Pancreatic cancer incurs the worst survival rate of the major cancers. High levels of the protease matrix metalloproteinase-7 (MMP-7) in circulation correlate with poor prognosis and limited survival of patients. MMP-7 is required for a key path of pancreatic tumorigenesis in mice and is present throughout tumor progression. Enhancements to chemotherapies are needed for increasing the number of pancreatic tumors that can be removed and for preventing relapses after surgery. With these ends in mind, selective inhibition of MMP-7 may be worth investigation. An anti-MMP-7 monoclonal antibody was recently shown to increase the susceptibility of several pancreatic cancer cell lines to chemotherapeutics, increase their apoptosis, and decrease their migration. MMP-7 activities are most apparent at the surfaces of innate immune, epithelial, and tumor cells. Proteolytic shedding of multiple protein ectodomains by MMP-7 from such cell surfaces influence apoptosis, proliferation, migration, and invasion. These activities warrant targeting of MMP-7 selectively in pancreatic cancer and other tumors of mucosal epithelia. Competitive and non-competitive modes of MMP-7 inhibition are discussed.
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Review Article| March 28 2022
MMP-7 marks severe pancreatic cancer and alters tumor cell signaling by proteolytic release of ectodomains
Steven R. Van Doren
1Department of Biochemistry, University of Missouri, Columbia, MO 65211, U.S.A.
2Institute for Data Science and Informatics, University of Missouri, Columbia, MO 65211, U.S.A.
Correspondence: Steven R. Van Doren (firstname.lastname@example.org)
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Publisher: Portland Press Ltd
Received: January 31 2022
Revision Received: March 10 2022
Accepted: March 14 2022
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2022 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
Steven R. Van Doren; MMP-7 marks severe pancreatic cancer and alters tumor cell signaling by proteolytic release of ectodomains. Biochem Soc Trans 29 April 2022; 50 (2): 839–851. doi: https://doi.org/10.1042/BST20210640
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