Cumulative Influence of Matrix Metalloproteinase-1 and -2 in the Migration of Melanoma Cells within Three-Dimensional Type I Collagen Lattices

2001 ◽  
Vol 270 (1) ◽  
pp. 110-118 ◽  
Author(s):  
Carole Ntayi ◽  
Sandrine Lorimier ◽  
Odile Berthier-Vergnes ◽  
William Hornebeck ◽  
Philippe Bernard
Keyword(s):  
Matrix Metalloproteinase ◽  
Type I Collagen ◽  
Three Dimensional ◽  
Melanoma Cells ◽  
Type I ◽  
Matrix Metalloproteinase 1 ◽  
Collagen Lattices

scholarly journals Skullcapflavone II Inhibits Degradation of Type I Collagen by Suppressing MMP-1 Transcription in Human Skin Fibroblasts

2019 ◽  
Vol 20 (11) ◽  
pp. 2734 ◽  
Author(s):  
Young Hun Lee ◽  
Eun Kyoung Seo ◽  
Seung-Taek Lee
Keyword(s):  
Type I Collagen ◽  
Three Dimensional ◽  
Transcriptional Level ◽  
Type I ◽  
Cancer Therapies ◽  
Dependent Manner ◽  
Reverse Transcription Pcr ◽  
Matrix Metalloproteinase 1 ◽  
Extracellular Signal ◽  
Tnf Α

Skullcapflavone II is a flavonoid derived from the root of Scutellaria baicalensis, a herbal medicine used for anti-inflammatory and anti-cancer therapies. We analyzed the effect of skullcapflavone II on the expression of matrix metalloproteinase-1 (MMP-1) and integrity of type I collagen in foreskin fibroblasts. Skullcapflavone II did not affect the secretion of type I collagen but reduced the secretion of MMP-1 in a dose- and time-dependent manner. Real-time reverse transcription-PCR and reporter gene assays showed that skullcapflavone II reduced MMP-1 expression at the transcriptional level. Skullcapflavone II inhibited the serum-induced activation of the extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) signaling pathways required for MMP-1 transactivation. Skullcapflavone II also reduced tumor necrosis factor (TNF)-α-induced nuclear factor kappa light chain enhancer of activated B cells (NF-κB) activation and subsequent MMP-1 expression. In three-dimensional culture of fibroblasts, skullcapflavone II down-regulated TNF-α-induced MMP-1 secretion and reduced breakdown of type I collagen. These results indicate that skullcapflavone II is a novel biomolecule that down-regulates MMP-1 expression in foreskin fibroblasts and therefore could be useful in therapies for maintaining the integrity of extracellular matrix.

scholarly journals A Novel Host/Tumor Cell Interaction Activates Matrix Metalloproteinase 1 and Mediates Invasion through Type I Collagen

1999 ◽  
Vol 274 (36) ◽  
pp. 25371-25378 ◽  
Author(s):  
Ulrike Benbow ◽  
Matthias P. Schoenermark ◽  
Teresa I. Mitchell ◽  
Joni L. Rutter ◽  
Ken-ichi Shimokawa ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Tumor Cell ◽  
Type I Collagen ◽  
Cell Interaction ◽  
Type I ◽  
Matrix Metalloproteinase 1 ◽  
Novel Host

scholarly journals Sesquiterpenes From Oplopanax elatus Stems and Their Anti-Photoaging Effects by Down-Regulating Matrix Metalloproteinase-1 Expression via Anti-Inflammation

2021 ◽  
Vol 9 ◽  
Author(s):  
Jiejing Yan ◽  
Mimi Hao ◽  
Yu Han ◽  
Jingya Ruan ◽  
Dandan Zheng ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Type I Collagen ◽  
Ultraviolet B ◽  
Type I ◽  
Dependent Manner ◽  
Hacat Cells ◽  
Western Blot Assay ◽  
Concentration Dependent Manner ◽  
Matrix Metalloproteinase 1 ◽  
Oplopanax Elatus

In the process of continuing to investigate ultraviolet b (UVB) irradiation protective constituents from Oplopanax elatus stems, nine new sesquiterpenes, named as eurylosesquiterpenosides A–D (1–4), eurylosesquiterpenols E–I (5–9), and ten known ones (10–19) were gained. Their structures were established by analysis of their NMR spectroscopic data, and electronic circular dichroism calculations were applied to define their absolute configurations. In addition, UVB induced HaCaT cells were used to study their anti-photoaging activities and mechanism. The results consolidated that compounds 7, 11, and 14 could improve the survival rate of HaCaT cells in concentration dependent manner at 10, 25, and 50 μM. Furthermore, western blot assay suggested that all of them could inhibit the expression of matrix metalloproteinase-1 (MMP-1), and increase the level of type I collagen markedly. Compounds 11 and 14 could reduce the phosphorylation of extracellular signal-regulated kinase and p38, respectively. Besides, compounds 7, 11, and 14 could significantly down-regulate the expression of inflammation related protein, such as tumor necrosis factor-α and cyclooxygenase-2, which indicated that they played anti-photoaging activities by reducing MMP-1 expression via down-regulating the production of inflammatory mediators and cytokines in UVB-induced HaCaT cells.

scholarly journals Physiological type I collagen organization induces the formation of a novel class of linear invadosomes

2012 ◽  
Vol 23 (2) ◽  
pp. 297-309 ◽  
Author(s):  
Amélie Juin ◽  
Clotilde Billottet ◽  
Violaine Moreau ◽  
Olivier Destaing ◽  
Corinne Albiges-Rizo ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Type I Collagen ◽  
Three Dimensional ◽  
Collagen Matrix ◽  
Matrix Metalloproteases ◽  
Collagen I ◽  
Matrix Metalloproteinase 2 ◽  
Type I ◽  
Fibrillar Collagen ◽  
Functional Relationships

Invadosomes are F-actin structures capable of degrading the matrix through the activation of matrix metalloproteases. As fibrillar type I collagen promotes pro-matrix metalloproteinase 2 activation by membrane type 1 matrix metalloproteinase, we aimed at investigating the functional relationships between collagen I organization and invadosome induction. We found that fibrillar collagen I induced linear F-actin structures, distributed along the fibrils, on endothelial cells, macrophages, fibroblasts, and tumor cells. These structures share features with conventional invadosomes, as they express cortactin and N-WASP and accumulate the scaffold protein Tks5, which proved essential for their formation. On the basis of their ability to degrade extracellular matrix elements and their original architecture, we named these structures “linear invadosomes.” Interestingly, podosomes or invadopodia were replaced by linear invadosomes upon contact of the cells with fibrillar collagen I. However, linear invadosomes clearly differ from classical invadosomes, as they do not contain paxillin, vinculin, and β1/β3 integrins. Using knockout mouse embryonic fibroblasts and RGD peptide, we demonstrate that linear invadosome formation and activity are independent of β1 and β3 integrins. Finally, linear invadosomes also formed in a three-dimensional collagen matrix. This study demonstrates that fibrillar collagen I is the physiological inducer of a novel class of invadosomes.

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