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- W1985605704 abstract "Bone sialoprotein (BSP) has been shown to induce limited gelatinase activity in latent matrix metalloproteinase-2 (MMP-2) without removal of the propeptide and to restore enzymatic activity to MMP-2 previously inhibited by tissue inhibitor of matrix metalloproteinase-2 (TIMP2). The current study identifies structural domains in human BSP and MMP-2 that contribute to these interactions. The 26 amino acid domain encoded by exon 4 of BSP is shown by a series of binding and activity assays to be involved in the displacement of MMP-2’s propeptide from the active site and thereby inducing the protease activity. Binding assays in conjunction with enzyme activity assays demonstrate that both amino- and carboxy-terminal domains of BSP contribute to restoration of activity to TIMP2-inhibited MMP-2, while the MMP-2 hemopexin domain is not required for reactivation." @default.
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- W1985605704 date "2008-08-26" @default.
- W1985605704 modified "2023-10-10" @default.
- W1985605704 title "Structural Requirements for Bone Sialoprotein Binding and Modulation of Matrix Metalloproteinase-2" @default.
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- W1985605704 doi "https://doi.org/10.1021/bi801068p" @default.
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