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• W2130094155 abstract "During vascular development, endothelial platelet-derived growth factor B (PDGF-B) is critical for pericyte recruitment. Deletion of the conserved C-terminal heparin-binding motif impairs PDGF-BB retention and pericyte recruitment in vivo, suggesting a potential role for heparan sulfate (HS) in PDGF-BB function during vascular development. We studied the participation of HS chains in pericyte recruitment using two mouse models with altered HS biosynthesis. Reduction of N -sulfation due to deficiency in N -deacetylase/ N -sulfotransferase-1 attenuated PDGF-BB binding in vitro, and led to pericyte detachment and delayed pericyte migration in vivo. Reduced N -sulfation also impaired PDGF-BB signaling and directed cell migration, but not proliferation. In contrast, HS from glucuronyl C5-epimerase mutants, which is extensively N- and 6- O- sulfated, but lacks 2- O -sulfated L-iduronic acid residues, retained PDGF-BB in vitro, and pericyte recruitment in vivo was only transiently delayed. These observations were supported by in vitro characterization of the structural features in HS important for PDGF-BB binding. We conclude that pericyte recruitment requires HS with sufficiently extended and appropriately spaced N -sulfated domains to retain PDGF-BB and activate PDGF receptor β (PDGFRβ) signaling, whereas the detailed sequence of monosaccharide and sulfate residues does not appear to be important for this interaction." @default.
• W2130094155 created "2016-06-24" @default.
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• W2130094155 date "2007-02-01" @default.
• W2130094155 modified "2023-10-18" @default.
• W2130094155 title "Defective <i>N</i>-sulfation of heparan sulfate proteoglycans limits PDGF-BB binding and pericyte recruitment in vascular development" @default.
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• W2130094155 doi "https://doi.org/10.1101/gad.398207" @default.
• W2130094155 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1785125" @default.
• W2130094155 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17289920" @default.
• W2130094155 hasPublicationYear "2007" @default.
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