Calcium Regulation of Matrix Metalloproteinase-mediated Migration in Oral Squamous Cell Carcinoma Cells

Munshi, Hidayatullah G.; Wu, Yi; Ariztia, Edgardo V.; Stack, M. Sharon

doi:10.1074/jbc.m207695200

Cited by 53 publications

(63 citation statements)

References 72 publications

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“…In contrast, the effect of MT1-MMP on cellular aggregation does seem to depend on calcium levels, as aggregation was clearly blocked under low-calcium conditions (data not shown). At this time, it is not yet clear whether the effects of low calcium result from a failure to engage cell-cell adhesion molecules other than E-cadherin or because of our previously published observation that catalytic function of MT1-MMP in keratinocytes is attenuated in low calcium conditions (30).…”

Section: Discussionmentioning

confidence: 96%

“…Generation of MT1-MMP-inducible OKF6 and SCC25 CellsThe coding sequence for the full-length MT1-MMP, the catalytically inactive EA, and the tail-deleted DC mutants of MT1-MMP have been described previously (30) and were subcloned into pRetroX-Tight-Pur vector (33). All plasmids were verified by DNA sequencing.…”

Section: Methodsmentioning

confidence: 99%

“…To examine the effect of ECM on cellular phenotype, cells were plated onto tissue culture plates coated with type I collagen (BD Biosciences) or laminin-5 (30,34).…”

Section: Methodsmentioning

confidence: 99%

“…SCC25 cells were obtained from American Type Culture Collection (29). SCC25 cells were routinely maintained in DMEM and Ham's F-12 medium (1:1) containing 10% fetal calf serum and supplemented with 100 units/ml penicillin and 100 g/ml streptomycin (4,30). OKF6 cells were maintained in keratinocyte-SFM supplemented with 100 units/ml penicillin, 100 g/ml streptomycin, 25 g/ml bovine pituitary extract (supplied with the medium), 0.2 ng/ml epidermal growth factor, and 0.31 mM CaCl 2 (31,32).…”

Section: Methodsmentioning

confidence: 99%

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Rho-ROCK-Myosin Signaling Meditates Membrane Type 1 Matrix Metalloproteinase-induced Cellular Aggregation of Keratinocytes

Dangi-Garimella

Redig

Shields

et al. 2010

Journal of Biological Chemistry

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Matrix metalloproteinases (MMPs) 2 are a large family of highly conserved metalloendopeptidases with proteolytic activity directed against a variety of extracellular matrix (ECM) substrates (1-3). MMPs have been implicated in basement membrane proteolysis, activation of growth factors, and cleavage of cell-adhesion molecules. Extending mechanistic investigation to cancer biology, numerous studies have shown that MMP overexpression enhances the invasive activity of tumor cell lines (4 -6). Analysis of human disease further supports the pro-tumorigenic role of MMPs, as increased expression of these proteases in tumor samples is clinically associated with invasion, metastasis, poor prognosis, and shorter survival times (7,8). In the specific case of squamous cell carcinoma (SCC), increased expression of membrane type 1-MMP (MT1-MMP, MMP14) is associated with ECM breakdown, tissue invasion, and lymph node metastasis (8).However, several animal studies have now clearly demonstrated that multiple members of the MMP family provide a paradoxically protective effect during the relentless molecular destruction that characterizes malignant progression. MMPs may have been initially identified as potent pro-tumorigenic proteases, but their simultaneous ability to function in an opposing, anti-tumorigenic role is now equally well established (9, 10). Such data underscore both the complexity of MMP activity in cellular signaling events as well as the importance of stringently evaluating the context in which these proteases take on either an anti-tumorigenic or pro-tumorigenic role. Intriguingly, several recent studies using SCC models have begun to suggest a putative mechanism through which MMPs may be induced to function primarily as anti-tumorigenic proteases. When exposed to carcinogens, MMP3-null mice developed squamous cell skin cancers that not only grew faster but were also strikingly less differentiated than those of control animals (11). Significantly, orthotopic injection of MMP3-expressing tumor cells resulted in pronounced tumor cell differentiation (12). However, although such findings indicate that MMPs may inhibit SCC progression by promoting tumor cell differentiation, the precise mechanism through which these proteinases regulate this process has not yet been elucidated.In normal tissue keratinocyte differentiation is a complex process mediated by cell-ECM and cell-cell interactions that subsequently activate downstream signaling pathways (13-15). Specifically, among structural proteins, integrins mediate primarily cell-ECM interactions, whereas cadherins are responsible for cell-cell interactions (13). In vitro activation of integrins or inhibition of cadherins after ligation or dominant negative expression, respectively, results in negative regulation of human keratinocyte differentiation (16 -18). Furthermore, beyond structural proteins, Rho GTPases are also known to be an important component of keratinocyte differentiation pathways. Rho signaling has been shown to mediate cell-cell and cell-matrix adhesion...

