TGF-β1-stimulation of matrix metalloproteinase-13 expression by down-regulation of miR-203a-5p in rat osteoblasts

We have found an association of miR-122 down-regulation with myocardial fibrosis in AS patients, probably through TGF-β1 up-regulation and stimulation of the enzymatic systems involved in extracellular collagen type I synthesis and deposition.

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FK506 suppresses the stimulation of matrix metalloproteinase 13 synthesis by interleukin-1β in rheumatoid synovial fibroblasts

Immunology Letters ◽

10.1016/j.imlet.2004.11.014 ◽

2005 ◽

Vol 98 (2) ◽

pp. 194-199 ◽

Cited By ~ 16

Author(s):

Kiyoshi Migita ◽

Taichiro Miyashita ◽

Yumi Maeda ◽

Takahiko Aoyagi ◽

Yojiro Kawabe ◽

...

Keyword(s):

Matrix Metalloproteinase ◽

Synovial Fibroblasts ◽

Interleukin 1Β ◽

Matrix Metalloproteinase 13 ◽

Stimulation Of

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Sirtuin 1 Is a Negative Regulator of Parathyroid Hormone Stimulation of Matrix Metalloproteinase 13 Expression in Osteoblastic Cells

Journal of Biological Chemistry ◽

10.1074/jbc.m114.602763 ◽

2015 ◽

Vol 290 (13) ◽

pp. 8373-8382 ◽

Cited By ~ 21

Author(s):

Yurong Fei ◽

Emi Shimizu ◽

Michael W. McBurney ◽

Nicola C. Partridge

Keyword(s):

Parathyroid Hormone ◽

Matrix Metalloproteinase ◽

Negative Regulator ◽

Sirtuin 1 ◽

Osteoblastic Cells ◽

Hormone Stimulation ◽

Matrix Metalloproteinase 13 ◽

Stimulation Of

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Regulation of transforming growth factor-β1-stimulation of Runx2 acetylation for matrix metalloproteinase 13 expression in osteoblastic cells

Biological Chemistry ◽

10.1515/hsz-2021-0292 ◽

2021 ◽

Vol 0 (0) ◽

Author(s):

Kanagaraj Gomathi ◽

Muthukumar Rohini ◽

Nicola C. Partridge ◽

Nagarajan Selvamurugan

Keyword(s):

Growth Factor ◽

Matrix Metalloproteinase ◽

Transforming Growth Factor Beta ◽

Target Genes ◽

Transforming Growth Factor ◽

Bone Development ◽

Osteoblastic Cells ◽

Post Translational Modification ◽

Matrix Metalloproteinase 13 ◽

Tgf Β1

Abstract Transforming growth factor beta 1 (TGF-β1) functions as a coupling factor between bone development and resorption. Matrix metalloproteinase 13 (MMP13) is important in bone remodeling, and skeletal dysplasia is caused by a deficiency in MMP13 expre-ssion. Runx2, a transcription factor is essential for bone development, and MMP13 is one of its target genes. TGF-β1 promoted Runx2 phosphorylation, which was necessary for MMP13 production in osteoblastic cells, as we previously shown. Since the phosphorylation of some proteins causes them to be degraded by the ubiquitin/proteasome pathway, we hypothesized that TGF-β1 might stabilize the phosphorylated Runx2 protein for its activity by other post-translational modification (PTM). This study demonstrated that TGF-β1-stimulated Runx2 acetylation in rat osteoblastic cells. p300, a histone acetyltransferase interacted with Runx2, and it promoted Runx2 acetylation upon TGF-β1-treatment in these cells. Knockdown of p300 decreased the TGF-β1-stimulated Runx2 acetylation and MMP13 expression in rat osteoblastic cells. TGF-β1-treatment stimulated the acetylated Runx2 bound at the MMP13 promoter, and knockdown of p300 reduced this effect in these cells. Overall, our studies identified the transcriptional regulation of MMP13 by TGF-β1 via Runx2 acetylation in rat osteoblastic cells, and these findings contribute to the knowledge of events presiding bone metabolism.

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Down-regulation of interleukin-1alpha-induced matrix metalloproteinase-13 expression via EP1 receptors by prostaglandin E2 in human periodontal ligament cells

Oral Microbiology and Immunology ◽

10.1111/j.1399-302x.2004.00187.x ◽

2005 ◽

Vol 20 (1) ◽

pp. 56-59 ◽

Cited By ~ 10

Author(s):

K. Noguchi ◽

S. M. P. M. Ruwanpura ◽

M. Yan ◽

N. Yoshida ◽

I. Ishikawa

Keyword(s):

Matrix Metalloproteinase ◽

Prostaglandin E2 ◽

Periodontal Ligament ◽

Periodontal Ligament Cells ◽

Down Regulation ◽

Matrix Metalloproteinase 13 ◽

Human Periodontal Ligament Cells

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The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases

Biochemical Journal ◽

10.1042/bj3640181 ◽

2002 ◽

Vol 364 (1) ◽

pp. 181-190 ◽

Cited By ~ 77

Author(s):

Heather STANTON ◽

Linh UNG ◽

Amanda J. FOSANG

Keyword(s):

Matrix Metalloproteinase ◽

Conditioned Medium ◽

Articular Chondrocytes ◽

Interleukin 1 ◽

Cartilage Explants ◽

Dependent Manner ◽

Collagen Binding ◽

Matrix Metalloproteinase 13 ◽

Cultured Chondrocytes ◽

Stimulation Of

Fragments of fibronectin occur naturally in vivo and are increased in the synovial fluid of arthritis patients. We have studied the 45kDa fragment (Fn-f 45), representing the N-terminal collagen-binding domain of fibronectin, for its ability to modulate the expression of metalloproteinases by porcine articular chondrocytes in vitro. We report that stimulation of cultured chondrocytes, or cartilage explants, with Fn-f 45 increased the levels of matrix metalloproteinase-13 (MMP-13; collagenase-3) released into the conditioned medium in a dose-dependent manner. Increased levels of MMP-13 were due to stimulation of MMP-13 synthesis, rather than release of MMP-13 from accumulated matrix stores. Fn-f 45 also stimulated the synthesis of MMP-3 (stromelysin-1) from cultured chondrocytes and cartilage cultures. The Fn-f 45-induced increase in MMP-3 and MMP-13 synthesis occurred via an interleukin 1-independent mechanism, since the receptor antagonist of interleukin-1 was unable to block the increased synthesis. The gelatinases, MMP-2 and MMP-9, were not modulated by Fn-f 45 in these culture systems. Fn-f 45 also stimulated the release of aggrecan from cartilage explants into conditioned medium. Neoepitope antibodies specific for aggrecan fragments generated by MMPs or aggrecanases showed that the Fn-f 45-induced aggrecan loss was mediated by aggrecanases, and not by MMPs. Extracts of cultured cartilage contained elevated levels of the aggrecanase-derived ITEGE373-G1 domain, whereas levels of the matrix metalloproteinase-derived DIPEN341-G1 domain were unchanged. These studies show that Fn-f 45 can induce a catabolic phenotype in articular chondrocytes by up-regulating the expression of metalloproteinases specific for the degradation of collagen and aggrecan.

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