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Vol. 11, Issue 7, 2387-2401, July 2000
Department of Internal Medicine and the University of Michigan
Comprehensive Cancer Center, University of Michigan, Ann Arbor,
Michigan 48109
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
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.
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