Abstract
The cell surface heparan sulfate proteoglycan syndecan-2 regulates the activation of matrix metalloproteinase-7 (MMP-7) as a docking receptor. Here, we demonstrate the role of MMP-7 on syndecan-2 shedding in colon cancer cells. Western blot analysis showed that shed syndecan-2 was found in the culture media from various colon cancer cells. Overexpression of MMP-7 enhanced syndecan-2 shedding, whereas the opposite was true when MMP-7 levels were knocked-down using small inhibitory RNAs. Consistently, HT29 cells treated with MMP-7, but neither MMP-2 nor MMP-9, showed increased shed syndecan-2 in a time- and concentration-dependent manner. Furthermore, MALDI-TOF MS analysis and N-terminal amino acid sequencing revealed that MMP-7 cleaved both recombinant syndecan-2 and an endogenously glycosylated syndecan-2 ectodomain in the N-terminus at Leu 149 residue in vitro. Taken together, the data suggest that MMP-7 directly mediates shedding of syndecan-2 from colon cancer cells.
Original language | English |
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Pages (from-to) | 1260-1264 |
Number of pages | 5 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 417 |
Issue number | 4 |
DOIs | |
State | Published - 27 Jan 2012 |
Bibliographical note
Funding Information:This study was supported by a Grant of the Korea Healthcare technology R&D Projects, Ministry for Health, Welfare, and Family Affairs, Republic of Korea (A090615 to ESO) and the National Research Foundation of Korea (NRF) Grant funded by the Korea Government (MEST) (No. 2010-0026103).
Keywords
- Colon cancer
- Matrix metalloproteinase-7
- Shedding
- Syndecan-2