Modulation of MMPs by Cell Surface Integrin Receptor α5β1

Pal, Samares; Ganguly, Kirat Kumar; Moulik, Shuvojit; Chatterjee, Amitava

doi:10.2174/187152012802650183

Cited by 11 publications

(10 citation statements)

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“…Masking of integrin α 5 drastically reduce the MMP-9 expression. In earlier reports α 5 β 1 integrin, receptor for FN, was shown to play major role in FNmediated downstream signaling leading to upregulation of MMPs in different other cell lines (Das et al, 2008;Jia et al, 2004;Maity et al, 2010;Pal et al, 2012;Sen et al, 2010). Integrins activate various protein tyrosine kinases including FAK, which is an important component of focal adhesion.…”

Section: Discussionmentioning

confidence: 97%

Extracellular matrix protein fibronectin induces matrix metalloproteinases in human prostate adenocarcinoma cells PC-3

Pal

Ganguly

Chatterjee

2013

Cell Communication & Adhesion

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Studies on interaction of tumor cells with ECM components showed increased extracellular protease activity mediated by the family of matrix metalloproteinases (MMPs). Here we studied the effect of human prostate adenocarcinoma PC-3 cells -fi bronectin (FN) interaction on MMPs and the underlying signaling pathways. Culturing of PC-3 cells on FN-coated surface upregulated MMP-9 and MMP-1. This response is abrogated by the blockade of α 5 integrin. siRNA and inhibitor studies indicate possible involvement of phosphatidyl-inositol-3-kinase (PI-3K), focal adhesion kinase (FAK) and nuclear factor-kappaB (NF-κ B) in FN-induced upregulation of MMPs. FN treatment also enhanced phosphorylation of FAK, PI3K, protein kinase B (PKB or Akt), nuclear translocation of NF-κ B, surface expression of CD-44, and cell migration. Our fi ndings indicate that, binding of PC-3 cells to FN, possibly via α 5 β 1 integrin, induces signaling involving FAK, PI-3K, Akt, NF-κ B followed by upregulation of MMP-9 and MMP-1. CD-44 may have role in modulating MMP-9 activity.

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Section: Discussionmentioning

confidence: 97%

Extracellular matrix protein fibronectin induces matrix metalloproteinases in human prostate adenocarcinoma cells PC-3

Pal

Ganguly

Chatterjee

2013

Cell Communication & Adhesion

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“…Our experiments showed that laminin-induced MMP-9 expression was appreciably decreased by inhibition of ERK and PI3K, both of which are downstream targets of FAK [7]. PI3K signaling cascade has been linked to proliferation, cell survival, cytoskeletal rearrangement etc.…”

Section: Discussionmentioning

confidence: 67%

“…This family comprises 25 related, yet distinct vertebrate gene products, of which 24 are found in mammals [6]. Although MMPs differ in their substrate specificity, some of them show overlapping specificity [7]. Gelatinase A (MMP-2) and gelatinase B (MMP-9) readily digest the denatured collagens, gelatins.…”

Section: Introductionmentioning

confidence: 99%

Extracellular Matrix Protein Laminin Induces Matrix Metalloproteinase-9 in Human Breast Cancer Cell Line MCF-7

Pal

Moulik

Dutta

et al. 2014

Cancer Microenvironment

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Studies on interaction of tumor cells with extracellular matrix (ECM) components showed increased extracellular protease activity mediated by the family of matrix metalloproteinases (MMPs). Here we studied the effect of human breast cancer cell line MCF-7-laminin (LM) interaction on MMPs and the underlying signaling pathways. Culturing of MCF-7 cells on LM coated surface upregulated MMP-9 expression as well as reduced tissue inhibitor of metalloproteinases-1 (TIMP-1) expression. LM induced MMP-9 expression is abrogated by the blockade of α 2 integrin. Inhibitor studies indicate possible involvement of phosphatidyl-inositol-3-kinase (PI3K), extracellular signal regulated kinase (ERK) and nuclear factor-kappaB (NF-κB) in LM induced signaling. LM treatment also enhanced phosphorylation of FAK (focal adhesion kinase), PI3K, ERK; nuclear translocation of ERK, pERK, NF-κB and cell migration. Our findings indicate that, binding of MCF-7 cells to LM, possibly via α 2 β 1 integrin, induces signaling involving FAK, PI3K, ERK, NF-κB followed by upregulation of MMP-9 and cell migration.

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“…VEGF is reported to have regulatory role on MMP-2. It has been reported that tea polyphenols have inhibitory effect on VEGF [39]. TIMP-2 has also been reported to increase during black tea polyphenol treatment [39] [40] indicating strong reasons for MMP-2 inhibition.…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that tea polyphenols have inhibitory effect on VEGF [39]. TIMP-2 has also been reported to increase during black tea polyphenol treatment [39] [40] indicating strong reasons for MMP-2 inhibition. The black tea polyphenols also have inhibitory effect on cell signalling molecules [41].…”

Section: Discussionmentioning

confidence: 99%

Effect of Black Tea Polyphenol on Cell-ECM Interaction and MMP

Bhattacharyya¹,

Mondal²,

Moulik³

et al. 2017

AJPS

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Tea is one of the most widely consumed beverages in the world. Black tea, obtained from the leaves of Camellia sinensis is the preferred beverage in India and in most western countries. Epidemiological studies on black tea and cancer are limited. However, preliminary studies indicate a positive correlation between black tea consumption and a lower incidence of breast and ovarian cancer. In the present communication, we wanted to see the effect of black tea extract and the polyphenol theaflavin on cell-ECM interaction, MMP activity etc. to strengthen the anti-cancer effect of black tea.

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Modulation of MMPs by Cell Surface Integrin Receptor α5β1

Cited by 11 publications

References 0 publications

Extracellular matrix protein fibronectin induces matrix metalloproteinases in human prostate adenocarcinoma cells PC-3

Extracellular matrix protein fibronectin induces matrix metalloproteinases in human prostate adenocarcinoma cells PC-3

Extracellular Matrix Protein Laminin Induces Matrix Metalloproteinase-9 in Human Breast Cancer Cell Line MCF-7

Effect of Black Tea Polyphenol on Cell-ECM Interaction and MMP

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