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• W2023374250 endingPage "2401" @default.
• W2023374250 startingPage "2387" @default.
• W2023374250 abstract "Membrane type-1 matrix metalloproteinase (MT1-MMP) is the prototypical member of a subgroup of membrane-anchored proteinases that belong to the matrix metalloproteinase family. Although synthesized as a zymogen, MT1-MMP plays an essential role in extracellular matrix remodeling after an undefined process that unmasks its catalytic domain. We now report the existence of a proprotein convertase-MT1-MMP axis that regulates the processing and functional activity of the metalloproteinase. Two sets of basic motifs in the propeptide region of MT1-MMP are identified that potentially can be recognized by the proprotein convertase family of subtilisin-like proteases. Processing of proMT1-MMP as well as the expression of its proteolytic activity were blocked by mutating these recognition motifs or by inhibiting the proprotein convertases furin and PC6 with the serpin-based inhibitor alpha(1) antitrypsin Portland. Furthermore, both furin-dependent and furin-independent MT1-MMP processing pathways are identified that require tethering of the metalloproteinase to the cell surface. These findings demonstrate the existence of a proprotein convertase-MT1-MMP axis that can regulate extracellular matrix remodeling." @default.
• W2023374250 created "2016-06-24" @default.
• W2023374250 creator A5080476399 @default.
• W2023374250 creator A5091286795 @default.
• W2023374250 date "2000-07-01" @default.
• W2023374250 modified "2023-10-12" @default.
• W2023374250 title "Regulation of Membrane Type-1 Matrix Metalloproteinase Activation by Proprotein Convertases" @default.
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• W2023374250 doi "https://doi.org/10.1091/mbc.11.7.2387" @default.
• W2023374250 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/14927" @default.
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