scholarly journals Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues.

1994 ◽  
Vol 269 (12) ◽  
pp. 9352-9360 ◽  
Author(s):  
K.J. Leco ◽  
R. Khokha ◽  
N. Pavloff ◽  
S.P. Hawkes ◽  
D.R. Edwards
Keyword(s):  
Extracellular Matrix ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Distinctive Pattern ◽  
Tissue Inhibitor ◽  
Mouse Cells

scholarly journals Large inhibitor of metalloproteinases (LIMP) contains tissue inhibitor of metalloproteinases (TIMP)-2 bound to 72,000-Mr progelatinase

1992 ◽  
Vol 285 (1) ◽  
pp. 143-147 ◽  
Author(s):  
V A Curry ◽  
I M Clark ◽  
H Bigg ◽  
T E Cawston
Keyword(s):  
Extracellular Matrix ◽  
Connective Tissue ◽  
Inhibitory Activity ◽  
Culture Medium ◽  
Lung Fibroblasts ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Metalloproteinase Inhibitor ◽  
Cells In Culture ◽  
Foetal Lung

Connective-tissue cells in culture produce a family of metalloproteinases which, once activated, can degrade all the components of the extracellular matrix. These potent enzymes are all inhibited by the tissue inhibitor of metalloproteinases (TIMP), and it was thought that this inhibitor was solely responsible for the inhibition of these enzymes within connective tissue. However, other inhibitors have recently been described, including large inhibitor of metalloproteinases (LIMP) present in the culture medium of human foetal lung fibroblasts. Here we show that a large proportion of the inhibitory activity of LIMP consists of 72,000-M(r)-progelatinase bound to TIMP-2, a recently discovered low-M(r) metalloproteinase inhibitor closely related to TIMP. The physiological implications of the secretion of a complex of 72,000-M(r) progelatinase and TIMP-2 are discussed, and the separation of the complex in 6 M-urea is described.

scholarly journals Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene.

1996 ◽  
Vol 135 (6) ◽  
pp. 1669-1677 ◽  
Author(s):  
C M Alexander ◽  
E W Howard ◽  
M J Bissell ◽  
Z Werb
Keyword(s):  
Extracellular Matrix ◽  
Epithelial Cells ◽  
Transgenic Mice ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Alveolar Epithelial Cells ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Extracellular Matrix Molecule

We have used transgenic mice overexpressing the human tissue inhibitor of metalloproteinases (TIMP)-1 gene under the control of the ubiquitous beta-actin promoter/enhancer to evaluate matrix metalloproteinase (MMP) function in vivo in mammary gland growth and development. By crossing the TIMP-1 transgenic animals with mice expressing an autoactivating stromelysin-1 transgene targeted to mammary epithelial cells, we obtained a range of mice with genetically engineered proteolytic levels. The alveolar epithelial cells of mice expressing autoactivating stromelysin-1 underwent unscheduled apoptosis during late pregnancy. When stromelysin-1 transgenic mice were crossed with mice overexpressing TIMP-1, apoptosis was extinguished. Entactin (nidogen) was a specific target for stromelysin-1 in the extracellular matrix. The enhanced cleavage of basement membrane entactin to above-normal levels was directly related to the apoptosis of overlying mammary epithelial cells and paralleled the extracellular MMP activity. These results provide direct evidence for cleavage of an extracellular matrix molecule by an MMP in vivo.

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