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- W2011094518 abstract "Glycosaminoglycan (GAG) sugars are largely responsible for the bioactivity of the proteoglycan proteins they decorate, and are particularly important for mediating the processes of cell attachment and growth factor signaling. Here, we show that chlorate-induced de-sulfation of GAGs expressed by MG-63 osteosarcoma cells results in delayed cell proliferation when the cells are exposed to chlorate for short or medium periods, but a disrupted mineralization without altered cell proliferation in response to long-term chlorate exposure. Analysis of GAG-binding growth factor activity indicated that chlorate disrupted BMP2/noggin signaling, but not FGF2 activity. Microarray analyses, which were confirmed by subsequent cell-based assays, indicated that chlorate predominantly disrupted the cell cycle and actin cytoskeleton and upregulated cholesterol synthesis, without affecting cell migration or attachment. Furthermore, we observed that disruption of the functions of the proteoglycan syndecan-4 replicated phenotypes induced by chlorate, implicating a primary role for this proteoglycan in providing bioactivity for these cells. J. Cell. Physiol. 219: 572–583, 2009. © 2009 Wiley-Liss, Inc." @default.
- W2011094518 created "2016-06-24" @default.
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- W2011094518 creator A5056730499 @default.
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- W2011094518 date "2009-06-01" @default.
- W2011094518 modified "2023-10-17" @default.
- W2011094518 title "De-sulfation of MG-63 cell glycosaminoglycans delays in vitro osteogenesis, up-regulates cholesterol synthesis and disrupts cell cycle and the actin cytoskeleton" @default.
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- W2011094518 doi "https://doi.org/10.1002/jcp.21700" @default.
- W2011094518 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19142873" @default.
- W2011094518 hasPublicationYear "2009" @default.
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