Membrane-Type Matrix Metalloproteinases in Human Dermal Microvascular Endothelial Cells: Expression and Morphogenetic Correlation

Chan, Vincent T.; Zhang, Dan Ning; Nagaravapu, Usha; Hultquist, Kevin; Romero, Luz; Herron, G. Scott

doi:10.1046/j.1523-1747.1998.00416.x

Cited by 38 publications

(29 citation statements)

References 38 publications

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“…We also report a preferential involvement of MT1-MMP in CCL2-and CXCL8-versus CXCL12-induced angiogenesis in human ECs. Our data show that CCL2 and CXCL8, but not CXCL12, increased MT1-MMP surface expression in ECs similar to other angiogenic factors and inflammatory cytokines (31,32), in this case by partially inhibiting MT1-MMP internalization. In addition, CCL2 and CXCL8 increased MT1-MMP clustering at endothelial membrane protrusions, and this correlated with an increase in MT1-MMP activity.…”

Section: Discussionmentioning

confidence: 49%

Membrane Type 1-Matrix Metalloproteinase Is Regulated by Chemokines Monocyte-Chemoattractant Protein-1/CCL2 and Interleukin-8/CXCL8 in Endothelial Cells during Angiogenesis

Gálvez¹,

Genı́s²,

Matı́as-Román³

et al. 2005

Journal of Biological Chemistry

100

108

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We have investigated the putative role and regulation of membrane type 1-matrix metalloproteinase (MT1-MMP) in angiogenesis induced by inflammatory factors of the chemokine family. The absence of MT1-MMP from null mice or derived mouse lung endothelial cells or the blockade of its activity with inhibitory antibodies resulted in the specific decrease of in vivo and in vitro angiogenesis induced by CCL2 but not CXCL12. Similarly, CCL2-and CXCL8-induced tube formation by human endothelial cells (ECs) was highly dependent on MT1-MMP activity. CCL2 and CXCL8 significantly increased MT1-MMP surface expression, clustering, activity, and function in human ECs. Investigation of the signaling pathways involved in chemokine-induced MT1-MMP activity in ECs revealed that CCL2 and CXCL8 induced cortical actin polymerization and sustained activation of phosphatidylinositol 3-kinase (PI3K) and the small GTPase Rac. Inhibition of PI3K or actin polymerization impaired CCL2-induced MT1-MMP activity. Finally, dimerization of MT1-MMP was found to be enhanced by CCL2 in ECs in a PI3K-and actin polymerization-dependent manner. In summary, we identify MT1-MMP as a molecular target preferentially involved in angiogenesis mediated by CCL2 and CXCL8, but not CXCL12, and suggest that MT1-MMP dimerization might be an important mechanism of its regulation during angiogenesis.

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Section: Discussionmentioning

confidence: 49%

Membrane Type 1-Matrix Metalloproteinase Is Regulated by Chemokines Monocyte-Chemoattractant Protein-1/CCL2 and Interleukin-8/CXCL8 in Endothelial Cells during Angiogenesis

Gálvez¹,

Genı́s²,

Matı́as-Román³

et al. 2005

Journal of Biological Chemistry

100

108

View full text Add to dashboard Cite

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“…Reverse Transcriptase-Polymerase Chain Reaction (RT-PCR)-A total of 3 g of isolated RNA was subjected to first strand cDNA synthesis with Moloney-murine leukemia virus reverse transcriptase, RNase inhibitor (Roche Molecular Biochemicals), and oligo(dT) [12][13][14][15][16][17][18] primer (Life Technologies, Inc.) for 1 h at 37°C according to the manufacturer's instructions. One-tenth of the cDNA generated from the reverse transcriptase reaction was used for PCR amplification in the presence of Taq DNA polymerase (Roche Molecular Biochemicals) and oligonucleotide primers, 5Ј-CAG ATC TTC GGG GAC TAT TAC CAC-3Ј (sense) and 5Ј-CCT GTT GTC ATT CAT CTG TGT GTA CC-3Ј (antisense).…”

Section: Methodsmentioning

confidence: 99%

“…Recent studies have shown that MT1-MMP is an endogenous activator of pro-MMP-2 (9). On the other hand, the increased expression of MT1-MMP has been correlated with physiological and pathological events such as embryogenesis (10), wound healing (11), angiogenesis (12), rheumatoid arthritis (13), osteoarthritis (14). and tumor invasion (15)(16)(17).…”

Section: Extracellular Matrix (Ecm)mentioning

confidence: 99%

Furin-independent Pathway of Membrane Type 1-Matrix Metalloproteinase Activation in Rabbit Dermal Fibroblasts

