Inhibitory Effect of Green Tea Polyphenols on Membrane-Type 1 Matrix Metalloproteinase, MT1-MMP1)

Oku, Naoto; Matsukawa, Motomi; Yamakawa, Satoru; Asai, Tomohiro; Yahara, Shoji; Hashimoto, Fumio; Akizawa, Toshifumi

doi:10.1248/bpb.26.1235

Cited by 65 publications

(43 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One common intracellular pathway may also involve Ca 2ϩ /calmodulin-dependent signaling, which has been shown to regulate MT1-MMP cell surface processing (25), as well as the phosphorylation of CD44 required for cell migration on HA (62). Finally, we also report that EGCg, an effective inhibitor of MT1-MMP-mediated functions (36,63), also antagonized MT1-MMP-mediated cell surface HA-binding.…”

Section: Discussionmentioning

confidence: 52%

Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells

Annabi

Thibeault

Moumdjian

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Hyaluronan (HA) is a component of the brain extracellular matrix environment that is synthesized and secreted by glioma cells. The primary cell surface receptor for HA is CD44, a membrane glycoprotein that is functionally regulated by a membrane type 1 matrix metalloproteinase (MT1-MMP). Both CD44 and MT1-MMP are partially located in Triton X-100-insoluble domains, but no functional link has yet been established between them. In the present study, we studied the regulation of HA cell surface binding in U-87 glioma cells. We show that an MMP-dependent mechanism regulates the intrinsic cell surface binding of HA as ilomastat, a broad MMP inhibitor, increased HA binding to glioma cells. HA binding was also rapidly and specifically up-regulated by 3-fold by type I collagen in U-87 cells, which also induced a significant morphological reorganization associated with the activation of a latent form of MMP-2 through a MT1-MMP-mediated mechanism. Interestingly, caveolae depletion with a cell surface cholesteroldepleting agent ␤-cyclodextrin triggered an additional increase (9-fold) in the binding of HA, in synergy with type I collagen. On the other hand, HA cell surface binding was diminished by the MEK inhibitor PD98059 and by the overexpression of a recombinant, wild type MT1-MMP, whereas its cytoplasmic-deleted form had no effect. Taken together, our results suggest that MT1-MMP regulates, through its cytoplasmic domain, the cell surface functions of CD44 in a collagen-rich pericellular environment. Additionally, we describe a new molecular mechanism regulating the invasive potential of glioma cells involving a MT1-MMP/CD44/caveolin interaction, which could represent a potential target for anti-cancer therapies.The principal molecules that have been identified in the normal brain extracellular matrix (ECM) 1 are hyaluronan (HA; also known as hyaluronic acid, hyaluronate) and chondroitin sulfate (1, 2). HA is an important glycosaminoglycan constituent believed to be implicated in angiogenesis, the formation of new blood vessels from preexisting vasculature. Although the serum level of HA is already used as an indicator of progressive malignant disease (3), its effects on in vivo angiogenesis and endothelial cell (EC) function are complex and have been reported to depend on HA concentration and molecular size (4, 5). Accordingly, whereas high molecular weight HA was shown to inhibit EC functions (6), low molecular weight HA stimulated EC proliferation, tubulogenesis (6, 7), and neovascularization (8). Moreover, small HA polymers efficiently regulated CD44 cell surface functional expression and promoted tumor cell migration (9). Astrocytic tumors of the central nervous system express CD44 among other cell adhesion receptors of the integrin or immunoglobulin superfamily. Although HA is the principal ligand of CD44, other CD44 ligands include the ECM components collagen, fibronectin, laminin, and chondroitin sulfate, whereas mucosal addressin, serglycin, osteopontin, and the class II invariant chain represent ECM-unrelat...

show abstract

Section: Discussionmentioning

confidence: 52%

Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells

Annabi

Thibeault

Moumdjian

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Recombinant human soluble MT1-MMP was prepared according to the method described previously (Itoh et al, 1996;Oku et al, 2003). In brief, the cDNAs for procatalytic domains of human MT1-MMP were prepared by polymerase chain reactions using sets of primers (5' primer, GG CG GATCCAT-GCTCGCCTCCCTCGGCTCG, 3' primer, GCCGTC-GACGTTCCCGTCACAGATGTTGGG) based on the reported sequences, and the template (poly (A) + RNA isolated from a human rectal carcinoma cell line pME18S-MTMMP having a 3.5 Kb cDNA fragment of MT1-MMP).…”

