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Bone Sialoprotein Does Not Interact With Pro-Gelatinase A (MMP-2) or Mediate MMP-2 Activation

Bone Sialoprotein Does Not Interact With Pro-Gelatinase A (MMP-2) or Mediate MMP-2 Activation

Queena Hwang, Sela Cheifetz, Christopher M Overall, Christopher A McCulloch, Jaro Sodek

BMC Cancer. 2009 Apr 22;9:121.

PMID: 19386107

Abstract:

Background:
A recent model for activation of the zymogen form of matrix metalloproteinase 2 (MMP-2, also known as gelatinase A) has suggested that interactions between the SIBLING protein bone sialoprotein (BSP) and MMP-2 leads to conformational change in MMP-2 that initiates the conversion of the pro-enzyme into a catalytically active form. This model is particularly relevant to cancer cell metastasis to bone since BSP, bound to the alphavbeta3 integrin through its arginine-glycine-aspartic acid motif, could recruit MMP-2 to the cell surface.
Methods:
We critically assessed the relationship between BSP and proMMP-2 and its activation using various forms of recombinant and purified BSP and MMP-2. Gelatinase and collagenase assays, fluorescence binding assays, real-time PCR, cell culture and pull-down assays were employed to test the model.
Results:
Studies with a fluorogenic substrate for MMP-2 showed no activation of proMMP-2 by BSP. Binding and pull-down assays demonstrated no interaction between MMP-2 and BSP. While BSP-mediated invasiveness has been shown to depend on its integrin-binding RGD sequence, analysis of proMMP-2 activation and the level of membrane type 1 (MT1)-MMP in cells grown on a BSP substratum showed that the BSP-alphavbeta3 integrin interaction does not induce the expression of MT1-MMP.
Conclusion:
These studies do not support a role for BSP in promoting metastasis through interactions with pro-MMP-2.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416003	MMP-2 Substrate, Fluorogenic			Price

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