MMPs and matrix proteases are critical effectors of cell responses. This function is ever more pertinent to dynamic states in which cells have to interact with their surrounding matrix to perform physiologic functions, or in disease states. Blood vessels undergo dynamic changes of their component cells to adapt to stresses or maladapt and cause disease. MMPs are intimately involved in these processes, but as apparent with the data presented herein, manipulation of MMP activity to modify the course of diseases may lead to adverse and unforeseen consequences.
Metalloproteases: Protein molecules (enzymes) that require the presence of metal ion bound to their sequence to maintain a proper structure that allows their functional activity. The main function of metalloproteases is to activate or to inactivate (inhibit) other proteins (substrates), usually by cutting off one or more of their fragments.
Multidomain structure: Domains are regions in a protein molecule that are determined by amino-acid sequence and that form defined, functionally distinct units. Thus, multidomain structure is specific for and characterizes a particular protein. If several proteins have similar multidomain structure, it means these proteins may also have similar functions.
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His interests are focused on pulmonary pathology and molecular mechanisms responsible for pulmonary diseases. His grants are supported by the NIH/NHLBI, AHA, and other foundations.
Dr. Iwona Fijalkowska is a Research Associate in Cardiopulmonary Pathology in the Department of Pathology, Johns Hopkins University School of Medicine. Her scientific interests cover protein chemistry and protein-protein interactions in angiogenesis and hemostasis.
Dr. Rubin M. Tuder, Professor of Pathology and Medicine, in the Department of Pathology, Johns Hopkins University School of Medicine.
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