scholarly journals Phosphorylation of Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) and Its Vesicle-associated Membrane Protein 7 (VAMP7)-dependent Trafficking Facilitate Cell Invasion and Migration

2011 ◽  
Vol 286 (50) ◽  
pp. 43405-43416 ◽  
Author(s):  
Karla C. Williams ◽  
Marc G. Coppolino
Keyword(s):  
Membrane Protein ◽  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Invasion And Migration ◽  
Membrane Type ◽  
And Migration

scholarly journals SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) mediate trafficking of membrane type 1–matrix metalloproteinase (MT1-MMP) during invadopodium formation and tumor cell invasion

2014 ◽  
Vol 25 (13) ◽  
pp. 2061-2070 ◽  
Author(s):  
Karla C. Williams ◽  
Rachael E. McNeilly ◽  
Marc G. Coppolino
Keyword(s):  
Membrane Protein ◽  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Cellular Invasion ◽  
Protein Receptor ◽  
Ecm Degradation ◽  
Membrane Type ◽  
Regulated Trafficking

Movement through the extracellular matrix (ECM) requires cells to degrade ECM components, primarily through the action of matrix metalloproteinases (MMPs). Membrane type 1–matrix metalloproteinase (MT1-MMP) has an essential role in matrix degradation and cell invasion and localizes to subcellular degradative structures termed invadopodia. Trafficking of MT1-MMP to invadopodia is required for the function of these structures, and here we examine the role of N-ethylmaleimide–sensitive factor–activating protein receptor (SNARE)–mediated membrane traffic in the transport of MT1-MMP to invadopodia. During invadopodium formation in MDA-MB-231 human breast cancer cells, increased association of SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) is detected by coimmunoprecipitation. Blocking the function of these SNAREs perturbs invadopodium-based ECM degradation and cell invasion. Increased level of SNAP23-Syntaxin4-VAMP7 interaction correlates with decreased Syntaxin4 phosphorylation. These results reveal an important role for SNARE-regulated trafficking of MT1-MMP to invadopodia during cellular invasion of ECM.

Neutrophil-derived serine proteinases enhance membrane type-1 matrix metalloproteinase–dependent tumor cell invasion

Surgery ◽  
2000 ◽  
Vol 127 (2) ◽  
pp. 142-147 ◽  
Author(s):  
Peter Shamamian ◽  
Ben J.Z. Pocock ◽  
Jess D. Schwartz ◽  
Sara Monea ◽  
Neal Chuang ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Tumor Cell ◽  
Cell Invasion ◽  
Tumor Cell Invasion ◽  
Serine Proteinases ◽  
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.

scholarly journals Upregulation of SPOCK2 inhibits the invasion and migration of prostate cancer cells by regulating the MT1-MMP/MMP2 pathway

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7163 ◽  
Author(s):  
Gang Liu ◽  
Fang Ren ◽  
Yongsheng Song
Keyword(s):  
Prostate Cancer ◽  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Mrna Level ◽  
Matrix Metalloproteinase 2 ◽  
Lncap Cells ◽  
Prostate Hyperplasia ◽  
Invasion And Migration ◽  
Messenger Ribonucleic Acid ◽  
And Migration

Background It is known that secreted protein acidic and cysteine rich (osteonectin), cwcv and kazal-like domains proteoglycan 2 (SPOCK2) plays a significant role in the development and progression of several human cancers; however, the role of SPOCK2 in prostate cancer (PCa) remains unclear. This study aimed to find the role and mechanism of SPOCK2 in the development and progression of PCa. Methods The messenger ribonucleic acid (mRNA) expression of SPOCK2 in PCa tissue was detected by real-time polymerase chain reaction (PCR). Upregulation of the SPOCK2 gene was achieved using the DU145 and LNCaP cells by transfecting the cells with SPOCK2 recombinant fragment. Cell invasion and migration ability were detected by transwell chamber and wound healing assay. The expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) and matrix metalloproteinase 2 (MMP2) in the cells was detected by Western Blot and zymography gel assay. Results The mRNA level of SPOCK2 was significantly lower in the PCa tissue compared to benign prostate hyperplasia. Upregulation of SPOCK2 inhibited cell invasion and migration in DU145 and LNCaP cells, inhibited the expression of MT1-MMP and MMP2 and, inhibited activation of MMP2 in DU145 and LNCaP cells. Conclusion SPOCK2 is associated with the progression of PCa. Upregulation of SPOCK2 can inhibit PCa cell invasion and metastasis by decreasing MT1-MMP and MMP2 gene expression and decreasing MMP2 protein activation.

A novel celecoxib analog UTX-121 inhibits HT1080 cell invasion by modulating membrane-type 1 matrix metalloproteinase

2020 ◽  
Vol 521 (1) ◽  
pp. 137-144
Author(s):  
Hirari Yamahana ◽  
Takahisa Takino ◽  
Yoshio Endo ◽  
Hisatsugu Yamada ◽  
Takeshi Suzuki ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Ht1080 Cell ◽  
Membrane Type
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