• Login
    View Item 
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of ChristieCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsProfilesView

    My Account

    LoginRegister

    Local Links

    The Christie WebsiteChristie Library and Knowledge Service

    Statistics

    Display statistics

    Patterns of sulphation in heparan sulphate: polymorphism based on a common structural theme.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Gallagher, John T
    Turnbull, Jeremy E
    Lyon, Malcolm
    Affiliation
    CRC Department of Medical Oncology, Christie Hospital and Holt Radium Institute, Manchester, U.K.
    Issue Date
    1992-04
    
    Metadata
    Show full item record
    Abstract
    HS appears to be a well-organised molecule with a domain structure that is apparently unique amongst the GAG family (Gallagher, 1989). Further refinements in sequence analysis are needed to corroborate the simplified model proposed in Fig. 4. It is still not clear why evolution has favoured a structural motif of widely spaced sulphated domains. Presumably, some advantages must accrue to the organism from this design, and one idea, that we have discussed previously, is that the polysaccharide functions as a "template" for the organisation of structural proteins in the ECM and for the binding and presentation of growth factors within the matrix polymer network. The sulphated regions are likely to display considerable conformational versatility as a result of the presence of the iduronate residues, and this property may be very important for the protein-binding properties of the polysaccharides (Casu et al., 1988). Sulphation patterns within these regions could favour oligosaccharide conformations necessary for specific protein interactions. An important question in this context is why different cells express on their surfaces HS with subtle differences in sulphation pattern. Perhaps the polymorphic features of HS are involved in higher-order tissue- and organ-specific mechanisms controlling cellular recognition and morphogenesis. The consistency with which aberrant sulphation of HS is detected in malignant disease (Gallagher and Lyon, 1989) in which cellular recognition and differentiation are impaired, adds some substance to this view.
    Citation
    Patterns of sulphation in heparan sulphate: polymorphism based on a common structural theme. 1992, 24 (4):553-60 Int J Biochem
    Journal
    The International Journal of Biochemistry
    URI
    http://hdl.handle.net/10541/117650
    DOI
    10.1016/0020-711X(92)90326-V
    PubMed ID
    1516727
    Type
    Article
    Language
    en
    ISSN
    0020-711X
    ae974a485f413a2113503eed53cd6c53
    10.1016/0020-711X(92)90326-V
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

    entitlement

    Related articles

    • Selective impairment of the synthesis of basic fibroblast growth factor binding domains of heparan sulphate in a COS cell mutant defective in N-sulphotransferase.
    • Authors: Ishihara M, Guo Y, Swiedler SJ
    • Issue date: 1993 Feb
    • Sequence analysis of heparan sulphate indicates defined location of N-sulphated glucosamine and iduronate 2-sulphate residues proximal to the protein-linkage region.
    • Authors: Turnbull JE, Gallagher JT
    • Issue date: 1991 Jul 15
    • Multiprotein signalling complexes: regional assembly on heparan sulphate.
    • Authors: Gallagher JT
    • Issue date: 2006 Jun
    • Distribution of iduronate 2-sulphate residues in heparan sulphate. Evidence for an ordered polymeric structure.
    • Authors: Turnbull JE, Gallagher JT
    • Issue date: 1991 Feb 1
    • Structural differences and the presence of unsubstituted amino groups in heparan sulphates from different tissues and species.
    • Authors: Toida T, Yoshida H, Toyoda H, Koshiishi I, Imanari T, Hileman RE, Fromm JR, Linhardt RJ
    • Issue date: 1997 Mar 1
    DSpace software (copyright © 2002 - 2025)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.