Membrane-type matrix metalloproteinases (MT-MMPs) in human endometrium during the cycle

2006 ◽  
Vol 45 (3) ◽  
pp. e124
Author(s):  
Margreet Plaisier ◽  
Pieter Koolwijk ◽  
Clarissa Jungerius ◽  
Elle K.J. Risse ◽  
Frans Helmerhorst ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Human Endometrium ◽  
Membrane Type

scholarly journals Membrane-type matrix metalloproteinases and vascularization in human endometrium during the menstrual cycle

2006 ◽  
Vol 12 (1) ◽  
pp. 11-18 ◽  
Author(s):  
Margreet Plaisier ◽  
Pieter Koolwijk ◽  
Roeland Hanemaaijer ◽  
Robert A. Verwey ◽  
Robin M.F. van der Weiden ◽  
...  
Keyword(s):  
Menstrual Cycle ◽  
Matrix Metalloproteinases ◽  
Human Endometrium ◽  
Membrane Type

scholarly journals Suppression of matrix metalloproteinases inhibits establishment of ectopic lesions by human endometrium in nude mice.

1997 ◽  
Vol 99 (12) ◽  
pp. 2851-2857 ◽  
Author(s):  
K L Bruner ◽  
L M Matrisian ◽  
W H Rodgers ◽  
F Gorstein ◽  
K G Osteen
Keyword(s):  
Matrix Metalloproteinases ◽  
Nude Mice ◽  
Human Endometrium

scholarly journals Membrane-type matrix metalloproteinases mediate curcumin-induced cell migration in non-tumorigenic colon epithelial cells differing in Apc genotype

2002 ◽  
Vol 23 (6) ◽  
pp. 1065-1070 ◽  
Author(s):  
Jenifer I. Fenton ◽  
Margaret S. Wolff ◽  
Michael W. Orth ◽  
Norman G. Hord
Keyword(s):  
Cell Migration ◽  
Epithelial Cells ◽  
Matrix Metalloproteinases ◽  
Membrane Type

scholarly journals Detection of a latent soluble form of membrane type 1 matrix metalloprotease bound with tissue inhibitor of matrix metalloproteinases-2 in periprosthetic tissues and fluids from loose arthroplasty endoprostheses

FEBS Journal ◽  
2013 ◽  
Vol 280 (24) ◽  
pp. 6541-6555 ◽  
Author(s):  
Anna Niarakis ◽  
Eleftheria Giannopoulou ◽  
Panagiota Ravazoula ◽  
Elias Panagiotopoulos ◽  
Ioannis K. Zarkadis ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Soluble Form ◽  
Matrix Metalloprotease ◽  
Tissue Inhibitor ◽  
Membrane Type

Expression of membrane-type 5 matrix metalloproteinase in human endometrium and endometriosis

2007 ◽  
Vol 23 (10) ◽  
pp. 567-573 ◽  
Author(s):  
Regine Gaetje ◽  
Uwe Holtrich ◽  
Knut Engels ◽  
Katherina Kourtis ◽  
Eva Cikrit ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Human Endometrium ◽  
Membrane Type

Membrane type-matrix metalloproteinases (MT-MMP)

2003 ◽  
pp. 1-74 ◽  
Author(s):  
Stanley Zucker ◽  
Duanqing Pei ◽  
Jian Cao ◽  
Carlos Lopez-Otin
Keyword(s):  
Matrix Metalloproteinases ◽  
Membrane Type

scholarly journals Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

2020 ◽  
Vol 21 (12) ◽  
pp. 4383
Author(s):  
Katherine Falkowski ◽  
Ewa Bielecka ◽  
Ida B. Thøgersen ◽  
Oliwia Bocheńska ◽  
Karolina Płaza ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Gelatin Zymography ◽  
Amino Acid Sequences ◽  
Initial Assessment ◽  
Edman Degradation ◽  
Activation Domain ◽  
Additional Layer ◽  
Murine Fibroblasts ◽  
Membrane Type

Kallikrein-related peptidases (KLKs) and matrix metalloproteinases (MMPs) are secretory proteinases known to proteolytically process components of the extracellular matrix, modulating the pericellular environment in physiology and in pathologies. The interconnection between these families remains elusive. To assess the cross-activation of these families, we developed a peptide, fusion protein-based exposition system (Cleavage of exposed amino acid sequences, CleavEx) aiming at investigating the potential of KLK14 to recognize and hydrolyze proMMP sequences. Initial assessment identified ten MMP activation domain sequences which were validated by Edman degradation. The analysis revealed that membrane-type MMPs (MT-MMPs) are targeted by KLK14 for activation. Correspondingly, proMMP14-17 were investigated in vitro and found to be effectively processed by KLK14. Again, the expected neo-N-termini of the activated MT-MMPs was confirmed by Edman degradation. The effectiveness of proMMP activation was analyzed by gelatin zymography, confirming the release of fully active, mature MT-MMPs upon KLK14 treatment. Lastly, MMP14 was shown to be processed on the cell surface by KLK14 using murine fibroblasts overexpressing human MMP14. Herein, we propose KLK14-mediated selective activation of cell-membrane located MT-MMPs as an additional layer of their regulation. As both, KLKs and MT-MMPs, are implicated in cancer, their cross-activation may constitute an important factor in tumor progression and metastasis.

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