Fluorescence imaging to assess the matrix metalloproteinase activity and its inhibitor in vivo

2008 ◽  
Vol 13 (1) ◽  
pp. 011006 ◽  
Author(s):  
Zhihong Zhang ◽  
Jie Yang ◽  
Jinling Lu ◽  
Juqiang Lin ◽  
Shaoqun Zeng ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Fluorescence Imaging ◽  
The Matrix ◽  
Metalloproteinase Activity

scholarly journals Overexpression of the Matrix Metalloproteinase Matrilysin Results in Premature Mammary Gland Differentiation and Male Infertility

1998 ◽  
Vol 9 (2) ◽  
pp. 421-435 ◽  
Author(s):  
Laura A. Rudolph-Owen ◽  
Paul Cannon ◽  
Lynn M. Matrisian
Keyword(s):  
Matrix Metalloproteinase ◽  
Transgenic Animals ◽  
Reproductive Organs ◽  
Mammary Development ◽  
Seminiferous Tubules ◽  
Interstitial Tissue ◽  
Wild Type ◽  
The Matrix

To examine the role of matrilysin (MAT), an epithelial cell-specific matrix metalloproteinase, in the normal development and function of reproductive tissues, we generated transgenic animals that overexpress MAT in several reproductive organs. Three distinct forms of human MAT (wild-type, active, and inactive) were placed under the control of the murine mammary tumor virus promoter/enhancer. Although wild-type, active, and inactive forms of the human MAT protein could be produced in an in vitro culture system, mutations of the MAT cDNA significantly decreased the efficiency with which the MAT protein was produced in vivo. Therefore, animals carrying the wild-type MAT transgene that expressed high levels of human MAT in vivo were further examined. Mammary glands from female transgenic animals were morphologically normal throughout mammary development, but displayed an increased ability to produce β-casein protein in virgin animals. In addition, beginning at approximately 8 mo of age, the testes of male transgenic animals became disorganized with apparent disintegration of interstitial tissue that normally surrounds the seminiferous tubules. The disruption of testis morphology was concurrent with the onset of infertility. These results suggest that overexpression of the matrix-degrading enzyme MAT alters the integrity of the extracellular matrix and thereby induces cellular differentiation and cellular destruction in a tissue-specific manner.

Discovery and development of a type II collagen neoepitope (TIINE) biomarker for matrix metalloproteinase activity: From in vitro to in vivo

2007 ◽  
Vol 361 (1) ◽  
pp. 93-101 ◽  
Author(s):  
O.V. Nemirovskiy ◽  
D.R. Dufield ◽  
T. Sunyer ◽  
P. Aggarwal ◽  
D.J. Welsch ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Metalloproteinase Activity

scholarly journals Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo

Blood ◽  
2002 ◽  
Vol 100 (4) ◽  
pp. 1160-1167 ◽  
Author(s):  
G. Angus McQuibban ◽  
Jiang-Hong Gong ◽  
Julie P. Wong ◽  
John L. Wallace ◽  
Ian Clark-Lewis ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Chemokine Receptor ◽  
Chemokine Receptors ◽  
Leukemic Cell ◽  
Proteolytic Processing ◽  
Cc Chemokine ◽  
Monocyte Chemoattractant ◽  
The Matrix

Monocyte chemoattractant protein (MCP)–3 is inactivated upon cleavage by the matrix metalloproteinase (MMP) gelatinase A (MMP-2). We investigated the susceptibility to proteolytic processing of the 4 human MCPs by 8 recombinant MMPs to determine whether MCP-3 is an isolated example or represents a general susceptibility of chemokines to proteolytic inactivation by these important inflammatory proteases. In addition to MMP-2, MCP-3 is efficiently cleaved by membrane type 1 (MT1)–MMP, the cellular activator of MMP-2, and by collagenase-1 and collagenase-3 (MMP-1, MMP-13) and stromelysin-1 (MMP-3). Specificity was shown by absence of cleavage by matrilysin (MMP-7) and the leukocytic MMPs neutrophil collagenase (MMP-8) and gelatinase B (MMP-9). The closely related chemokines MCP-1, MCP-2, and MCP-4 were not cleaved by MMP-2 or MT1-MMP, but were cleaved by MMP-1 and MMP-3 with varying efficiency. MCPs were typically cleaved between residues 4 and 5, but MCP-4 was further processed at Val7-Pro8. Synthetic MCP analogs corresponding to the MMP-cleaved forms bound CC chemokine receptor (CCR)–2 and CCR-3, but lacked chemoattractant activity in pre-B cells transfected with CCR-2 and CCR-3 or in THP-1 monocytic cells, a transformed leukemic cell line. Moreover, the truncated products of MCP-2 and MCP-4, like MCP-3, were potent antagonists of their cognate CC chemokine receptors in transwell cell migration assays in vitro. When they were injected 24 hours after the initiation of carrageenan-induced inflammation in rat paws, their in vivo antagonist activities were revealed by a greater than 66% reduction in inflammatory edema progression after 12 hours. We propose that MMPs have an important role in modulating inflammatory and immune responses by processing chemokines in wound healing and in disease.

scholarly journals Scintigraphic Imaging of Matrix Metalloproteinase Activity in the Arterial Wall In Vivo

Circulation ◽  
2004 ◽  
Vol 109 (21) ◽  
pp. 2554-2559 ◽  
Author(s):  
Michael Schäfers ◽  
Burkhard Riemann ◽  
Klaus Kopka ◽  
Hans-Jörg Breyholz ◽  
Stefan Wagner ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Arterial Wall ◽  
Scintigraphic Imaging ◽  
Metalloproteinase Activity

In Vivo Migration of Transplanted Myoblasts Requires Matrix Metalloproteinase Activity

2000 ◽  
Vol 258 (2) ◽  
pp. 279-287 ◽  
Author(s):  
E. El Fahime ◽  
Y. Torrente ◽  
N.J. Caron ◽  
M.D. Bresolin ◽  
J.P. Tremblay
Keyword(s):  
Matrix Metalloproteinase ◽  
Metalloproteinase Activity

scholarly journals NADPH Oxidase Restrains the Matrix Metalloproteinase Activity of Macrophages

2005 ◽  
Vol 280 (34) ◽  
pp. 30201-30205 ◽  
Author(s):  
Sean Y. Kassim ◽  
Xiaoyun Fu ◽  
W. Conrad Liles ◽  
Steven D. Shapiro ◽  
William C. Parks ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Nadph Oxidase ◽  
The Matrix ◽  
Metalloproteinase Activity

scholarly journals In Vivo Optical Molecular Imaging of Matrix Metalloproteinase Activity following Celecoxib Therapy for Colorectal Cancer

2012 ◽  
Vol 11 (5) ◽  
pp. 7290.2012.00003 ◽  
Author(s):  
Rahul A. Sheth ◽  
Alexandra Kunin ◽  
Lars Stangenberg ◽  
Mark Sinnamon ◽  
Kenneth E. Hung ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Molecular Imaging ◽  
Matrix Metalloproteinase ◽  
Optical Molecular Imaging ◽  
Metalloproteinase Activity
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