Matrilysin (MMP-7) degrades VE-cadherin and accelerates accumulation of beta-catenin in the nucleus of human umbilical vein endothelial cells

Ichikawa, Yasushi; Ishikawa, Takashi; Momiyama, Nobuyoshi; Kamiyama, Masako; Sakurada, Harumi; Matsuyama, Ryusei; Hasegawa, S.; Chishima, Takashi; Hamaguchi, Yohei; Fujii, Satoshi; Saito, Shuji; Kubota, Kaori; Hasegawa, Shingo; Ike, Hideyuki; Oki, Sadaaki; Shimada, Hiroshi

doi:10.3892/or.15.2.311

Cited by 37 publications

(40 citation statements)

References 16 publications

(18 reference statements)

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“…Thus, EBV and KSHV may promote B-cell proliferation by stabilizing ␤-catenin (34). ␤-catenin release from cadherins has been implicated in Wnt-dependent and Wnt-independent induction of transcription during cancer (34,39,44). While we did not observe increased ␤-catenin levels in cells coexpressing K5 and LANA and while K5 reduced the expression of Wnt target proteins (Fig.…”

Section: Discussioncontrasting

confidence: 51%

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Remodeling of Endothelial Adherens Junctions by Kaposi's Sarcoma-Associated Herpesvirus

Mansouri¹,

Rose²,

Moses³

et al. 2008

J Virol

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Vascular endothelial cadherin (VE-cadherin) connects neighboring endothelial cells (ECs) via interendothelial junctions and regulates EC proliferation and adhesion during vasculogenesis and angiogenesis. The cytoplasmic domain of VE-cadherin recruits ␣-and ␤-catenins and ␥-catenin, which interact with the actin cytoskeleton, thus modulating cell morphology. Dysregulation of the adherens junction/cytoskeletal axis is a hallmark of invasive tumors. We now demonstrate that the transmembrane ubiquitin ligase K5/MIR-2 of Kaposi's sarcoma-associated herpesvirus targets VE-cadherin for ubiquitin-mediated destruction, thus disturbing EC adhesion. In contrast, N-cadherin levels in K5-expressing cells were increased compared to those in control cells. Steady-state levels of ␣-and ␤-catenins and ␥-catenin in K5-expressing ECs were drastically reduced due to proteasomal destruction. Moreover, the actin cytoskeleton was rearranged, resulting in the dysregulation of EC barrier function as measured by electric cell-substrate impedance sensing. Our data represent the first example of a viral protein targeting adherens junction proteins and suggest that K5 contributes to EC proliferation, vascular leakage, and the reprogramming of the EC proteome during Kaposi's sarcoma tumorigenesis.

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Section: Discussioncontrasting

confidence: 51%

“…It was previously reported that ␤-catenin released from the cadherin scaffold induces the transcription of Wnt-regulated genes independently of Wnt signaling (39,50). Therefore, we examined the expression of the Wnt-/␤-catenin-regulated proteins cyclin D1 and survivin.…”

Section: Methodsmentioning

confidence: 99%

Remodeling of Endothelial Adherens Junctions by Kaposi's Sarcoma-Associated Herpesvirus

Mansouri¹,

Rose²,

Moses³

et al. 2008

J Virol

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“…As a possible underlying mechanism, this effect could be mediated by degradation of VE-cadherin and nuclear accumulation of b-catenin in HUVECs (Ichikawa et al, 2006). Additionally, in light of the secretion of VEGF (Huo et al, 2002) and CTGF (Brigstock, 1999) by HUVECs, the HUVEC proliferation induced by MMP-7 could also be explained by liberation of CTGF-sequestered VEGF, helping endothelial cells use the self-made VEGF.…”

Section: Mmp-7 Activates Latent Vegf From Fibroblasts T-k Ito Et Almentioning

confidence: 99%

The VEGF angiogenic switch of fibroblasts is regulated by MMP-7 from cancer cells

et al. 2007

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“…It has been demonstrated previously that when matrix metalloproteinases (MMPs) cleave an extracellular classic cadherin domain, β-catenin is removed from its position near the cell membrane and in many cases will translocate to the cell nucleus (Lochter et al, 1997;Sanceau et al, 2003;Ichikawa et al, 2006;Cowden Dahl et al, 2008;Dwivedi et al, 2009;Zheng et al, 2009;Lynch et al, 2010). This translocation is associated with cell movement (reviewed in Tanaka et al, 2011).…”

Section: Matrix Metalloproteinases and Cell Movementmentioning

confidence: 99%

Modulation of Cell-Cell Junctional Complexes by Matrix Metalloproteinases

Bartlett¹,

Smith

2012

J Dent Res

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The ameloblast cell layer of the enamel organ is in contact with the forming enamel as it develops into the hardest substance in the body. Ameloblasts move in groups that slide by one another as the enamel layer thickens. Each ameloblast is responsible for the formation of one enamel rod, and the rods are the mineralized trail that moving ameloblasts leave behind. Matrix metalloproteinases (MMPs) facilitate cell movement in various tissues during development, and in this review we suggest that the tooth-specific MMP, enamelysin (MMP20), facilitates ameloblast movements during enamel development. Mmp20 null mice have thin brittle enamel with disrupted rod patterns that easily abrades from the underlying dentin. Strikingly, the Mmp20 null mouse enamel organ morphology is noticeably dysplastic during latestage development, when MMP20 is no longer expressed. We suggest that in addition to its role of cleaving enamel matrix proteins, MMP20 also cleaves junctional complexes present on ameloblasts to foster the cell movement necessary for formation of the decussating enamel rod pattern. Therefore, inactivation of MMP20 would result in tight ameloblast cell-cell attachments that may cause maturation-stage enamel organ dysplasia. The tight ameloblast attachments would also preclude the ameloblast movement necessary to form decussating enamel rod patterns.

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Matrilysin (MMP-7) degrades VE-cadherin and accelerates accumulation of beta-catenin in the nucleus of human umbilical vein endothelial cells

Cited by 37 publications

References 16 publications

Remodeling of Endothelial Adherens Junctions by Kaposi's Sarcoma-Associated Herpesvirus

Remodeling of Endothelial Adherens Junctions by Kaposi's Sarcoma-Associated Herpesvirus

The VEGF angiogenic switch of fibroblasts is regulated by MMP-7 from cancer cells

Modulation of Cell-Cell Junctional Complexes by Matrix Metalloproteinases

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