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    The molecular phenotype of heparan sulfate in the Hs2st-/- mutant mouse.

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    Authors
    Merry, Catherine L R
    Bullock, Simon L
    Swan, Daniel C
    Backen, Alison C
    Lyon, Malcolm
    Beddington, Rosa S
    Wilson, Valerie A
    Gallagher, John T
    Affiliation
    Cancer Research Campaign Department of Medical Oncology, Christie Hospital NHS Trust, Manchester M20 4BX, United Kingdom. cmerry@picr.man.ac.uk
    Issue Date
    2001-09-21
    
    Metadata
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    Abstract
    Heparan sulfate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. We previously described the phenotype of mice with a gene-trap mutation in Hs2st, encoding the key HS 2-O-sulfotransferase enzyme in HS polymer modification. In contrast to the early developmental failure of embryos lacking HS, the onset of abnormalities in the Hs2st(-/-) mice occurs only after midgestation, the most dramatic being the complete failure of kidney development. Uronate 2-O-sulfates were not detected in the mutant HS, indicating a complete loss of function of Hs2st. However, the domain structure of the mutant HS is conserved, and compensatory increases in N- and 6-O-sulfation maintain the overall charge density. The apparent affinities of the mutant HS for hepatocyte growth factor/scatter factor and fibronectin were unchanged but were reduced for fibroblast growth factor-1 and -2. Surprisingly, the Hs2st(-/-) cells were able to mount an apparently normal signaling response to fibroblast growth factor-1 and -2 as well as to hepatocyte growth factor/scatter factor.
    Citation
    The molecular phenotype of heparan sulfate in the Hs2st-/- mutant mouse. 2001, 276 (38):35429-34 J. Biol. Chem.
    Journal
    The Journal of Biological Chemistry
    URI
    http://hdl.handle.net/10541/85732
    DOI
    10.1074/jbc.M100379200
    PubMed ID
    11457822
    Type
    Article
    Language
    en
    ISSN
    0021-9258
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M100379200
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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