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Section: Discussionmentioning

confidence: 96%

Section: Methodsmentioning

confidence: 99%

“…To examine the effect of ECM on cellular phenotype, cells were plated onto tissue culture plates coated with type I collagen (BD Biosciences) or laminin-5 (30,34).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Rho-ROCK-Myosin Signaling Meditates Membrane Type 1 Matrix Metalloproteinase-induced Cellular Aggregation of Keratinocytes

Dangi-Garimella

Redig

Shields

et al. 2010

Journal of Biological Chemistry

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“…Analysis of the internalized pool of E-cadherin was performed as described previously (31). Briefly, cells were surfacelabeled on ice with a sulfhydryl-cleavable biotin derivative (Sulfo-NHS-SS-Biotin at 1 mg/ml; Pierce), shifted to 37°C in the presence of bead-immobilized ␤1 integrin antibody or control IgG to induce integrin clustering for 1 h, and then treated with MESNA (100 mM) to remove any remaining surface-associated (i.e.…”

Section: Methodsmentioning

confidence: 99%

Integrin Regulation of β-Catenin Signaling in Ovarian Carcinoma

Burkhalter

Symowicz

Hudson

et al. 2011

Journal of Biological Chemistry

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Reversible modulation of integrin-regulated cell-matrix adhesion and epithelial (E)-cadherin-mediated cell-cell adhesion plays a critical role in the establishment of ovarian cancer metastases. In contrast to most epithelial cell-derived tumors that down-regulate E-cadherin expression during progression, acquisition of E-cadherin expression accompanies malignant transformation of the ovarian surface epithelium and is maintained in peritoneal metastases. Metastatic epithelial ovarian cancer cells are disseminated intraperitoneally and preferentially adhere via integrins to interstitial collagens in the peritoneal cavity. This study was undertaken to determine whether integrin engagement influences E-cadherin and ␤-catenin localization and function. The data demonstrate that multivalent integrin engagement results in increased internalization of E-cadherin, inhibition of GSK-3␤, elevated levels of nuclear ␤-catenin, increased ␤-catenin-regulated promoter activation, and transcriptional activation of Wnt/␤-catenin target genes. Blocking ␤-catenin transcriptional control with inhibitor of ␤-catenin and Tcf-4 reduces cellular invasion, suggesting a key role for ␤-catenin nuclear signaling in EOC invasion and metastasis. These studies support a model wherein cell-matrix engagement regulates the functional integrity of cell-cell contacts, leading to increased ␤-catenin nuclear signaling and enhanced cellular invasive activity. Furthermore, these results provide a mechanism for activation of Wnt/␤-catenin signaling in the absence of activating mutations in this pathway.Epithelial (E) 3 -cadherin is a single-span transmembrane glycoprotein that mediates calcium-dependent cell-cell adhesion via interaction with the extracellular domains of cadherins on the surface of neighboring cells (1, 2). Key functions of E-cadherin include the regulation of cell polarity and the maintenance of epithelial organization (3). Although most normal epithelia express high levels of E-cadherin, this cadherin is absent in the mesenchymally derived normal ovarian surface epithelium, which expresses neural (N)-cadherin. In most carcinomas, E-cadherin expression is down-regulated or lost, facilitating cellular dispersal, invasion, and metastasis (4). However, a unique feature of EOC is that E-cadherin becomes more abundant in primary differentiated carcinomas, with all histotypes displaying strong immunoreactivity (reviewed in Refs. 5, 6). There is less clarity regarding relative E-cadherin levels during ovarian tumor progression and metastasis. Although complete loss of E-cadherin is uncommon, reduced staining is often detected in late stage tumors and in ascites-derived tumor cells (7-9), and negative E-cadherin is predictive of poor overall survival (10, 11).␤-Catenin is found predominantly in association with the E-cadherin cytoplasmic domain at cell-cell junctions (12). In the absence of cell-cell contact and Wnt signaling, cytosolic ␤-catenin forms a complex with adenomatous poliosis coli, Axin/conductin, casein kinases 1␣ and 1⑀, and glyc...

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Slug is a downstream mediator of transforming growth factor‐β1‐induced matrix metalloproteinase‐9 expression and invasion of oral cancer cells

Joseph

Dangi-Garimella

Shields

et al. 2009

J of Cellular Biochemistry

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Members of Snail family of transcription factors play an important role in oral cancer progression by inducing epithelial-mesenchymal transition, by promoting invasion and by increasing matrix metalloproteinase (MMP) expression. Although Snail (Snai1) is the best characterized and the most extensively studied member of this family, the role and regulation of Slug (Snai2) in oral cancer progression is less well understood. In this report, we show that transforming growth factor-beta1 (TGF-beta1) increases Slug levels in tert-immortalized oral keratinocytes and in malignant oral squamous cell carcinoma (OSCC) cells. Inhibiting ERK1/2 signaling, but not PI3-kinase signaling, blocked TGF-beta1-induced Slug expression in the malignant UMSCC1 cells. To further examine the role of Slug in OSCC progression, we generated UMSCC1 cells with inducible expression of Slug protein. Induction of Slug in UMSCC1 cells did not repress E-cadherin levels or regulate individual movement of UMSCC1 cells. Instead, Slug enhanced cohort migration and Matrigel invasion by UMSCC1 cells. Slug increased MMP-9 levels and MMP-9-specific siRNA blocked Slug-induced Matrigel invasion. Interestingly, Slug-specific siRNA attenuated TGF-beta1-induced MMP-9 expression and Matrigel invasion. These data demonstrate that TGF-beta1 increases Slug via ERK1/2 signaling, and thereby contributes to OSCC progression.

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Calcium Regulation of Matrix Metalloproteinase-mediated Migration in Oral Squamous Cell Carcinoma Cells

Cited by 53 publications

References 72 publications

Rho-ROCK-Myosin Signaling Meditates Membrane Type 1 Matrix Metalloproteinase-induced Cellular Aggregation of Keratinocytes

Rho-ROCK-Myosin Signaling Meditates Membrane Type 1 Matrix Metalloproteinase-induced Cellular Aggregation of Keratinocytes

Integrin Regulation of β-Catenin Signaling in Ovarian Carcinoma

Slug is a downstream mediator of transforming growth factor‐β1‐induced matrix metalloproteinase‐9 expression and invasion of oral cancer cells

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