scholarly journals Surface‐bound matrix metalloproteinase‐8 on macrophages: Contributions to macrophage pericellular proteolysis and migration through tissue barriers

2021 ◽  
Vol 9 (5) ◽  
Author(s):  
Xiaoyun Wang ◽  
Duo Zhang ◽  
Quynh‐Anh Fucci ◽  
Clare M. Dollery ◽  
Caroline A. Owen
Keyword(s):  
Matrix Metalloproteinase ◽  
And Migration ◽  
Pericellular Proteolysis

CEMIP regulates the proliferation and migration of vascular smooth muscle cells in atherosclerosis through the WNT–beta-catenin signaling pathway

2020 ◽  
Vol 98 (2) ◽  
pp. 249-257
Author(s):  
Qiang Xue ◽  
Xiaoli Wang ◽  
Xiaohui Deng ◽  
Yue Huang ◽  
Wei Tian
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Matrix Metalloproteinase ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Signaling Pathway ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
And Migration ◽  
Proliferation And Migration

In this study we investigated the regulatory role of cell-migration-inducing and hyaluronan-binding protein (CEMIP) in the proliferation and migration of vascular smooth muscle cells (VSMCs). The mRNA and protein levels of CEMIP were upregulated in the plasma samples from patients with atherosclerosis, and in VSMCs stimulated with platelet-derived growth factor-BB (PDGF-BB), compared with plasma from healthy subjects and untreated VSMCs. Silencing CEMIP suppressed PDGF-BB-induced cell migration and proliferation in VSMCs, as determined using a Cell Counting Kit-8 assays, 5-ethynyl-2′-deocyuridine (EDU) assays, flow cytometry, wound healing assays, and Transwell assays. Overexpression of CEMIP promoted the proliferation and migration of VSMCs via activation of the Wnt–β-catenin signaling pathway and the upregulation of its target genes, including matrix metalloproteinase-2, matrix metalloproteinase-7, cyclin D1, and c-myc, whereas CEMIP deficiency showed the opposite effects. The knockdown of CEMIP in ApoE−/− mice by intravenous injection of lentiviral vector expressing si-CEMIP protected against high-fat-diet-induced atherosclerosis, as shown by the reduced aortic lesion areas, aortic sinus lesion areas, and the concentration of blood lipids compared with mice normally expressing CEMIP. These results demonstrated that CEMIP regulates the proliferation and migration of VSMCs in atherosclerosis by activating the WNT–β-catenin signaling pathway, which suggests the therapeutic potential of CEMIP for the management of atherosclerosis.

scholarly journals A Novel CD44-binding Peptide from the Pro-Matrix Metalloproteinase-9 Hemopexin Domain Impairs Adhesion and Migration of Chronic Lymphocytic Leukemia (CLL) Cells

2014 ◽  
Vol 289 (22) ◽  
pp. 15340-15349 ◽  
Author(s):  
Estefanía Ugarte-Berzal ◽  
Elvira Bailón ◽  
Irene Amigo-Jiménez ◽  
Juan Pablo Albar ◽  
José A. García-Marco ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 9 ◽  
Lymphocytic Leukemia ◽  
Binding Peptide ◽  
And Migration ◽  
Hemopexin Domain ◽  
Metalloproteinase 9

Gypenosides inhibits migration and invasion of human oral cancer SAS cells through the inhibition of matrix metalloproteinase-2 -9 and urokinase-plasminogen by ERK1/2 and NF-kappa B signaling pathways

2010 ◽  
Vol 30 (5) ◽  
pp. 406-415 ◽  
Author(s):  
Kung-Wen Lu ◽  
Jung-Chou Chen ◽  
Tung-Yuan Lai ◽  
Jai-Sing Yang ◽  
Shu-Wen Weng ◽  
...  
Keyword(s):  
Oral Cancer ◽  
Matrix Metalloproteinase ◽  
Cancer Cells ◽  
Time Dependent ◽  
Migration And Invasion ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Invasion And Migration ◽  
Oral Cancer Cells ◽  
And Migration

