Literature DB >> 16368506

Regulation of matrix metalloproteinase (MMP) gene expression by protein kinases.

Paul M Reuben1, Herman S Cheung.   

Abstract

Matrix metalloproteinases (MMPs) are a family of structurally and functionally related zinc-containing endopeptidases that are capable of degrading almost all of the components of the extracellular matrix (ECM). Under physiological and pathological conditions, the MMPs play a significant role in the efficient tissue turnover and remodeling. Specific MMPs are responsible for the matrix degradation and remodeling. Maintenance of the equilibrium between deposition and degradation of the extracellular matrix is essential to the normal tissue development. Therefore, synthesis and breakdown of the MMPs are tightly controlled by protein kinases which mediate a host of other cellular processes. The MMPs are often induced by several agents and any uncontrolled expression of the MMPs can contribute to the pathogenesis of many human diseases. This review focuses on the regulation of the MMPs by the protein kinases at the level of gene expression and their signaling pathways.

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Year:  2006        PMID: 16368506     DOI: 10.2741/1873

Source DB:  PubMed          Journal:  Front Biosci        ISSN: 1093-4715


  17 in total

1.  Variability in melanoma metalloproteinase expression profiling.

Authors:  Orsi Giricz; Janelle L Lauer; Gregg B Fields
Journal:  J Biomol Tech       Date:  2010-12

2.  Glioblastoma cells vampirize WNT from neurons and trigger a JNK/MMP signaling loop that enhances glioblastoma progression and neurodegeneration.

Authors:  Marta Portela; Varun Venkataramani; Natasha Fahey-Lozano; Esther Seco; Maria Losada-Perez; Frank Winkler; Sergio Casas-Tintó
Journal:  PLoS Biol       Date:  2019-12-17       Impact factor: 8.029

3.  Naringenin inhibits migration of lung cancer cells via the inhibition of matrix metalloproteinases-2 and -9.

Authors:  Huai-Lu Chang; Yuh-Ming Chang; Shih-Chan Lai; Ke-Min Chen; Kuan-Chu Wang; Tsu-Ting Chiu; Fu-Hsin Chang; Li-Sung Hsu
Journal:  Exp Ther Med       Date:  2016-12-22       Impact factor: 2.447

4.  Physiological loading of joints prevents cartilage degradation through CITED2.

Authors:  Daniel J Leong; Yong H Li; Xiang I Gu; Li Sun; Zuping Zhou; Philip Nasser; Damien M Laudier; Jameel Iqbal; Robert J Majeska; Mitchell B Schaffler; Mary B Goldring; Luis Cardoso; Mone Zaidi; Hui B Sun
Journal:  FASEB J       Date:  2010-09-08       Impact factor: 5.191

5.  Up-regulated isocitrate dehydrogenase 1 suppresses proliferation, migration and invasion in osteosarcoma: in vitro and in vivo.

Authors:  Xiang Hu; Yang Liu; Chunxia Qin; Zhenyu Pan; Jun Luo; Aixi Yu; Zhen Cheng
Journal:  Cancer Lett       Date:  2013-12-22       Impact factor: 8.679

6.  Blockade of the RhoA-JNK-c-Jun-MMP2 cascade by atorvastatin reduces osteosarcoma cell invasion.

Authors:  Olivia Fromigué; Zahia Hamidouche; Pierre J Marie
Journal:  J Biol Chem       Date:  2008-08-29       Impact factor: 5.157

7.  c-Jun N-Terminal Kinase in Inflammation and Rheumatic Diseases.

Authors:  Monica Guma; Gary S Firestein
Journal:  Open Rheumatol J       Date:  2012-09-07

8.  In Vitro Effect of Antigenic Extract of Trichophyton verrucosum on Fibroblast Proliferation and Matrix Metalloproteinase -2 Activities.

Authors:  Ar Salehinodeh; S Rezai; H Javanmard-Khamene; P Ekhtiyari; A Mirshafiey
Journal:  Iran J Public Health       Date:  2012-06-30       Impact factor: 1.429

Review 9.  Protein kinase C in heart failure: a therapeutic target?

Authors:  Suresh Selvaraj Palaniyandi; Lihan Sun; Julio Cesar Batista Ferreira; Daria Mochly-Rosen
Journal:  Cardiovasc Res       Date:  2009-01-24       Impact factor: 13.081

10.  Regulation of the JNK pathway by TGF-beta activated kinase 1 in rheumatoid arthritis synoviocytes.

Authors:  Deepa R Hammaker; David L Boyle; Tomoyuki Inoue; Gary S Firestein
Journal:  Arthritis Res Ther       Date:  2007       Impact factor: 5.156

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