scholarly journals Invasion by activated macrophages requires delivery of nascent membrane‐type‐1 matrix metalloproteinase through late endosomes/lysosomes to the cell surface

Traffic ◽  
2019 ◽  
Author(s):  
Joan Röhl ◽  
Zoe E. West ◽  
Maren Rudolph ◽  
Andreea Zaharia ◽  
Derek Van Lonkhuyzen ◽  
...  
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Activated Macrophages ◽  
Late Endosomes ◽  
Membrane Type

scholarly journals Rapid Trafficking of Membrane Type 1-Matrix Metalloproteinase to the Cell Surface Regulates Progelatinase A Activation

2002 ◽  
Vol 82 (12) ◽  
pp. 1673-1684 ◽  
Author(s):  
Stanley Zucker ◽  
Michelle Hymowitz ◽  
Cathleen E Conner ◽  
Elizabeth A DiYanni ◽  
Jian Cao
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Membrane Type

scholarly journals The Oncogenic Response to MiR-335 Is Associated with Cell Surface Expression of Membrane-Type 1 Matrix Metalloproteinase (MT1-MMP) Activity

PLoS ONE ◽  
2015 ◽  
Vol 10 (7) ◽  
pp. e0132026 ◽  
Author(s):  
Fausto Rojas ◽  
Maria E. Hernandez ◽  
Milagros Silva ◽  
Lihua Li ◽  
Subbaya Subramanian ◽  
...  
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Membrane Type

scholarly journals Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP)

FEBS Letters ◽  
1996 ◽  
Vol 385 (3) ◽  
pp. 238-240 ◽  
Author(s):  
Hiroshi Sato ◽  
Takahisa Takino ◽  
Takeshi Kinoshita ◽  
Kazushi Imai ◽  
Yasunori Okada ◽  
...  
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Gelatinase A ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
Membrane Type

scholarly journals Increased Aggressiveness of Human Prostate PC-3 Tumor Cells Expressing Cell Surface Localized Membrane Type-1 Matrix Metalloproteinase (MT1-MMP)

2009 ◽  
Vol 30 (3) ◽  
pp. 259-274 ◽  
Author(s):  
X. Wang ◽  
M. J. Wilson ◽  
J. W. Slaton ◽  
A. A. Sinha ◽  
S. L. Ewing ◽  
...  
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Tumor Cells ◽  
Human Prostate ◽  
Membrane Type

scholarly journals Membrane interactions with membrane type 1 matrix metalloproteinase

2018 ◽  
Author(s):  
◽  
Tara Marcink
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Catalytic Domain ◽  
Membrane Surface ◽  
Membrane Binding ◽  
Tumor Cell Migration ◽  
Peripheral Protein ◽  
Membrane Type ◽  
Dynamics Simulations

Membrane type 1 matrix metalloproteinase (MT1-MMP) is essential to a myriad of extracellular activities including tumor cell migration and angiogenesis. At the cell surface, MT1-MMP is a major factor in the proteolysis of receptors, growth factors, and collagen. MT1-MMP extracellular domains bind the cell surface which can be influential in bringing these complexes together. This study uses new techniques to uncover the interactions between MT1-MMP and the cell surface. Described here is the development of techniques in protein and lipid preparations, NMR data acquisition, and structure determination by molecular dynamics simulations. Through these methods, the HPX domain was shown to bind nanodiscs by opposing tips of blade II and blade IV. The protruding part of these tips contain an EPGYPK sequence that are seen dipping into the membrane surface making contact with the lipid head groups. Blade IV membrane binding allows collagen to bind unhindered. Both blade II and blade IV membrane binding structures are shown to be favorable for homodimerization without disruption of the collagen binding site. The catalytic domain is shown to at least transiently bind membranes. This study then hypothesizes and discusses how these interactions impact both future peripheral protein membrane interaction studies and uncover similarities between the MMP family.

