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The Membrane-Type Matrix Metalloproteinases (MT1-MMP and MT2-MMP) of the umbilical cord
| Content Provider | Semantic Scholar |
|---|---|
| Author | Galewska, Zofia Romanowicz, Lech |
| Copyright Year | 2011 |
| Abstract | Background: Turnover of matrix proteins including collagen and proteoglycans depends on their the novo synthesis and cleavage. The latter is performed by huge number of enzymes. Among them metalloproteinases (MMPs) play an important role not only in initialization of that process but also in enzyme activation. Methods: We used Western Immunoblot method and immunoenzymatic assay (ELISA) for detection of membrane-type metalloproteinases (MT-MMPs). Results: The umbilical cord arteries, vein and Wharton’s jelly of control and preeclamptic newborns contained MT1-MMP (MMP-14) and MT2-MMP (MMP-15). Both enzymes existed in a form of high molecular complexes. Furthermore, a distinct increase in the amount of MT1-MMP in preeclamptic umbilical cord vessel walls and significant decrease in preeclamptic Wharton’s jelly was found. All preeclamptic tissues contained twice higher amount of MMP-15 in comparison to controls. Conclusions: Free latent form of both investigated MT-MMPs was not detected in all investigated tissue extracts. Indicated molecular weight of about 54 kDa corresponded to free active form of respective MMP. High molecular weight complexes detected in all umbilical cord tissues contained these metalloproteinases bound to tissue inhibitors of matrix metalloproteinases and/or other extracellular components. Both MT-MMPs can activate gelatinases, which may be one of the mechanisms of extracellular matrix remodelling in the umbilical cord of preeclamptic newborns. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.ptmp.com.pl/archives/apm/17-3/APM173-6-Galewska.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |