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Synthesis of Fluorophore-Tagged Xylosides That Prime Glycosaminoglycan Chains
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Abstract
Biosynthesis and functions of glycosaminoglycan (GAG) chains are complex and remain elusive. To better understand the factors that regulate the biosynthesis and functions, fluorophore-tagged xylosides carrying two different linkages between fluorophore and xylose residue were synthesized and evaluated for their ability to prime GAG chains such as heparan sulfate (HS), chondroitin sulfate (CS), and dermatan sulfate (DS) in various cell lines. These in vitro studies resulted in the identification of fluorophore-tagged xylosides that prime high molecular weight GAG chains. Primed GAG chains carrying a fluorophore group has several advantages for studying the factors that regulate the biosynthesis, analyzing intact fine structures at low detection limits, and setting the stage for studying structure–function relations of GAG chains of cellular origin.
Title: Synthesis of Fluorophore-Tagged Xylosides That Prime
Glycosaminoglycan Chains
Description:
Abstract
Biosynthesis and functions of glycosaminoglycan (GAG) chains are complex and remain elusive.
To better understand the factors that regulate the biosynthesis and functions, fluorophore-tagged xylosides carrying two different linkages between fluorophore and xylose residue were synthesized and evaluated for their ability to prime GAG chains such as heparan sulfate (HS), chondroitin sulfate (CS), and dermatan sulfate (DS) in various cell lines.
These in vitro studies resulted in the identification of fluorophore-tagged xylosides that prime high molecular weight GAG chains.
Primed GAG chains carrying a fluorophore group has several advantages for studying the factors that regulate the biosynthesis, analyzing intact fine structures at low detection limits, and setting the stage for studying structure–function relations of GAG chains of cellular origin.
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