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https://hdl.handle.net/2440/7444
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Type: | Journal article |
Title: | Highly sensitive sequencing of the sulfated domains of heparan sulfate |
Author: | Merry, C. Lyon, M. Deakin, J. Hopwood, J. Gallagher, J. |
Citation: | Journal of Biological Chemistry, 1999; 274(26):18455-18462 |
Publisher: | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
Issue Date: | 1999 |
ISSN: | 0021-9258 1083-351X |
Statement of Responsibility: | Catherine L. R. Merry, Malcolm Lyon, Jon A. Deakin, John J. Hopwood and John T. Gallagher |
Abstract: | The heparan sulfates (HS) are hypervariable linear polysaccharides that act as membrane co-receptors for growth factors, chemokines, and extracellular matrix proteins. In most instances, the molecular basis of protein recognition by HS is poorly understood. We have sequenced 75% of the sulfated domains (S-domains) of fibroblast HS, including all of the major ones. This analysis revealed tight coupling of N- and 2-O-sulfation and a low frequency but precise positioning of 6-O-sulfates, which are required functional groups for HS-mediated activation of the fibroblast growth factors. S-domain sequencing was conducted using a novel and highly sensitive method based on a new way of reading the sequence from high performance liquid chromatography separation profiles of metabolically labeled HS-saccharides following specific chemical and enzymatic scission. The implications of the patterns seen in the sulfated domains for better understanding of the synthesis and function of HS are discussed. |
Keywords: | 3T3 Cells Animals Mice Sulfates Heparitin Sulfate Chromatography, Gel Chromatography, High Pressure Liquid Carbohydrate Sequence Molecular Sequence Data |
DOI: | 10.1074/jbc.274.26.18455 |
Published version: | http://dx.doi.org/10.1074/jbc.274.26.18455 |
Appears in Collections: | Aurora harvest Paediatrics publications |
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