Tissue Inhibitor of Metalloproteinases-2 (TIMP-2) Suppresses TKR-Growth Factor Signaling Independent of Metalloproteinase Inhibition
TLDR
These studies represent a new functional paradigm for TIMP-2 in which TIMP suppresses EGF-mediated mitogenic signaling by short-circuiting EGFR activation.About:
This article is published in Journal of Biological Chemistry.The article was published on 2001-02-02 and is currently open access. It has received 127 citations till now. The article focuses on the topics: Epidermal growth factor & Growth factor receptor.read more
Citations
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How Matrix Metalloproteinases Regulate Cell Behavior
Mark D. Sternlicht,Zena Werb +1 more
TL;DR: Recent advances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localization, and clearance are controlled.
Journal ArticleDOI
The microenvironment of the tumour-host interface
Lance A. Liotta,Elise C. Kohn +1 more
TL;DR: A new class of cancer therapies that targets this pathological communication interface between tumour cells and host cells is currently under development.
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The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity
Keith Brew,Hideaki Nagase +1 more
TL;DR: Tissue inhibitors of metalloproteinases (TIMPs) are widely distributed in the animal kingdom and the human genome contains four paralogous genes encoding TIMPs 1 to 4, and their range of activities has now been found to be broader as it includes the inhibition of several of the disintegrin-metallop proteinases, ADAMs and ADAMTSs.
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A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2.
Jian Hua Qi,Quteba Ebrahem,Nina Z. Moore,Gillian Murphy,Lena Claesson-Welsh,Mark Bond,Andrew Baker,Bela Anand-Apte +7 more
TL;DR: The ability of TIMP3 to inhibit vascular endothelial factor (VEGF)–mediated angiogenesis is demonstrated and the potential mechanism by which this occurs is identified, indicating a new function for this molecule.
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The Matrix Metalloproteinase System: Changes, Regulation, and Impact throughout the Ovarian and Uterine Reproductive Cycle
Thomas E. Curry,Kevin G. Osteen +1 more
TL;DR: The current review will highlight the key features of the MMPs and tissue inhibitors of metalloproteinases, focus on the changes and regulation of theMMP system that take place throughout the estrous and menstrual cycles, and address the impact of the dynamic tissue remodeling processes on ovarian and uterine physiology.
References
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The hallmarks of cancer.
TL;DR: This work has been supported by the Department of the Army and the National Institutes of Health, and the author acknowledges the support and encouragement of the National Cancer Institute.
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Cell Adhesion: The Molecular Basis of Tissue Architecture and Morphogenesis
TL;DR: A coupling between physical adhesion and developmental signaling provides a mechanism to tightly integrate physical aspects of tissue morphogenesis with cell growth and differentiation, a coordination that is essential to achieve the intricate patterns of cells in tissues.
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MMP-9/Gelatinase B Is a Key Regulator of Growth Plate Angiogenesis and Apoptosis of Hypertrophic Chondrocytes
Thiennu H. Vu,J. Michael Shipley,Gabriele Bergers,Joel E. Berger,Jill A. Helms,Douglas Hanahan,Steven D. Shapiro,Robert M. Senior,Zena Werb +8 more
TL;DR: Transplantation of wild-type bone marrow cells rescues vascularization and ossification in gelatinase B-null growth plates, indicating that these processes are mediated by gelatinaseB-expressing cells of bone marrow origin, designated chondroclasts.
PatentDOI
EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
TL;DR: In this article, agents and methods for growth factor receptor activation by modulating the G-protein mediated signal transduction pathway were described, and a method to activate the growth factor receptors was proposed.
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Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells.
Takashi Chijiwa,Atsushi Mishima,Masatoshi Hagiwara,Mamoru Sano,Kyozo Hayashi,Tsutomu Inoue,Naito Kenji,Tadashi Toshioka,Hiroyoshi Hidaka +8 more
TL;DR: In this article, a newly synthesized isoquinolinesulfonamide, H-89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinoline-sulfoneamide), was shown to have a potent and selective inhibitory action against cyclic AMP-dependent protein kinase (protein kinase A), with an inhibition constant of 0.048 +/- 0.008 microM.