Stimulation of MMP-11 (stromelysin-3) expression in mouse fibroblasts by cytokines, collagen and co-culture with human breast cancer cell lines

Selvey, Saxon; Haupt, Larisa M.; Thompson, Erik W.; Matthaei, Klaus I.; Irving, Michael G.; Griffiths, Lyn R.

doi:10.1186/1471-2407-4-40

Cited by 27 publications

(24 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In other fibrotic models, TGF-b stimulated MMP-2 and MMP-11 production (55)(56)(57)(58)(59)(60). Likewise, the TGF-b inhibitor perfenidone decreased MMP-11, but not MMP-2, in malignant glioma cells (61).…”

Section: Figurementioning

confidence: 95%

Myometrial cells undergo fibrotic transformation under the influence of transforming growth factor β-3

Joseph

Malik

Nurudeen

et al. 2010

Fertility and Sterility

View full text Add to dashboard Cite

Section: Figurementioning

confidence: 95%

Myometrial cells undergo fibrotic transformation under the influence of transforming growth factor β-3

Joseph

Malik

Nurudeen

et al. 2010

Fertility and Sterility

View full text Add to dashboard Cite

“…Previous studies showed that the ECM regulates the activity of MT1-MMP (12,45). Therefore, we examined the impact of the ECM on ischemia-induced cleavage and/or loss of E-and N-cadherin.…”

Section: Effects Of Proteinase Inhibitors On Ischemia-induced Cadherimentioning

confidence: 99%

Ischemia-induced cleavage of cadherins in NRK cells requires MT1-MMP (MMP-14)

Covington

Burghardt²,

Parrish³

2006

American Journal of Physiology-Renal Physiology

View full text Add to dashboard Cite

Ischemia is a leading cause of acute renal failure (ARF), a disease associated with high morbidity and mortality. Disruption of intercellular adhesion in the proximal tubules is linked to ARF, although the molecular mechanism(s) remains unclear. Our previous studies showed that ischemia is associated with cadherin cleavage and loss in NRK cells, putatively due to a matrix metalloproteinase (MMP) (7). In the current studies, a MMP required for E-cadherin cleavage and N-cadherin loss was identified. Chemical inhibitors against a number of soluble MMPs (1, 2, 3, 8, 9) failed to completely attenuate ischemia-induced cadherin loss. Under ischemic conditions, there was an increase in active membrane-type (MT)1-MMP but a decrease in MMP-2 protein expression. Plating cells on fibronectin protected against ischemia-induced loss of cadherins and, interestingly, no increase in active MT1-MMP levels was seen in ischemic cells on fibronectin-coated dishes. In addition, L cells stably expressing E- (LE) or N-cadherin (LN), but lacking MT1-MMP expression, were resistant to ischemia-induced cadherin loss. The role of MT1-MMP in ischemia-induced cadherin loss was confirmed by either blocking MT1-MMP activity with a neutralizing antibody or expression with shRNA constructs which protected full-length E- and N-cadherin during ischemia. Using shRNA constructs to suppress MT1-MMP expression, ischemia-induced disruption of cadherin function was ablated, and cell-cell contacts were preserved. These results demonstrate that ischemia induces increased expression of active MT1-MMP and subsequent disruption of cadherin/catenin complexes, implying that MT1-MMP plays a role in ischemia-induced ARF.

show abstract

“…MMP11 in particular, a member of the matrix metalloproteinases, exhibits collagenolytic function against collagen VI under normal and malignant conditions (4), and is closely related to invasiveness and tumor progression (5). MMP-ll expression is simulated in mouse fibroblasts by cytokines, collagen and co-culture with human breast cancer cells (6), and its overexpression in lobular carcinoma cells of the breast promotes resistance to anoikis (7). MMP 11 is identified as the novel undetected gene of cervical carcinoma and contributes to the pathogenesis of cervical carcinoma (8).…”

mentioning

confidence: 99%

Knockdown of MMP11 Inhibits Proliferation and Invasion of Gastric Cancer Cells

et al. 2013

Int J Immunopathol Pharmacol

View full text Add to dashboard Cite

Matrix metalloproteinase 11(MMPll or stromelysin-3) has recently been reported to playa crucial role in the development and progression of multiple malignancies. The aim of this study was to investigate the function ofMMPll expression in human gastric adenocarcinoma (GAC). Using immunohistochemistry assay, we studied the expression level of MMPll in GAC and adjacent non-cancerous tissues (ANCT). The association between MMPll expression and tumor size and pathological grade, as well as metastatic potential was analyzed. Through small hairpin RNA (shRNA)-mediated MMPll knockdown in SGC-7901 GAC cells, we observed the changes of the biological behaviors of GAC cells. Our results indicated that the rate of positive expression ofMMPll was higher in GAC tissues than in ANCT (55.0% vs 30.0%, P=0.025). MMPll expression had no association with the factors of age or gender of the GAC patients, or the size, pathological staging and lymph node metastases of the tumors (each P>0.05). Furthermore, MMPll knockdown inhibited the proliferative activities and invasive potential of SGC-7901 GAC cells with decreased expression of IGF-l, PCNA and VEGF. Taken together, our findings demonstrated that MMPll expression was increased in GAC tissues, but did not correlate with the clinicopathologic features. Knockdown of MMPll expression could inhibit the proliferation and invasion of GAC cells probably through down-regulation of the IGF-l signaling pathway, suggesting that MMPll might be a potential therapeutic target for the treatment of gastric cancer.Gastric cancer (GC) is a world health burden, ranging as the second cause of cancer death worldwide. The prognosis of gastric cancer is poor with an estimated relative five year survival rate of less than 20% (1). Etiologically, GC arises not only from the combined effects of environmental factors and susceptible genetic variants but also from the accumulation of genetic and epigenetic alterations. Molecular oncobiology studies have brought to light a number of genes that are implicated in gastric carcinogenesis (2).Matrix metalloproteases (MMPs) playa key role in the metabolism of connective tissue proteins in the norm and in pathology. Major MMP subfamilies and matrixins act through promoting the oncogenic transformation of the cells, and angiogenesis (3). MMPs constitute one of the major extracellular matrix degrading enzymic families implicated in cancer development. MMP11 in particular, a member of the matrix metalloproteinases, exhibits collagenolytic function against collagen VI under normal and malignant conditions (4), and is closely related to invasiveness and tumor progression (5). MMP-ll expression is simulated in mouse

show abstract

Stimulation of MMP-11 (stromelysin-3) expression in mouse fibroblasts by cytokines, collagen and co-culture with human breast cancer cell lines

Cited by 27 publications

References 25 publications

Myometrial cells undergo fibrotic transformation under the influence of transforming growth factor β-3

Myometrial cells undergo fibrotic transformation under the influence of transforming growth factor β-3

Ischemia-induced cleavage of cadherins in NRK cells requires MT1-MMP (MMP-14)

Knockdown of MMP11 Inhibits Proliferation and Invasion of Gastric Cancer Cells

Contact Info

Product

Resources

About