کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1930237 | 1050493 | 2012 | 5 صفحه PDF | دانلود رایگان |

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 Leu149 residue in vitro. Taken together, the data suggest that MMP-7 directly mediates shedding of syndecan-2 from colon cancer cells.
► Overexpression of MMP-7 enhances syndecan-2 shedding.
► MMP-7 enhances the shedding of syndecan-2 from human colon cancer cells.
► MMP-7 cleaved syndecan-2 ectodomain in the N-terminus at Leu149 residue in vitro.
► MMP-7 directly mediates shedding of syndecan-2 from colon cancer cells.
Journal: Biochemical and Biophysical Research Communications - Volume 417, Issue 4, 27 January 2012, Pages 1260–1264