QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

Help viewing high resolution images Return to article

Fig. 1. Partitioning of MMP9 chimeras into distinct membrane domains. (A) Schematic representation of the MMP9-GPI and the MMP9-LDL chimeras. (B) Gelatinolytic activity in membrane (M) and cytosolic (C) fractions isolated from MMP9-GPI-, MMP9-LDL-, MMP9-wt and mock-transfected MCF-7 cells. ProMMP9 (solid arrowhead) and MMP9 (open arrowhead) activity in HT-1080 conditioned medium (H). (C) Gelatinolytic activity in conditioned medium from the same cells as in B after 24 hours of serum depletion. (D) MCF-7 cells expressing all MMP9 forms were fractionated in flotation gradients and analyzed by zymography. Fractions 1 and 6 represent the top and the bottom of the gradient, respectively. The same fractions were analyzed by western blot with anti-TfR and anti-VIP21 (CAV-1) as controls for non-raft- and raft-associated proteins, respectively. (E) Confocal microscopy of MMP9-expressing cells stained with cholera toxin ß-subunit (green) and anti-MMP9 antibody (red); yellow staining indicates colocalization of the molecules. The two-color overlays show representative cells for (a) MMP9-GPI, (b) MMP9-LDL and (c) MMP9-wt (n=50). The boxed regions in these images are enlarged in d, e and f, respectively. Scale bar, 10 µm. Single-color images are available: Fig. S1, http://jcs.biologists.org/supplemental/

Return to article