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An artificial receptor for pro MMP ‐9 was created by fusing tissue inhibitor of  MMP ‐1 ( TIMP ‐1) with type  II  transmembrane mosaic serine protease ( MSP ‐T1). Expression of  MSP ‐T1 in 293T cells induced binding of pro MMP ‐9, which was processed by  MMP ‐2 activated by membrane type 1  MMP  ( MT 1‐ MMP ).  HT 1080 cells transfected with the   MSP ‐T1  gene produced activated  MMP ‐9 in collagen gel, and addition of pro MMP ‐2 to the culture augmented it, which resulted in intensive collagen digestion. These cells metastasized into chick embryonic liver more than control cells. Treatment of  HT 1080 cells with concanavalin A in the presence of exogenous pro MMP ‐2 induced activation of not only pro MMP ‐2 but also pro MMP ‐9. Knockdown of  MT 1‐ MMP  or  TIMP ‐2 expression with si RNA  suppressed activation of both pro MMP ‐2 and pro MMP ‐9. Transfection of  TIMP ‐1 si RNA  suppressed cell binding and activation of pro MMP ‐9, but not pro MMP ‐2 activation. Knockdown of a disintegrin and metalloproteinase 10 ( ADAM 10) expression reduced cell binding and processing of pro MMP ‐9. These results suggest that pro MMP ‐9, which binds to a receptor complex containing  TIMP ‐1 and  ADAM 10, is activated by the  MT 1‐ MMP / MMP ‐2 axis, and  MMP ‐9 thus activated stimulates cellular proteolysis and metastasis.

Activation of MMP ‐9 by membrane type‐1 MMP / MMP ‐2 axis stimulates tumor metastasis