Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Kevin J. Leco"'
Publikováno v:
Development, Growth & Differentiation. 51:17-24
Tissue inhibitors of metalloproteinases (TIMPs) regulate extracellular matrix (ECM) degradation by matrix metalloproteinases (MMPs) throughout lung development. We examined lungs from TIMP3 null mice and found significant air space enlargement compar
Publikováno v:
American Journal of Physiology-Lung Cellular and Molecular Physiology. 293:L779-L789
Mice deficient in tissue inhibitor of metalloproteinase-3 (TIMP-3) develop an emphysema-like phenotype involving increased pulmonary compliance, tissue degradation, and matrix metalloproteinase (MMP) activity. After a septic insult, they develop a fu
Publikováno v:
Cardiovascular Research. 75:359-368
Objective We have recently demonstrated that endothelial nitric oxide synthase (eNOS) promotes cardiomyocyte proliferation. However, mechanisms by which eNOS regulates cardiomyocyte proliferation are not fully understood. The goal of the present stud
Autor:
Lynda McCaig, Erica L. Martin, Ruud A. W. Veldhuizen, James F. Lewis, Timothy C. Bailey, Emily A. Truscott, Kevin J. Leco
Publikováno v:
Experimental Lung Research. 33:99-113
Tissue inhibitor of metalloproteinase-3 (TIMP3) null mice develop emphysema-like airspace enlargement due to an enzymatic imbalance. This study investigates how these abnormalities alter lung mechanics and the response to 2 different mechanical venti
Publikováno v:
Developmental Biology. 298:540-554
Tissue inhibitors of metalloproteinases (TIMPs) regulate extracellular matrix (ECM) degradation by matrix metalloproteinases (MMPs) throughout embryogenesis. We examined lungs from TIMP3 null mice and found decreased bronchiole branching, enhanced ac
Autor:
Brent Z. Moyer, Ruud A. W. Veldhuizen, Kevin J. Leco, Erica L. Martin, Lynda McCaig, James F. Lewis, M. Cynthia Pape
Publikováno v:
American Journal of Physiology-Lung Cellular and Molecular Physiology. 289:L244-L251
An imbalance in matrix metalloproteinases (MMPs) and the tissue inhibitors of metalloproteinases (TIMPs) leads to excessive or insufficient tissue breakdown, which is associated with many disease processes. The TIMP-3 null mouse is a model of MMP/TIM
Autor:
M. Cynthia Pape, Brent Z. Moyer, Barry Starcher, Kevin J. Leco, Erica L. Martin, Ruud A. W. Veldhuizen
Publikováno v:
American Journal of Physiology-Lung Cellular and Molecular Physiology. 285:L1222-L1232
Matrix metalloproteinases (MMPs) are degradative enzymes, which act to remodel tissue. Their activity is regulated by the tissue inhibitors of metalloproteinases (TIMPs). An imbalance in the degradation/inhibition activities has been associated with
Publikováno v:
Obstetrics & Gynaecology Publications
Tissue inhibitors of metalloproteinases (TIMPs) regulate extracellular matrix (ECM) degradation by matrix metalloproteinases (MMPs). We have examined the role of TIMP-3 on ECM homeostasis and bronchiole branching morphogenesis during murine embryogen
Autor:
Caroline J. Lundy, Dylan R. Edwards, Robert K. Nuttall, Blaine W. Phillips, Ian M. Clark, Gilbert A. Schultz, Aileen Hogan, Kevin J. Leco, David Young
Publikováno v:
Biochemical Journal. 364:89-99
We have used real-time quantitative reverse transcriptase PCR (TaqMan®) to quantify the expression of the four tissue inhibitor of metalloproteinases (Timp) genes in mouse tissues during development and in the adult. Among the four Timp genes, Timp-
Autor:
Kevin J. Leco, Suneel S. Apte, Gary T. Taniguchi, Gilbert A. Schultz, Rama Khokha, Dylan R. Edwards, Susan P. Hawkes
Publikováno v:
FEBS Letters. 401:213-217
We have isolated cDNA clones corresponding to a new member of the murine tissue inhibitor of metalloproteinase (TIMP) family, designated Timp-4. The nucleotide sequence predicts a protein of 22,609 Da that contains the characteristic 12 cysteine TIMP