 induction, and pathophysiological conditions that favor overexpression of SAF-1, such as an acute inflammatory condition, can trigger cellular growth arrest.

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Induction of matrix metalloproteinase 1 gene expression is regulated by inflammation‐responsive transcription factor SAF‐1 in osteoarthritis

Cited by 33 publications

References 40 publications

Increased serum ADAMTS-4 in knee osteoarthritis: a potential indicator for the diagnosis of osteoarthritis in early stages

Increased serum ADAMTS-4 in knee osteoarthritis: a potential indicator for the diagnosis of osteoarthritis in early stages

Tyrosine 740 Phosphorylation of Discoidin Domain Receptor 2 by Src Stimulates Intramolecular Autophosphorylation and Shc Signaling Complex Formation

Overexpression of Serum Amyloid A-Activating Factor 1 Inhibits Cell Proliferation by the Induction of Cyclin-Dependent Protein Kinase Inhibitor p21WAF-1/Cip-1/Sdi-1 Expression

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