Gypenosides (Gyp), found in Gynostemma pentaphyllum Makino, has been used as a folk medicine in the Chinese population for centuries and is known to have diverse pharmacologic effects, including anti-proliferative and anti-cancer actions. However, the effects of Gyp on prevention from invasion and migration of oral cancer cells are still unsatisfactory. The purpose of this study was to investigate effects of Gyp treatment on migration and invasion of SAS human oral cancer cells. SAS cells were cultured in the presence of 90 and 180 μg/mL Gyp for 24 and 48 hours. Gyp induced cytotoxic effects and inhibited SAS cells migration and invasion in dose- and time-dependent response. Wound-healing assay and boyden chamber assay were carried out to investigate Gyp-inhibited migration and invasion of SAS cells. Gyp decreased the abundance of several proteins, including nuclear factor-kappa B (NF-κB), cyclooxygenase-2 (COX-2), extracellular signal-regulated kinase 1/2 (ERK1/ 2), matrix metalloproteinase-9, -2 (MMP-9, -2), sevenless homolog (SOS), Ras, urokinase-type plasminogen activator (uPA), focal adhesion kinase (FAK) and RAC-alpha serine/threonine-protein kinase (Akt), in a time-dependent manner. In addition, Gyp decreased mRNA levels of MMP-2, MMP-7, MMP-9 but did not affect FAK and Rho A mRNA levels in SAS cells. These results provide evidences for the role of Gyp as a potent anti-metastatic agent, which can markedly inhibit the metastatic and invasive capacity of oral cancer cells. The inhibition of NF-κB and MMP-2, -7 and -9 signaling may be one of the mechanisms that is present in Gyp-inhibited cancer cell invasion and migration.

Triple Inhibitory Activity of Cliona celata Against TNF-α-Induced Matrix Metalloproteinase-9 Production Via Downregulated NF-κB and AP-1, Enzyme Activity, and Migration Potential

Inflammation ◽  
2011 ◽  
Vol 35 (2) ◽  
pp. 736-745 ◽  
Author(s):  
Seok-Jong Suh ◽  
Choong-Hwan Kwak ◽  
Kwon-Ho Song ◽  
Kyung-Min Kwon ◽  
Tae-Wook Chung ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Matrix Metalloproteinase ◽  
Inhibitory Activity ◽  
Matrix Metalloproteinase 9 ◽  
Tnf Α ◽  
Migration Potential ◽  
Cliona Celata ◽  
And Migration ◽  
Metalloproteinase 9

miR-150-5p and miR-133a suppress glioma cell proliferation and migration through targeting membrane-type-1 matrix metalloproteinase

Gene ◽  
2016 ◽  
Vol 587 (2) ◽  
pp. 155-162 ◽  
Author(s):  
Moustafa Sakr ◽  
Takahisa Takino ◽  
Hemragul Sabit ◽  
Mitsutoshi Nakada ◽  
Zichen Li ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Matrix Metalloproteinase ◽  
Glioma Cell ◽  
Cell Proliferation And Migration ◽  
Glioma Cell Proliferation ◽  
Membrane Type ◽  
And Migration ◽  
Proliferation And Migration

Pericellular proteolysis by matrix metalloproteinase-7 is differentially modulated by cholesterol sulfate, sulfatide, and cardiolipin

FEBS Journal ◽  
2014 ◽  
Vol 281 (15) ◽  
pp. 3346-3356 ◽  
Author(s):  
Kazuhiro Yamamoto ◽  
Kaoru Miyazaki ◽  
Shouichi Higashi
Keyword(s):  
Matrix Metalloproteinase ◽  
Cholesterol Sulfate ◽  
Matrix Metalloproteinase 7 ◽  
Pericellular Proteolysis

Platelet‐activating factor (PAF) induces activation of matrix metalloproteinase 2 activity and vascular endothelial cell invasion and migration

2004 ◽  
Vol 18 (3) ◽  
pp. 568-570 ◽  
Author(s):  
T. William Axelrad ◽  
Dayanand D. Deo ◽  
Paulo Ottino ◽  
Jennefer Van Kirk ◽  
Nicolas G. Bazan ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Vascular Endothelial Cell ◽  
Platelet Activating Factor ◽  
Matrix Metalloproteinase 2 ◽  
Vascular Endothelial ◽  
Invasion And Migration ◽  
And Migration
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