Heparan sulfate (HS) shows enormous structural heterogeneity generated by the combined modification of epimerization, N-sulfation, and O-sulfation in the polysaccharide chain. A novel family of extracellular sulfatases (SulfFP1/sulf-1 and SulfFP2/sulf-2) identified in quail, rats, humans, and mice (Dhoot et al. 2001; Morimoto-Tomita 2002; Ohto et al. 2002) act as endosulfatases, which remove 6-O sulfate from N-acetylglucosamine residues in intact heparin/HS. Previous studies have revealed that these endosulfatases modulated the signaling of many heparin-binding factors, suggesting that they play a role in the regulation of cellular signaling in vivo. Here, we describe a method to measure the endosulfatase activity.
KeywordsConditioned Medium Heparan Sulfate Choroid Plexus Hydrogen Sulfate Disaccharide Unit
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