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Lysosomal Degradation of Heparin and Heparan Sulphate

  • Craig Freeman
  • John Hopwood
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 313)

Abstract

This review is a limited update of a previous review of enzymes that degrade heparan sulphate (HS) and heparin (Hopwood, 1989). Newly-synthesised HS proteoglycan (HSPG) is internalised from the cell surface and catabolised with a half-time of 4 to 6 h in rat ovarian granulosa cells (Yanagishita and Hascall, 1984), and by more than 28 h in human colon carcinoma cells (Iozzo, 1987). Studies of both cell types have shown the existence of preliminary protease and an initial endoglycosidase activity in non-lysosomal (chloroquine-insensitive compartments) to generate HS intermediates of Mr 10 kDa, and further chloroquine-sensitive endoglycosidic activity to produce HS fragments of Mr 5 kDa which are rapidly degraded in the lysosome by a series of exohydrolases to monosaccharides and sulphate without the generation of intermediates. A number of distinct lysosomal membrane transporters are involved in the efflux of the monomeric products GlcNAc, GlcA and IdoA and sulphate ions from the lysosome (Jonas et al., 1989; Jonas and Jobe, 1990a, 1990b; Mancini et al., 1989) which can be reutilised in biosynthetic pathways (Rome and Hill, 1986).

Keywords

Heparan Sulphate Carboxy Group Lysosomal Membrane Human Skin Fibroblast Sulphate Ester 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Craig Freeman
    • 1
  • John Hopwood
    • 1
  1. 1.Lysosomal Diseases Research Unit, Department of Chemical PathologyAdelaide Children’s HospitalNorth AdelaideAustralia

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