Integration of the NF-κB and mitogen-activated protein kinase/AP-1 pathways at the Collagenase-1 promoter: Divergence of IL-1 and TNF-dependent signal transduction in rabbit primary synovial fibroblasts

Barchowsky, Aaron; Frleta, Davor; Vincenti, Matthew P.

doi:10.1006/cyto.2000.0743

Cited by 148 publications

(123 citation statements)

References 44 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…Consistent with a prior report (38), IL-1␤ was a more effective stimulus, and TNF-␣ stimulation of ERK did not independently reach statistical significance (IL-1␤ stimulation of ERK 2, 150 Ϯ 16% control, p ϭ 0.027; TNF-␣ stimulation of ERK 2, 128 Ϯ 22% control, p ϭ 0.146) (Fig. 1, A and C).…”

Section: Activation Of Erk By Il-1␤ and Tnf-␣ In Flscssupporting

confidence: 90%

Cyclooxygenase-2-Derived E Prostaglandins Down-Regulate Matrix Metalloproteinase-1 Expression in Fibroblast-Like Synoviocytes via Inhibition of Extracellular Signal-Regulated Kinase Activation

Pillinger

Rosenthal

Tolani

et al. 2003

The Journal of Immunology

View full text Add to dashboard Cite

We examined the regulation of matrix metalloproteinase (MMP) production by mitogen-activated protein kinases and cyclooxygenases (COXs) in fibroblast-like synoviocytes (FLSCs). IL-1β and TNF-α stimulated FLSC extracellular signal-regulated kinase (ERK) activation as well as MMP-1 and -13 release. Pharmacologic inhibitors of ERK inhibited MMP-1, but not MMP-13 expression. Whereas millimolar salicylates inhibited both ERK and MMP-1, nonsalicylate COX and selective COX-2 inhibitors enhanced stimulated MMP-1 release. Addition of exogenous PGE1 or PGE2 inhibited MMP-1, reversed the effects of COX inhibitors, and inhibited ERK activation, suggesting that COX-2 activity tonically inhibits MMP-1 production via ERK inhibition by E PGs. Exposure of FLSCs to nonselective COX and selective COX-2 inhibitors in the absence of stimulation resulted in up-regulation of MMP-1 expression in an ERK-dependent manner. Moreover, COX inhibition sufficient to reduce PGE levels increased ERK activity. Our data indicate that: 1) ERK activation mediates MMP-1 but not MMP-13 release from FLSCs, 2) COX-2-derived E PGs inhibit MMP-1 release from FLSCs via inhibition of ERK, and 3) COX inhibitors, by attenuating PGE inhibition of ERK, enhance the release of MMP-1 by FLSC.

show abstract

Section: Activation Of Erk By Il-1␤ and Tnf-␣ In Flscssupporting

confidence: 90%

Cyclooxygenase-2-Derived E Prostaglandins Down-Regulate Matrix Metalloproteinase-1 Expression in Fibroblast-Like Synoviocytes via Inhibition of Extracellular Signal-Regulated Kinase Activation

Pillinger

Rosenthal

Tolani

et al. 2003

The Journal of Immunology

View full text Add to dashboard Cite

show abstract

“…Of the three MAPKs expressed in chondrocytes, JNK probably plays a more prominent role in 1L-1 0-induced catabolic stimuli in human chondrocytes due to its ability to activate transcription factor AP-1 [2,11,22,23,331. Two isoforms of JNK (p46 and p54) are expressed in human OA chondrocytes [8] and both are known to phosphorylate c-Jun resulting in enhanced transcriptional activity of AP-1.…”

Section: Discussionmentioning

confidence: 99%

Epigallocatechin‐3‐gallate selectively inhibits interleukin‐1 β‐induced activation of mitogen activated protein kinase subgroup c‐Jun N‐terminal kinase in human osteoarthritis chondrocytes

Singh

Ahmed

Malemud

et al. 2003

Journal Orthopaedic Research

View full text Add to dashboard Cite

Activation of mitogen activated protein kinases (MAPK) is a critical event in pro-inflammatory cytokine-induced signaling cascade in synoviocytes and chondrocytes that lead to the production of several mediators of cartilage damage in an arthritic joint. Green tea (Cunzelliu sinensis) is a widely consumed beverage and we earlier showed that polyphenols present in green tea (GTP) inhibit the development of inflammation and cartilage damage in an animal model of arthritis. In this study we evaluated the role of epigallocatechin-3-gallate (EGCG), a green tea polyphenol which mimics its anti-inflammtory effects, in modulating the IL-10-induced activation of MAPK's in human chondrocytes. We discovered that EGCG inhibited the IL-1 p-induced phosphorylation of c-Jm N-terminal kinase (JNK) isoforms, accumulation of phospho-c-Jun and DNA binding activity of AP-1 in osteoarthritis (OA) chondrocytes. Also IL-1 p, but not EGCG, induced the expression of JNK p46 without modulating the expression of JNK p54 in OA chondrocytes. In immunecomplex kinase assays, EGCG completely blocked the substrate phosphorylating activity of JNK but not of p38-MAPK. EGCG had no inhibitory effect on the activation of extracellular signal-regulated kinase p44/p42 (ERKp44/p42) or p38-MAPK in OA chondrocytes. EGCG or IL-Ip did not alter the total non-phosphorylated levels of either p38-MAPK or ERKp44/p42 in OA chondrocytes. These are novel findings and indicate that EGCG may be of potential benefit in inhibiting IL-1 pinduced catabolic effects in OA chondrocytes that are dependent on JNK activity.

show abstract

“…We used the so-called 2⌬⌬Ct method to analyze relative changes of Wnt-7b or -10a as described elsewhere by Livak et al 23 The means Ϯ SD of each Wnt gene, ␤-catenin, FRZB, and LRP5 expression were obtained from each RA, OA, or control group. Differences in the mean of each Wnt gene, ␤-catenin, FRZB, and LRP5 among experimental groups were evaluated with Dunnett's test.…”

Section: Tissue Collection and Processing For Reverse Transcribed-polmentioning

confidence: 99%

Expression Profiles and Functional Analyses of Wnt-Related Genes in Human Joint Disorders

Nakamura

Nawata

Wakitani

2005

The American Journal of Pathology

110

View full text Add to dashboard Cite

Integration of the NF-κB and mitogen-activated protein kinase/AP-1 pathways at the Collagenase-1 promoter: Divergence of IL-1 and TNF-dependent signal transduction in rabbit primary synovial fibroblasts

Cited by 148 publications

References 44 publications

Cyclooxygenase-2-Derived E Prostaglandins Down-Regulate Matrix Metalloproteinase-1 Expression in Fibroblast-Like Synoviocytes via Inhibition of Extracellular Signal-Regulated Kinase Activation

Cyclooxygenase-2-Derived E Prostaglandins Down-Regulate Matrix Metalloproteinase-1 Expression in Fibroblast-Like Synoviocytes via Inhibition of Extracellular Signal-Regulated Kinase Activation

Epigallocatechin‐3‐gallate selectively inhibits interleukin‐1 β‐induced activation of mitogen activated protein kinase subgroup c‐Jun N‐terminal kinase in human osteoarthritis chondrocytes

Expression Profiles and Functional Analyses of Wnt-Related Genes in Human Joint Disorders

Contact Info

Product

Resources

About