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    Highly sensitive sequencing of the sulfated domains of heparan sulfate.

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    Authors
    Merry, Catherine L R
    Lyon, Malcolm
    Deakin, Jon A
    Hopwood, John J
    Gallagher, John T
    Affiliation
    Cancer Research Campaign and University of Manchester Department of Medical Oncology, Christie Hospital NHS Trust, Manchester, M20 4BX, United Kingdom.
    Issue Date
    1999-06-25
    
    Metadata
    Show full item record
    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.
    Citation
    Highly sensitive sequencing of the sulfated domains of heparan sulfate. 1999, 274 (26):18455-62 J. Biol. Chem.
    Journal
    Journal of Biological Chemistry
    URI
    http://hdl.handle.net/10541/90785
    DOI
    10.1074/jbc.274.26.18455
    PubMed ID
    10373453
    Type
    Article
    Language
    en
    ISSN
    0021-9258
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.274.26.18455
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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