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pubmed:abstractText |
The functions of heparan sulfate (HS) depend on the expression of structural domains that interact with protein partners. Glycosaminoglycans (GAGs) exhibit a high degree of polydispersity in their composition, chain length, sulfation, acetylation, and epimerization patterns. It is essential for the understanding of GAG biochemistry to produce detailed structural information as a function of spatial and temporal factors in biological systems. Toward this end, we developed a set of procedures to extract GAGs from various rat organ tissues and examined and compared HS expression levels using liquid chromatography/mass spectrometry. Here we demonstrate detailed variations in HS GAG chains as a function of organ location. These studies shed new light on the structural variation of GAG chains with respect to average length, disaccharide composition, and expression of low abundance structural epitopes, including unsubstituted amino groups and lyase-resistant oligosaccharides. The data show the presence of a disaccharide with an unsubstituted amino group that is endogenous and widely expressed in mammalian organ tissues.
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