Glioma cell extracellular matrix metalloproteinase inducer (EMMPRIN) (CD147) stimulates production of membrane-type matrix metalloproteinases and activated gelatinase A in co-cultures with brain-derived fibroblasts

Sameshima, Tetsuro; Nabeshima, Kazuki; Toole, Bryan P.; Yokogami, Kiyotaka; Okada, Yasunori; Goya, Tomokazu; Koono, Masashi; Wakisaka, Shinichiro

doi:10.1016/s0304-3835(00)00485-7

Cited by 157 publications

(119 citation statements)

References 30 publications

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“…Using CD147-transfected COS cells and immobilized recombinant CD147-Fc fusion protein, it was revealed that CD147 engages in a homophilic interaction, providing evidence that CD147 may be a counterreceptor for itself. 57 While this finding provides an important clue, there may be other counterreceptor interactions between CD147 and unidentified cell-surface molecules because CD147 expression was not shown in peritumoral fibroblasts and connective tissue in the previous studies 12,16 as well as the present study. Lim et al 13 investigated the signaling pathway mediating CD147 stimulation of fibroblast MMP-1 production and determined that protein tyrosine kinase and p38 mitogen-activated protein kinase were involved in the response; however, no upstream cell-surface receptor was identified.…”

Section: Discussionmentioning

confidence: 52%

“…4 CD147 is more highly expressed on the surface of most human carcinoma cells compared to their normal counterparts and correlates with tumor progression and invasion by stimulating peritumoral fibroblasts to produce elevated levels of several MMPs. 4,[11][12][13][14][15][16] These results imply that a CD147 counterreceptor might exist on the surface of fibroblasts, but none has been identified. Using CD147-transfected COS cells and immobilized recombinant CD147-Fc fusion protein, it was revealed that CD147 engages in a homophilic interaction, providing evidence that CD147 may be a counterreceptor for itself.…”

Section: Discussionmentioning

confidence: 99%

“…4,11 Expression of EMMPRIN is enhanced in a variety of human carcinomas and correlates with tumor progression and invasion by inducing production of MMPs by stromal cells. 4,[11][12][13][14][15][16] It was also shown in vitro that recombinant EMMPRIN purified from Chinese hamster ovary cells transfected with cDNA for human EMMPRIN stimulates cultured human fibroblasts to produce MMP-1, MMP-2 and MMP-3. 17 EMMPRIN not only stimulates the production of interstitial collagenase (MMP-1) but also forms a complex with MMP-1 at the human lung carcinoma cell surface, which would facilitate invasive processes.…”

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confidence: 99%

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Basigin (cd147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts

Kanekura

Chen

Kanzaki

2002

Intl Journal of Cancer

267

210

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Key words: basigin (CD147); malignant melanoma; invasion; metastasis; matrix metalloproteinaseBasigin (CD147), a transmembrane glycoprotein belonging to the Ig superfamily, was cloned from F9 embryonic carcinoma cells. 1 The Ig domain has strong homology with both the Ig variable domain and the major histocompatibility complex class II ␤ chain. It is expressed in various embryonic and adult tissues. 1,2 Because of its broad distribution, it was expected that basigin plays fundamental roles in various physiologic processes. Molecules identical to basigin were subsequently identified and given different names: M6 3 and EMMPRIN 4 in human; HT7, 5 neurothelin 6 and 5A11 7 in chicken; gp42 8 in mouse; and OX-47 9 and CE9 10 in rat. Of them, EMMPRIN, previously termed TCSF, has been implicated in the induction of MMPs. 4,11 Expression of EMMPRIN is enhanced in a variety of human carcinomas and correlates with tumor progression and invasion by inducing production of MMPs by stromal cells. 4,[11][12][13][14][15][16] It was also shown in vitro that recombinant EMMPRIN purified from Chinese hamster ovary cells transfected with cDNA for human EMMPRIN stimulates cultured human fibroblasts to produce MMP-1, MMP-2 and MMP-3. 17 EMMPRIN not only stimulates the production of interstitial collagenase (MMP-1) but also forms a complex with MMP-1 at the human lung carcinoma cell surface, which would facilitate invasive processes. 18 MMPs are a family of enzymes that degrade different components of the ECM, and a number of studies indicate that they play an important role in tissue remodeling, tumor invasion and metastasis. 19 -24 There are 2 distinct types of MMP, secreted and nonsecreted. Based on their substrate specificities, secreted MMPs are classified into collagenases (MMP-1, MMP-8 and MMP-13), gelatinases (MMP-2 and MMP-9) and stromelysins (MMP-3 and MMP-10). 20 Several nonsecreted MMPs are bound to membranes and designated MT-MMPs. 25 Tumor spread is a multistep process, which requires degradation or breakdown of the ECM and connective tissue and is caused by the concerted effects of these MMPs. 26 In the initial stage of tumor invasion, the gelatinases, particularly MMP-2, degrade components of the basement membrane, including type IV collagen. Although MMP-3, one of the stromelysins, also breaks down type IV collagen of the basement membrane, it degrades a variety of matrix components, including proteoglycans and noncollagenous glycoproteins such as laminin and fibronectin. Local tumor invasion is facilitated by collagenases, particularly MMP-1, which degrades the ECM. 20 MT1-MMP triggers tumor invasion by activating MMP-2. 25,27,28 Cutaneous MM is characterized by a high potential for invasion and metastasis. Previous studies reported the involvement of MMPs in migration, invasion, metastasis and progression of MM. Elevated expression of MMP-1, MMP-2 or MMP-9 was correlated with migration and invasion of cultured human melanoma cells. 21,22,29,30 In human melanoma lesions, positive correlations between tumor progressio...

