Functional Characterization of Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) N- and C-Terminal Domains during<i>Xenopus laevis</i>Development

Nieuwesteeg, Michelle A.; Willson, Jessica A.; Cepeda, Mario; Fox, Mark A; Damjanovski, Sashko

doi:10.1155/2014/467907

Cited by 7 publications

(9 citation statements)

References 38 publications

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“…[22] Tissue inhibitor of metalloproteinases consists of a family of 4 secreted proteins (TIMP 1-4), which bind MMPs in a ratio of 1: 1 manner to inhibit their proteolytic activity. [2324] TIMP-1 is as a natural inhibitor of MMPs and is a glycoprotein expressed in multiple tissues in many organisms. [25] In addition to its inhibitory role, TIMP-1 is able to promote cell proliferation and inhibit apoptosis as well as regulate cell growth in a wide range of cell types.…”

Section: Introductionmentioning

confidence: 99%

Relationships of MMP-9 and TIMP-1 proteins with chronic obstructive pulmonary disease risk: A systematic review and meta-analysis

et al. 2016

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Background:We performed this meta-analysis in order to collect all the relevant studies to clarify the correlations of matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1) with chronic obstructive pulmonary disease (COPD).Materials and Methods:After a literature search in electronic databases, pertinent case-control studies investigating the correlations of MMP-9 and TIMP-1 protein expressions within a COPD setting were enrolled based on our strict inclusion and exclusion criteria. We used key words such as “chronic obstructive pulmonary disease,” “COPD” or “COAD” or “chronic obstructive airway disease” and “matrix metalloproteinases” or “MMPs” to make a searching strategy in this study. STATA software (version 12.0, Stata Corporation, College Station, TX, USA) was utilized for statistical analysis.Results:A total of 20 studies were enrolled into this meta-analysis including 923 COPD patients and 641 healthy controls. The findings of this meta-analysis revealed that serum expression levels of MMP-9 and TIMP-1 protein in COPD patients were higher than those of healthy controls (MMP-9: SMD = 1.44, 95%CI = 0.85 ~ 2.04, P < 0.001; TIMP-1: SMD = 3.53, 95% CI = 2.31 ~ 4.75, P < 0.001). Subgroup analysis based on ethnicity revealed that both Caucasians and Asian COPD patients exhibited higher MMP-9 and TIMP-1 serum protein levels than healthy controls (MMP-9: SMD = 0.81, 95%CI = 0.15~1.48, P = 0.016; TIMP-1: SMD = 4.43, 95%CI = 1.98 ~ 6.87, P = 0.016) and in Caucasians (MMP-9: SMD = 2.30, 95%CI = 1.21 ~ 3.38, P < 0.001; TIMP-1: SMD = 2.86, 95%CI = 1.47 ~ 4.24, P < 0.001).Conclusion:The result of this meta-analysis indicates that elevated levels of MMP-9 and TIMP-1 proteins may be correlated with the pathogenesis of COPD, and the two proteins may represent important biological markers for the early diagnosis of COPD.

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Section: Introductionmentioning

confidence: 99%

Relationships of MMP-9 and TIMP-1 proteins with chronic obstructive pulmonary disease risk: A systematic review and meta-analysis

et al. 2016

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“…MMP-9 activity could not be detected in the media (Fig. 2c) at the previously described molecular mass [10, 22, 23].…”

Section: Resultsmentioning

confidence: 82%

Modulation of RECK levels in Xenopus A6 cells: effects on MT1-MMP, MMP-2 and pERK levels

Willson

Bork

Muir

et al. 2019

J of Biol Res-Thessaloniki

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BackgroundMT1-MMP is a cell-surface enzyme whose regulation of pro-MMP-2 and ERK activation position it as a key facilitator of ECM remodelling and cell migration. These processes are modulated by endogenous MMP inhibitors, such as RECK, a GPI-anchored protein which has been shown to inhibit both MT1-MMP and MMP-2 activity. Our previous studies have revealed a link between MT1-MMP levels, and pro-MMP-2 and ERK activation in mammalian cells, as well as MT1-MMP and RECK co-localization in Xenopus embryos. We here investigated how modulation of RECK would impact MT1-MMP and MMP-2 levels, as well as ERK signalling in Xenopus A6 cells.ResultsWe used a Morpholino approach to knockdown RECK, plasmid transfection to overexpress RECK, and PI-PLC treatment to shed RECK from the cell surface of Xenopus A6 cells. RECK reduction did not alter pERK or MT1-MMP levels, nor MMP-2 activity as measured by zymography; thus RECK-knockdown cells maintained the ability to remodel the ECM. RECK overexpression and PI-PLC treatment both increased ECM remodelling potential through increased MT1-MMP protein and relative MMP-2 activation levels.ConclusionsRECK changes that reduce the ability of the cell to remodel the ECM (overexpression and cell surface shedding) are compensated for by increases in MT1-MMP, and MMP-2 levels as seen by zymography.

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“…In pancreatic cancer cells, TIMP1 overexpression can reduce the invasive ability both in vitro and in vivo. 42 TIMP1 can be up-regulated by CD82 and suppresses tumour invasion in human lung carcinoma cell lines. 43 In cervical cancer, the long non-coding TUC338 promotes cell migration and invasion by down-regulating TIMP1.…”

Section: Discussionmentioning

confidence: 96%

Knockdown of KDM1A suppresses tumour migration and invasion by epigenetically regulating the TIMP1/MMP9 pathway in papillary thyroid cancer

Zhang

Sun

Qin

et al. 2019

J Cellular Molecular Medi

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Epigenetic dysregulation plays an important role in cancer. Histone demethylation is a well‐known mechanism of epigenetic regulation that promotes or inhibits tumourigenesis in various malignant tumours. However, the pathogenic role of histone demethylation modifiers in papillary thyroid cancer (PTC), which has a high incidence of early lymphatic metastasis, is largely unknown. Here, we detected the expression of common histone demethylation modifiers and found that the histone H3 lysine 4 (H3K4) and H3 lysine 9 (H3K9) demethylase KDM1A (or lysine demethylase 1A) is frequently overexpressed in PTC tissues and cell lines. High KDM1A expression correlated positively with age <55 years and lymph node metastasis in patients with PTC. Moreover, KDM1A was required for PTC cell migration and invasion. KDM1A knockdown inhibited the migration and invasive abilities of PTC cells both in vitro and in vivo. We also identified tissue inhibitor of metalloproteinase 1 (TIMP1) as a key KDM1A target gene. KDM1A activated matrix metalloproteinase 9 (MMP9) through epigenetic repression of TIMP1 expression by demethylating H3K4me2 at the TIMP1 promoter region. Rescue experiments clarified these findings. Altogether, we have uncovered a new mechanism of KDM1A repression of TIMP1 in PTC and suggest that KDM1A may be a promising therapeutic target in PTC.

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Functional Characterization of Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) N- and C-Terminal Domains duringXenopus laevisDevelopment

Cited by 7 publications

References 38 publications

Relationships of MMP-9 and TIMP-1 proteins with chronic obstructive pulmonary disease risk: A systematic review and meta-analysis

Relationships of MMP-9 and TIMP-1 proteins with chronic obstructive pulmonary disease risk: A systematic review and meta-analysis

Modulation of RECK levels in Xenopus A6 cells: effects on MT1-MMP, MMP-2 and pERK levels

Knockdown of KDM1A suppresses tumour migration and invasion by epigenetically regulating the TIMP1/MMP9 pathway in papillary thyroid cancer

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