Cdc42 and RhoA have opposing roles in regulating membrane type 1-matrix metalloproteinase localization and matrix metalloproteinase-2 activation

2008 ◽  
Vol 295 (3) ◽  
pp. C600-C610 ◽  
Author(s):  
Eric Ispanovic ◽  
Damiano Serio ◽  
Tara L. Haas
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Actin Cytoskeleton ◽  
Cortical Actin ◽  
Rhoa Activity ◽  
Surface Localization ◽  
Cell Surface Localization ◽  
Membrane Type

Proteolysis of the basement membrane and interstitial matrix occurs early in the angiogenic process and requires matrix metalloproteinase (MMP) activity. Skeletal muscle microvascular endothelial cells exhibit robust actin stress fibers, low levels of membrane type 1 (MT1)-MMP expression, and minimal MMP-2 activation. Depolymerization of the actin cytoskeleton increases MT1-MMP expression and MMP-2 activation. Rho family GTPases are regulators of actin cytoskeleton dynamics, and their activity can be modulated in response to angiogenic stimuli such as vascular endothelial growth factor (VEGF). Therefore, we investigated their roles in MMP-2 and MT1-MMP production. Endothelial cells treated with H1152 [an inhibitor of Rho kinase (ROCK)] induced stress fiber depolymerization and an increase in cortical actin. Both MMP-2 and MT1-MMP mRNA increased, which translated into greater MMP-2 protein production and activation. ROCK inhibition rapidly increased cell surface localization of MT1-MMP and increased PI3K activity, which was required for MMP-2 activation. Constitutively active Cdc42 increased cortical actin polymerization, phosphatidylinositol 3-kinase activity, MT1-MMP cell surface localization, and MMP-2 activation similarly to inhibition of ROCK. Activation of Cdc42 was sufficient to decrease RhoA activity. Capillary sprout formation in a three-dimensional collagen matrix was increased in cultures treated with RhoAN19 or Cdc42QL and, conversely, decreased in cultures treated with dominant negative Cdc42N17. VEGF stimulation also induced activation of Cdc42 while inhibiting RhoA activity. Furthermore, VEGF-dependent activation of MMP-2 was reduced by inhibition of Cdc42. These results suggest that Cdc42 and RhoA have opposing roles in regulating cell surface localization of MT1-MMP and MMP-2 activation.

scholarly journals Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface

1998 ◽  
Vol 334 (2) ◽  
pp. 345-353 ◽  
Author(s):  
Kaisa LEHTI ◽  
Jouko LOHI ◽  
Heli VALTANEN ◽  
Jorma KESKI-OJA
Keyword(s):  
Cell Surface ◽  
Matrix Metalloproteinase ◽  
Human Fibroblasts ◽  
Proteolytic Processing ◽  
Gelatinase A ◽  
Surface Binding ◽  
Fibrosarcoma Cells ◽  
Subsequent Activation ◽  
Membrane Type

Human fibroblasts and HT-1080 fibrosarcoma cells express membrane-type-1 matrix metalloproteinase (MT1-MMP), the cell surface activator of gelatinase A, in separate forms of 63 kDa, 60 kDa and in some cases 43 kDa. In the present work the interrelationships between MT1-MMP processing and gelatinase A activation were analysed using HT-1080 fibrosarcoma cells as a model. It was found that MT1-MMP was synthesized as a 63 kDa protein, which was constitutively processed to a 60 kDa active enzyme with N-terminal Tyr112, as shown by immunoprecipitation, immunoblotting and sequence analyses. Co-immunoprecipitation results indicated that only the active 60 kDa form of MT1-MMP bound gelatinase A at the cell surface. Both the activation of pro-MT1-MMP and the membrane binding of the tissue inhibitor of metalloproteinases type 2 (TIMP-2) and gelatinase A, and subsequent activation of gelatinase A, were inhibited by calcium ionophores. Although the active MT1-MMP was required for cell surface binding and activation of gelatinase A, it was inefficient in activating gelatinase A in fibroblasts or in control HT-1080 cells alone. Low expression levels of TIMP-2 and rapid synthesis of MT1-MMP were found to be critical for gelatinase A activation. In HT-1080 cells, MT1-MMP was further processed to an inactive, 43 kDa cell surface form when overexpressed, or when the cells were treated with PMA. Under these conditions, the activated gelatinase A was detected in the culture medium, in cell membrane extracts and in MT1-MMP-containing complexes. These results indicate that proteolytic processing (activation and degradation/inactivation) of MT1-MMP and MT1-MMP/TIMP-2 relationships at the cell surface are important regulatory levels in the control of gelatinolytic activity.

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