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Section: Discussionmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Basigin (cd147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts

Kanekura

Chen

Kanzaki

2002

Intl Journal of Cancer

267

210

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“…A similar role within the microenvironment of brain tumors has also been suggested. Co-cultures of brainderived human fibroblasts involving interactions with glioblastoma cells induced production and activation of matrix metalloproteinase MMP2, and its activators MT1-MMP and MT2-MMP (Sameshima et al, 2000). These metalloproteinases have all been shown to be involved in the progression of gliomas (Belien et al, 1999;Sawaya et al, 1996;Uhm et al, 1996).…”

Section: Fibroblasts In the Brain Tumor Microenvironmentmentioning

confidence: 99%

The brain tumor microenvironment

Charles

Holland

Gilbertson

et al. 2011

Glia

687

327

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High-grade brain tumors are heterogeneous with respect to the composition of bona fide tumor cells and with respect to a range of intermingling parenchymal cells. Glioblastomas harbor multiple cell types, some with increased tumorigenicity and stem cell-like capacity. The stem-like cells may be the cells of origin for tumor relapse. However, the tumor-associated parenchymal cells such as vascular cells, microglia, peripheral immune cells, and neural precursor cells also play a vital role in controlling the course of pathology. In this review, we describe the multiple interactions of bulk glioma cells and glioma stem cells with parenchymal cell populations and highlight the pathological impact as well as signaling pathways known for these types of cell-cell communication. The tumor-vasculature not only nourishes glioblastomas, but also provides a specialized niche for these stem-like cells. In addition, microglial cells, which can contribute up to 30% of a brain tumor mass, play a role in glioblastoma cell invasion. Moreover, non-neoplastic astrocytes can be converted into a reactive phenotype by the glioma microenvironment and can then secrete a number of factors which influences tumor biology. The young brain may have the capacity to inhibit gliomagenesis by the endogenous neural precursor cells, which secrete tumor suppressive factors. The factors, pathways, and interactions described in this review provide a new prospective on the cell biology of primary brain tumors, which may ultimately generate new treatment modalities. However, our picture of the multiple interactions between parenchymal and tumor cells is still incomplete. V

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“…MT1-MMP activation pathways have been demonstrated by concavalin A stimulation, cytokine treatments and chemokine exposure (Yu et al, 1997;Sameshima et al, 2000;Bartolome et al, 2004). Proper localization and trafficking of MT1-MMP to the plasma membrane are also very important mechanisms of functional regulation (Mori et al, 2002;Remacle et al, 2003;Rozanov et al, 2004;Wang et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Hypoxia stimulates breast carcinoma cell invasion through MT1-MMP and MMP-2 activation

et al. 2005

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The process of cancer cell invasion involves degradation of the extracellular matrix (ECM) by proteases, integrin adhesion and cell motility. The role of ECM degrading proteases on the hypoxia-induced invasion of breast carcinoma cells was investigated. Hypoxia markedly increased the invasion capacity of MDA-MB-231 and MDA-MB-435 breast carcinoma cell lines. Matrix metalloproteinase (MMP) inhibitors blocked the hypoxia-induced invasion, whereas other protease inhibitors had no effect. Antibodies or siRNAs blocking either membrane type-1 MMP (MT1-MMP) or MMP-2 were effective in reducing the hypoxia-induced invasion. Serumfree reconstitution experiments confirmed the involvement of the MT1-MMP/MMP-2/tissue inhibitor of metalloproteinase-2 complex in this hypoxia-induced response. Overexpression of MT1-MMP in a poorly invasive breast cancer cell line, T47-D, promoted hypoxia-induced invasion and MMP-2 activation. Cell surface accumulation and activation of MT1-MMP without apparent regulation at the mRNA or protein levels indicated a post-translational adaptive response to hypoxia. Inhibition of the small GTPase RhoA eliminated the hypoxiainduced invasion and blocked the localization of MT1-MMP to the plasma membrane. Zymographic and molecular analysis of human breast tumors showed a strong correlation between hypoxic microenvironments and MMP-2 activation without changes in MT1-MMP expression. Our studies suggest that hypoxic tumor microenvironments promote breast cancer invasion through an MT1-MMP-dependent mechanism.

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Glioma cell extracellular matrix metalloproteinase inducer (EMMPRIN) (CD147) stimulates production of membrane-type matrix metalloproteinases and activated gelatinase A in co-cultures with brain-derived fibroblasts

Cited by 157 publications

References 30 publications

Basigin (cd147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts

Basigin (cd147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts

The brain tumor microenvironment

Hypoxia stimulates breast carcinoma cell invasion through MT1-MMP and MMP-2 activation

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