scholarly journals Selective function-blocking monoclonal human antibody highlights the important role of membrane type-1 matrix metalloproteinase (MT1-MMP) in metastasis

Oncotarget ◽  
2016 ◽  
Vol 8 (2) ◽  
pp. 2781-2799 ◽  
Author(s):  
Albert G. Remacle ◽  
Piotr Cieplak ◽  
Dong Hyun Nam ◽  
Sergey A. Shiryaev ◽  
Xin Ge ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Human Antibody ◽  
Membrane Type

scholarly journals Piezo1 mediates angiogenesis through activation of MT1-MMP signaling

2019 ◽  
Vol 316 (1) ◽  
pp. C92-C103 ◽  
Author(s):  
Hojin Kang ◽  
Zhigang Hong ◽  
Ming Zhong ◽  
Jennifer Klomp ◽  
Kayla J. Bayless ◽  
...  
Keyword(s):  
Shear Stress ◽  
Wall Shear Stress ◽  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Sprouting Angiogenesis ◽  
Sphingosine 1 Phosphate ◽  
Wall Shear ◽  
Membrane Type

Angiogenesis is initiated in response to a variety of external cues, including mechanical and biochemical stimuli; however, the underlying signaling mechanisms remain unclear. Here, we investigated the proangiogenic role of the endothelial mechanosensor Piezo1. Genetic deletion and pharmacological inhibition of Piezo1 reduced endothelial sprouting and lumen formation induced by wall shear stress and proangiogenic mediator sphingosine 1-phosphate, whereas Piezo1 activation by selective Piezo1 activator Yoda1 enhanced sprouting angiogenesis. Similarly to wall shear stress, sphingosine 1-phosphate functioned by activating the Ca2+ gating function of Piezo1, which in turn signaled the activation of the matrix metalloproteinase-2 and membrane type 1 matrix metalloproteinase during sprouting angiogenesis. Studies in mice in which Piezo1 was conditionally deleted in endothelial cells demonstrated the requisite role of sphingosine 1-phosphate-dependent activation of Piezo1 in mediating angiogenesis in vivo. These results taken together suggest that both mechanical and biochemical stimuli trigger Piezo1-mediated Ca2+ influx and thereby activate matrix metalloproteinase-2 and membrane type 1 matrix metalloproteinase and synergistically facilitate sprouting angiogenesis.

scholarly journals Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development

2007 ◽  
Vol 124 (1) ◽  
pp. 11-22 ◽  
Author(s):  
Takashi Hasebe ◽  
Rebecca Hartman ◽  
Liezhen Fu ◽  
Tosikazu Amano ◽  
Yun-Bo Shi
Keyword(s):  
Xenopus Laevis ◽  
Matrix Metalloproteinase ◽  
Gelatinase A ◽  
Membrane Type

scholarly journals Conversion of Stationary to Invasive Tumor Initiating Cells (TICs): Role of Hypoxia in Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) Trafficking

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e38403 ◽  
Author(s):  
Jian Li ◽  
Stanley Zucker ◽  
Ashleigh Pulkoski-Gross ◽  
Cem Kuscu ◽  
Mihriban Karaayvaz ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Tumor Initiating Cells ◽  
Invasive Tumor ◽  
Membrane Type

scholarly journals Membrane Localization of Membrane Type 1 Matrix Metalloproteinase by CD44 Regulates the Activation of Pro-Matrix Metalloproteinase 9 in Osteoclasts

2013 ◽  
Vol 2013 ◽  
pp. 1-13 ◽  
Author(s):  
Meenakshi A. Chellaiah ◽  
Tao Ma
Keyword(s):  
Matrix Metalloproteinase ◽  
Surface Expression ◽  
Membrane Localization ◽  
Wild Type ◽  
Cd44 Expression ◽  
Sequence Of Events ◽  
Membrane Type ◽  
And Migration

CD44, MT1-MMP, and MMP9 are implicated in the migration of osteoclast and bone resorption. This study was designed to determine the functional relationship between CD44 and MT1-MMP in the activation of pro-MMP9. We used osteoclasts isolated from wild-type and CD44-null mice. Results showed that MT1-MMP is present in multiple forms with a molecular mass ~63, 55, and 45 kDa in the membrane of wild-type osteoclasts. CD44-null osteoclasts demonstrated a 55 kDa active MT1-MMP form in the membrane and conditioned medium. It failed to activate pro-MMP9 because TIMP2 binds and inhibits this MT1-MMP (~55 kDa) in CD44-null osteoclasts. The role of MT1-MMP in the activation of pro-MMP9, CD44 expression, and migration was confirmed by knockdown of MT1-MMP in wild-type osteoclasts. Although knockdown of MMP9 suppressed osteoclast migration, it had no effects on MT1-MMP activity or CD44 expression. These results suggest that CD44 and MT1-MMP are directly or indirectly involved in the regulation of pro-MMP9 activation. Surface expression of CD44, membrane localization of MT1-MMP, and activation of pro-MMP9 are the necessary sequence of events in osteoclast migration.

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