Increased expression of G11α in osteoblastic cells enhances parathyroid hormone activation of phospholipase C and AP-1 regulation of matrix metalloproteinase-13 mRNA

2005 ◽  
Vol 204 (1) ◽  
pp. 336-343 ◽  
Author(s):  
Ricky Cheung ◽  
Mary S. Erclik ◽  
Jane Mitchell
Keyword(s):  
Parathyroid Hormone ◽  
Matrix Metalloproteinase ◽  
Phospholipase C ◽  
Osteoblastic Cells ◽  
Matrix Metalloproteinase 13

scholarly journals HDAC4 Represses Matrix Metalloproteinase-13 Transcription in Osteoblastic Cells, and Parathyroid Hormone Controls This Repression

2010 ◽  
Vol 285 (13) ◽  
pp. 9616-9626 ◽  
Author(s):  
Emi Shimizu ◽  
Nagarajan Selvamurugan ◽  
Jennifer J. Westendorf ◽  
Eric N. Olson ◽  
Nicola C. Partridge
Keyword(s):  
Parathyroid Hormone ◽  
Matrix Metalloproteinase ◽  
Osteoblastic Cells ◽  
Matrix Metalloproteinase 13

miR‐873‐3p targets HDAC4 to stimulate matrix metalloproteinase‐13 expression upon parathyroid hormone exposure in rat osteoblasts

2020 ◽  
Vol 235 (11) ◽  
pp. 7996-8009 ◽  
Author(s):  
Desai Malavika ◽  
Srinivasan Shreya ◽  
Vembar Raj Priya ◽  
Muthukumar Rohini ◽  
Zhiming He ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 13 ◽  
Hormone Exposure ◽  
Rat Osteoblasts

Parathyroid hormone increases the expression level of matrix metalloproteinase-13 in vivo

2001 ◽  
Vol 19 (4) ◽  
pp. 207-212 ◽  
Author(s):  
Motoyuki Uchida ◽  
Hideyuki Yamato ◽  
Yumiko Nagai ◽  
Hiroshi Yamagiwa ◽  
Tadashi Hayami ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Matrix Metalloproteinase ◽  
Expression Level ◽  
Matrix Metalloproteinase 13

scholarly journals Parathyroid hormone‐induced down‐regulation of miR‐532‐5p for matrix metalloproteinase‐13 expression in rat osteoblasts

2018 ◽  
Vol 119 (7) ◽  
pp. 6181-6193 ◽  
Author(s):  
Vishal Mohanakrishnan ◽  
Arumugam Balasubramanian ◽  
Gokulnath Mahalingam ◽  
Nicola Chennell Partridge ◽  
Ilangovan Ramachandran ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Matrix Metalloproteinase ◽  
Down Regulation ◽  
Matrix Metalloproteinase 13 ◽  
Rat Osteoblasts

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

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.

Nmp4/CIZ regulation of matrix metalloproteinase 13 (MMP-13) response to parathyroid hormone in osteoblasts

2004 ◽  
Vol 287 (2) ◽  
pp. E289-E296 ◽  
Author(s):  
Rita Shah ◽  
Marta Alvarez ◽  
Daniel R. Jones ◽  
Kitti Torrungruang ◽  
Andrew J. Watt ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Matrix Metalloproteinase ◽  
Osteoblast Differentiation ◽  
Matrix Protein ◽  
Type I Collagen ◽  
Zinc Finger Protein ◽  
Regulatory Region ◽  
Type I ◽  
Matrix Metalloproteinase 13 ◽  
Response Region

Parathyroid hormone (PTH) regulation of matrix metalloproteinase-13 ( MMP-13) expression in osteoblasts contributes to normal bone turnover. The PTH response region of the rat MMP-13 gene spans nucleotides (nt) −148 to −38 and supports binding of numerous transcription factors, including Runx2, necessary for osteoblast differentiation, c-Fos/c-Jun, and Ets-1. These trans-acting proteins mediate hormone induction via incompletely defined combinatorial interactions. Within this region, adjacent to the distal Runx2 site, is a homopolymeric(dA:dT) element (−119/−110 nt) that conforms to the consensus site for the novel transcription factor nuclear matrix protein-4/cas interacting zinc finger protein (Nmp4/CIZ). This protein regulates bone cell expression of type I collagen and suppresses BMP2-enhanced osteoblast differentiation. The aim of this study was to determine whether Nmp4/CIZ contributes to MMP-13 basal transcription and PTH responsiveness in osteoblasts. Electrophoretic mobility shift analysis confirms Nmp4/CIZ binding within the MMP-13 PTH response region. Mutation of the Nmp4/CIZ element decreases basal activity of an MMP-13 promoter-reporter construct containing the first 1329 nt of the 5′-regulatory region, and overexpression of Nmp4/CIZ protein enhances the activity of the wild-type promoter. The same mutation of the homopolymeric(dA:dT) element enhances the MMP-13 response to PTH and PGE2. Overexpression of Nmp4/CIZ diminishes hormone induction. Mutation of both the homopolymeric(dA:dT) element and the adjacent Runx2 site further augments the PTH response. On the basis of these data and previous studies, we propose that Nmp4/CIZ is a component of a multiprotein assemblage or enhanceosome within the MMP-13 PTH response region and that, within this context, Nmp4/CIZ promotes both basal expression and hormonal synergy.

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