Inhibitory Effects of the Halophyte Ligustrum Japonicum on Matrix Metalloproteinases Activity in PMA-stimulated HT-1080 cells

KSBB Journal ◽  
2020 ◽  
Vol 35 (1) ◽  
pp. 57-63
Author(s):  
Junse Kim ◽  
Chang-Suk Kong ◽  
Ki Hwan Moon ◽  
Youngwan Seo
2012 ◽  
Vol 28 (8) ◽  
pp. 903-908 ◽  
Author(s):  
May L. Mei ◽  
Q.L. Li ◽  
C.H. Chu ◽  
Cynthia K.Y. Yiu ◽  
Edward C.M. Lo

2017 ◽  
Vol 141 ◽  
pp. 147-155 ◽  
Author(s):  
Quynh-Mai Thi Ngo ◽  
Hyun-Su Lee ◽  
Van Thu Nguyen ◽  
Jeong Ah Kim ◽  
Mi Hee Woo ◽  
...  

2018 ◽  
Vol 7 (6) ◽  
pp. 541-553 ◽  
Author(s):  
Magdalena Matysiak-Kucharek ◽  
Magdalena Czajka ◽  
Krzysztof Sawicki ◽  
Marcin Kruszewski ◽  
Lucyna Kapka-Skrzypczak

AbstractMatrix metallopeptidases, commonly known as matrix metalloproteinases (MMPs), are a group of proteolytic enzymes whose main function is the remodeling of the extracellular matrix. Changes in the activity of these enzymes are observed in many pathological states, including cancer metastases. An increasing body of evidence indicates that nanoparticles (NPs) can lead to the deregulation of MMP expression and/or activity both in vitro and in vivo. In this work, we summarized the current state of knowledge on the impact of NPs on MMPs. The literature analysis showed that the impact of NPs on MMP expression and/or activity is inconclusive. NPs exhibit both stimulating and inhibitory effects, which might be dependent on multiple factors, such as NP size and coating or a cellular model used in the research.


2013 ◽  
Vol 141 (1) ◽  
pp. 503-509 ◽  
Author(s):  
Van-Tinh Nguyen ◽  
Zhong-Ji Qian ◽  
BoMi Ryu ◽  
Kil-Nam Kim ◽  
Daekyung Kim ◽  
...  

2013 ◽  
Vol 61 (15) ◽  
pp. 3631-3641 ◽  
Author(s):  
Atita Panyathep ◽  
Teera Chewonarin ◽  
Khanittha Taneyhill ◽  
Usanee Vinitketkumnuen ◽  
Young-Joon Surh

2003 ◽  
Vol 70 ◽  
pp. 125-133 ◽  
Author(s):  
Tim E. Cawston ◽  
Jenny M. Milner ◽  
Jon B. Catterall ◽  
Andrew D. Rowan

We have investigated proteinases that degrade cartilage collagen. We show that pro-inflammatory cytokines act synergistically with oncastatin M to promote cartilage collagen resorption by the up-regulation and activation of matrix metalloproteinases (MMPs). The precise mechanisms are not known, but involve the up-regulation of c-fos, which binds to MMP promoters at a proximal activator protein-1 (AP-1) site. This markedly up-regulates transcription and leads to higher levels of active MMP proteins.


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