Sato¹,

Kondo²,

Fujisawa³

et al. 1999

Journal of Biological Chemistry

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We investigated the gene expression and intracellular activity of processing protease furin and its involvement in the process of membrane type 1-matrix metalloproteinase (MT1-MMP) activation in rabbit dermal fibroblasts. When the rabbit fibroblasts were treated with concanavalin A (ConA), pro-MMP-2 was converted to an active 62-kDa MMP-2 through the appearance of a 64-kDa intermediate MMP-2. The ConA-induced pro-MMP-2 activation resulted from increasing the gene expression and production of MT1-MMP in the rabbit fibroblasts. Reverse transcriptase-polymerase chain reaction demonstrated that in rabbit dermal fibroblasts furin mRNA was detected and, unlike MT1-MMP, was not increased by ConA. These findings are further supported by the fact that the intracellular furin activity also was constitutively detected and was unchanged by the ConA treatment. Very similar phenomena were also observed in human uterine cervical fibroblasts, which are known to produce MT1-MMP by ConA stimulation. These results suggest that the expression of the furin gene and the intracellular activity are not regulated by ConA. On the other hand, neither a synthetic furin inhibitor, decanoyl-RVKR-CH 2 Cl (25-100 M) nor a furin antisense oligonucleotide (40 M) inhibited the MT1-MMP-mediated pro-MMP-2 activation in ConA-treated rabbit dermal fibroblasts, whereas these compounds interfered with pro-MMP-2 activation in ConA-treated human uterine cervical fibroblasts. Nonetheless, the furin antisense oligonucleotide completely suppressed furin gene expression in both rabbit and human fibroblasts. These results suggest that furin does not participate in the process of MT1-MMP activation induced by ConA in rabbit dermal fibroblasts.

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“…39 The evidence so far The smoking gun Already a substantial body of circumstantial evidence links the MMPs to angiogenesis. In vitro, endothelial cells (ECs) express a range of MMPs as well as TIMP-1, -2 and -3 [40][41][42] and it has been demonstrated that endothelial MMP expression and activity can be modulated by angiogenic factors. [43][44][45][46] Upregulated MMP expression has also been observed in blood vessels in vivo in several physiologic and pathologic conditions, indicating that MMPs are involved in the activity of the endothelium during these processes.…”

Section: Endogenous Inhibitors Of Metalloproteinasesmentioning

confidence: 99%

Metalloproteinases and their inhibitors in tumor angiogenesis

Handsley

Edwards

2005

Intl Journal of Cancer

264

211

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Angiogenesis is the process by which new blood vessels are formed from preexisting vasculature. It is an essential feature of the female reproductive cycle, embryonic development and wound repair. Angiogenesis has also been identified as a causal or contributing factor in several pathologies, including cancer, where it is a rate-limiting step during tumor progression. Matrix metalloproteinases (MMPs) are a family of soluble and membrane-anchored proteolytic enzymes that can degrade components of the extracellular matrix (ECM) as well as a growing number of modulators of cell function. Several of the MMPs, in particular the gelatinases and membrane-type 1 MMP (MT1-MMP), have been linked to angiogenesis. Potential roles for these proteases during the angiogenic process include degradation of the basement membrane and perivascular ECM components, unmasking of cryptic biologically relevant sites in ECM components, modulation of angiogenic factors and production of endogenous angiogenic inhibitors. This review brings together what is currently known about the functions of the MMPs and the closely related ADAM (a disintegrin and metalloproteinase domain) and ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) families in angiogenesis and considers how this information might be useful in manipulation of the angiogenic process, with a view to constraining tumor progression. ' 2005 Wiley-Liss, Inc.Key words: metalloproteinase; tumor; angiogenesis; tissue inhibitor of metalloproteinases; protease; extracellular matrix Angiogenesis is an essential feature of several physiologic processes such as the developmental growth of organs, wound healing and the female reproductive cycle. 1 It is also particularly significant in cancer progression, being a crucial step in the transition of a tumor from a hyperplastic but contained in situ state to a malignant phenotype. 2,3 To allow its growth beyond a certain critical size, a solid avascular tumor must develop its own blood supply in order to meet its growing metabolic requirements. 1 Vascularization of a tumor also provides a route for dissemination of the tumor cells to different sites around the body.Although angiogenesis appears to be the primary form of tumor vascularization, the malignant cells of a tumor can gain access to a blood supply through other means, such as via tumor-induced vasculogenesis, in which bone marrow-derived precursor endothelial cells contribute to the formation of tumor vessels. 4,5 Vasculogenic mimicry is another form of vessel formation that has been reported in certain tumor types, such as aggressive human uveal melanomas, prostate and breast tumors. [6][7][8] In these cases, networks of tumor cell-lined vascular channels were identified within the tumors. Finally, vessel co-option, implemented by tumor cells as a temporary means of gaining access to a blood supply, involves the tumor cells growing around and thus co-opting existing host vessels to form an initially well-vascularized tumor. 9 This review will highlight new insigh...

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Membrane-Type Matrix Metalloproteinases in Human Dermal Microvascular Endothelial Cells: Expression and Morphogenetic Correlation

Cited by 38 publications

References 38 publications

Membrane Type 1-Matrix Metalloproteinase Is Regulated by Chemokines Monocyte-Chemoattractant Protein-1/CCL2 and Interleukin-8/CXCL8 in Endothelial Cells during Angiogenesis

Membrane Type 1-Matrix Metalloproteinase Is Regulated by Chemokines Monocyte-Chemoattractant Protein-1/CCL2 and Interleukin-8/CXCL8 in Endothelial Cells during Angiogenesis

Furin-independent Pathway of Membrane Type 1-Matrix Metalloproteinase Activation in Rabbit Dermal Fibroblasts

Metalloproteinases and their inhibitors in tumor angiogenesis

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