Section: Preparation Of Recombinant Mt1-mmpmentioning

confidence: 99%

“…Inhibitory effects of various inhibitors were measured by a microplate reader assay method with fluorescence substrates described previously (Oku et al, 2003). Each 20 µl of inhibitor solution, assay buffer (50 mM Tris, pH 8.0, 5 mM CaCl 2 , 200 mM NaCl, and 50 µM ZnCl 2 , 0.1% Brij), distilled water and proteinase solution were mixed and pre-incubated in each well of 96 well microplates at 37°C for 15 min.…”

Section: Microplate Assaymentioning

confidence: 99%

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

et al. 2006

Self Cite

View full text Add to dashboard Cite

-During the characterization of hemorrhagic factor in venom of Rhabdophis tigrinus tigrinus, so-called Yamakagashi in Japan, one of the Colubridae family, a novel metalloproteinase with molecular weight of 38 kDa in the Duvernoy's gland of Yamakagashi was identified by gelatin zymography and by monitoring its proteolytic activity using a fluorescence peptide substrate, MOCAc-PLGLA 2 pr(Dnp)AR-NH 2 , which was developed for measuring the well-known matrix metalloproteinase (MMP) activity.After purification by gel filtration HPLC and/or column switch HPLC system consisting of an affinity column, which was immobilized with a synthetic BS-10 peptide (MQKPRCGVPD) originating from propeptide domain of MMP-7 and a reversed-phase column, the N-terminal amino acid sequence of the 38 kDa metalloproteinase was identified as FNTFPGDLK which shared a high homology to Xenopus MMP-9.The 38 kDa metalloproteinase required Zn 2+ and Ca 2+ ions for its proteolytic activity. In addition, the proteolytic activity was almost completely inhibited by BS-10, a MMP inhibitor, but not by the serine proteinase inhibitors, cysteine proteinase inhibitors and aspartic proteinase inhibitors.Together these results demonstrated that the 38 kDa proteinase is a novel snake verom metalloproteinase (SVMP) containing HExGHxxGxxH motif which possesses high affinity to the BS-10 peptide, into its molecule, and the enzymatic properties are closed to that of MMPs.Based on the results obtained in the present study, we concluded that the 38 kDa metalloproteinase is a novel metalloproteinase whose activity may be regulated by the cysteine switch mechanism, and could be classified as one of the matrix metalloproteinases rather than snake venom metalloproteinases.

show abstract

“…We synthesized four dimeric compounds: (9), and (+)-catechin- [4,8]-(−)-epigallocatechin (10) to determine which part is the most important for biological activities and if the total number of phenolic hydroxyl groups in the entire molecule correlates with biological properties. The synthesized compounds 7-10 are natural products that can be isolated from beverages, e.g., green tea [24] and beer [25], and are known as strongly bioactive polyphenols. Compounds 7-9 were synthesized using an electrophile 13 derived from commercially available (−)-epigallocatechin-3-O-gallate (EGCG: 4), as shown in Scheme 1.…”

Section: Resultsmentioning

confidence: 99%

Structure–Activity Relationship of Oligomeric Flavan-3-ols: Importance of the Upper-Unit B-ring Hydroxyl Groups in the Dimeric Structure for Strong Activities

et al. 2015

View full text Add to dashboard Cite

Proanthocyanidins, which are composed of oligomeric flavan-3-ol units, are contained in various foodstuffs (e.g., fruits, vegetables, and drinks) and are strongly biologically active compounds. We investigated which element of the proanthocyanidin structure is primarily responsible for this functionality. In this study, we elucidate the importance of the upper-unit of 4-8 condensed dimeric flavan-3-ols for antimicrobial activity against Saccharomyces cerevisiae (S. cerevisiae) and cervical epithelioid carcinoma cell line HeLa S3 proliferation inhibitory activity. To clarify the important constituent unit of proanthocyanidin, we synthesized four dimeric compounds, (−)-epigallocatechin- In addition to antimicrobial activity against S. cerevisiae and proliferation inhibitory activity on HeLa S3 cells, the correlation of 2,2-diphenyl-l-picrylhydrazyl radical scavenging activity with the number of phenolic hydroxyl groups was low. On the basis of the results of our SAR studies, we concluded that B-ring hydroxyl groups of the upper-unit of the dimer are crucially important for strong and effective activity.

show abstract

Inhibitory Effect of Green Tea Polyphenols on Membrane-Type 1 Matrix Metalloproteinase, MT1-MMP1)

Cited by 65 publications

References 17 publications

Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells

Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

Structure–Activity Relationship of Oligomeric Flavan-3-ols: Importance of the Upper-Unit B-ring Hydroxyl Groups in the Dimeric Structure for Strong Activities

Contact Info

Product

Resources

About