Membrane-type 1 matrix metalloproteinase (MT1-MMP) is an integral membrane proteinase that performs processing of cell surface proteins and degradation of extracellular matrix (ECM) components. Through these proteolytic events, MT1-MMP regulates various cellular functions, including ECM turnover, promotion of cell migration and invasion, and morphogenic responses to extracellular stimuli. MT1-MMP has to be regulated strictly to accomplish its function appropriately at various steps, including at the transcriptional and post-translational levels. MT1-MMP was originally identified as an invasion-promoting enzyme expressed in malignant tumour cells, and also as a specific activator of proMMP-2, which is believed to play a role in invasion of the basement membrane. Since then, it has attracted attention as a membrane-associated MMP that promotes cancer cell invasion and angiogenesis by endothelial cells. Although MT1-MMP has now become one of the best characterized enzymes in the MMP family, there remain numerous unanswered questions. In this chapter, we summarize our recent findings on how MT1-MMP is regulated during cell migration, and how cell migration is regulated by MT1-MMP.
Membrane-type 1 matrix metalloproteinase and cell migration
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Jeremy Saklatvala, Hideaki Nagase, Guy Salvesen, Motoharu Seiki, Hidetoshi Mori, Masahiro Kajita, Takamasa Uekita, Yoshifumi Itoh; Membrane-type 1 matrix metalloproteinase and cell migration. Biochem Soc Symp 1 September 2003; 70 253–262. doi: https://doi.org/10.1042/bss0700253
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