Proteomics

Dataset Information

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Oligosaccharide Substrate Preferences of Human Extracellular Sulfatase Sulf2


ABSTRACT: In this study, we characterized the substrate preferences of human HSulf2 using HS oligosaccharides with various lengths and sulfation degrees from several naturally occurring HS sources by applying liquid chromatography mass spectrometry based glycomics methods.

INSTRUMENT(S): 6520 Quadrupole Time-of-Flight LC/MS

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Small Intestine Mucosa

SUBMITTER: Yu Huang  

LAB HEAD: Joseph Zaia

PROVIDER: PXD001157 | Pride | 2014-07-22

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20110117_02.d.zip Other
20110117_03.d.zip Other
20110117_04.d.zip Other
20110118_02.d.zip Other
20110118_03.d.zip Other
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Publications

Oligosaccharide substrate preferences of human extracellular sulfatase Sulf2 using liquid chromatography-mass spectrometry based glycomics approaches.

Huang Yu Y   Mao Yang Y   Buczek-Thomas Jo Ann JA   Nugent Matthew A MA   Zaia Joseph J  

PloS one 20140815 8


Sulfs are extracellular endosulfatases that selectively remove the 6-O-sulfate groups from cell surface heparan sulfate (HS) chain. By altering the sulfation at these particular sites, Sulfs function to remodel HS chains. As a result of the remodeling activity, HSulf2 regulates a multitude of cell-signaling events that depend on interactions between proteins and HS. Previous efforts to characterize the substrate specificity of human Sulfs (HSulfs) focused on the analysis of HS disaccharides and  ...[more]

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