Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity

Kim, Hye Nan; Chung, Hye Shin

doi:10.5483/bmbrep.2008.41.12.858

Cited by 25 publications

(16 citation statements)

References 17 publications

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“…As both the exocyst complex and VAMP7 are associated with lipid rafts (47,48), Cav-1 and these molecules may coordinately regulate the MT1-MMP transport in the same lipid raft compartment. Contradicting our conclusion, it was reported that overexpression of Cav-1 inhibits the activity of coexpressed MT1-MMP (49). Because overexpression of Cav-1 compromises lipid raft-mediated endocytic pathway (50), the strict control of the expression level of caveoin-1 may be required for the proper trafficking of lipid raft-associated MT1-MMP.…”

Section: Discussionmentioning

confidence: 75%

Lipid Rafts and Caveolin-1 Are Required for Invadopodia Formation and Extracellular Matrix Degradation by Human Breast Cancer Cells

et al. 2009

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Invadopodia are ventral membrane protrusions through which invasive cancer cells degrade the extracellular matrix. They are thought to function in the migration of cancer cells through tissue barriers, which is necessary for cancer invasion and metastasis. Although many protein components of invadopodia have been identified, the organization and the role of membrane lipids in invadopodia are not well understood. In this study, the role of lipid rafts, which are cholesterol-enriched membrane microdomains, in the assembly and function of invadopodia in human breast cancer cells was investigated. Lipid rafts are enriched, internalized, and dynamically trafficked at invadopodia sites. Perturbation of lipid raft formation due to depleting or sequestering membrane cholesterol blocked the invadopodiamediated degradation of the gelatin matrix. Caveolin-1 (Cav-1), a resident protein of lipid rafts and caveolae, accumulates at invadopodia and colocalizes with the internalized lipid raft membranes. Membrane type 1 matrix metalloproteinase (MT1-MMP), a matrix proteinase associated with invadopodia, is localized at lipid raft-enriched membrane fractions and cotrafficked and colocalized with Cav-1 at invadopodia. The small interfering RNA-mediated silencing of Cav-1 inhibited the invadopodia-mediated and MT1-MMP-dependent degradation of the gelatin matrix. Furthermore, Cav-1 and MT1-MMP are coexpressed in invasive human breast cancer cell lines that have an ability to form invadopodia. These results indicate that invadopodia are the sites where enrichment and trafficking of lipid rafts occur and that Cav-1 is an essential regulator of MT1-MMP function and invadopodia-mediated breast cancer cell invasion. [Cancer Res 2009;69(22):8594-602]

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Section: Discussionmentioning

confidence: 75%

Lipid Rafts and Caveolin-1 Are Required for Invadopodia Formation and Extracellular Matrix Degradation by Human Breast Cancer Cells

et al. 2009

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“…These studies suggest that enhanced endocytosis decreases MMP-2’s activity, but why? We mentioned above that MT1-MMP is important in the activation of MMP-2; however, the interaction between MT1-MMP and caveolin-1 can trigger the caveolin-1-dependent endocytosis of MT1-MMP [33,34], and Kim et al [35] also found that caveolin-1 inhibits MT1-MMP activity. Therefore, endocytosis may be crucial in decreasing MMP-2 activity (Figure 1 and Figure 2).…”

Section: The Regulation Of Mmp-2 and Mmp-9 Activitymentioning

confidence: 99%

MMP-2 and 9 in Chronic Kidney Disease

Cheng

Limbu

Wang

et al. 2017

IJMS

129

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Gelatinases are members of the matrix metalloproteinase (MMPs) family; they play an important role in the degradation of the extracellular matrix (ECM). This effect is also crucial in the development and progression of chronic kidney disease (CKD). Its expression, as well as its activity regulation are closely related to the cell signaling pathways, hypoxia and cell membrane structural change. Gelatinases also can affect the development and progression of CKD through the various interactions with tumor necrosis factors (TNFs), monocyte chemoattractant proteins (MCPs), growth factors (GFs), oxidative stress (OS), and so on. Currently, their non-proteolytic function is a hot topic of research, which may also be associated with the progression of CKD. Therefore, with the in-depth understanding about the function of gelatinases, we can have a more specific and accurate understanding of their role in the human body.

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“…It is known that MMP-14 internalization is controlled by a clathrin-or caveolae dependent endocytic pathway or by a combination of these two pathways (Annabi et al 2001;Galvez et al 2004;Jiang et al 2001;Kim and Chung 2008;Miki et al 2007;Remacle et al 2003;Uekita et al 2001;Wu et al 2005). Some GPI-anchored proteins are known to be delivered to recycling endosomes via a Cdc42-regulated, clathrin-independent pinocytic pathway (Sabharanjak et al 2002).…”

Section: Discussionmentioning

confidence: 99%

Rat forming incisor requires a rigorous ECM remodeling modulated by MMP/RECK balance

et al. 2009

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Reversion-inducing-cysteine-rich protein with Kazal motifs (RECK) is a single membrane-anchored MMP-regulator and regulates matrix metalloproteinases (MMP) 2, 9 and 14. In turn, MMPs are endopeptidases that play a pivotal role in remodeling ECM. In this work, we decided to evaluate expression pattern of RECK in growing rat incisor during, specifically focusing out amelogenesis process. Based on different kinds of ameloblasts, our results showed that RECK expression was conducted by secretory and post-secretory ameloblasts. At the secretory phase, RECK was localized in the infra-nuclear region of the ameloblast, outer epithelium, near blood vessels, and in the stellate reticulum. From the transition to the maturation phases, RECK was strongly expressed by non-epithelial immuno-competent cells (macrophages and/or dendritic-like cells) in the papillary layer. From the transition to the maturation stage, RECK expression was increased. RECK mRNA was amplified by RT-PCR from whole enamel organ. Here, we verified the presence of RECK mRNA during all stages of amelogenesis. These events were governed by ameloblasts and by non-epithelial cells residents in the enamel organ. Concluding, we found differential expression of MMPs-2, -9 and RECK in the different phases of amelogenesis, suggesting that the tissue remodeling is rigorously controlled during dental mineralization.

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Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity

Cited by 25 publications

References 17 publications

Lipid Rafts and Caveolin-1 Are Required for Invadopodia Formation and Extracellular Matrix Degradation by Human Breast Cancer Cells

Lipid Rafts and Caveolin-1 Are Required for Invadopodia Formation and Extracellular Matrix Degradation by Human Breast Cancer Cells

MMP-2 and 9 in Chronic Kidney Disease

Rat forming incisor requires a rigorous ECM remodeling modulated by MMP/RECK balance

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