Lysosomal degradation of heparin and heparan sulfate

Peter J. Meikle, Maria Fuller, John J. Hopwood

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Citations (Scopus)

Abstract

Heparin (HP) and heparan sulfate (HS) proteoglycans are composed of linear-sulfated glycosaminoglycan (GAG) chains of up to several hundred, alternating uronic acid and N-acetylglucosamine residues that are modified through a series of reactions to produce a complex pattern of O- and N-sulfated monosaccharide as well as epimerized uronic acid residues. The uptake pathway of HP from its site of action has not been defined. HS proteoglycans, destined for turnover, traffic through the endocytic vacuolar network to the lysosome for degradation. HS proteoglycans are routed from the cell surface via clathrin-coated vesicles that fuse with early endosomes. The degradation of HP and HS begins with endo-hydrolysis to clip the long chain polysaccharides or GAG chains to shorter oligosaccharide fragments with the action of endo-glycosidases called heparanases. The lysosomal exo-enzymes are synthesized and processed in the endoplasmic reticulum as well as the Golgi apparatus. A signal sequence is required to direct mRNA and the ribosome complex to the rough endoplasmic reticulum for the commencement of protein synthesis. © 2005

Original languageEnglish
Title of host publicationChemistry and Biology of Heparin and Heparan Sulfate
PublisherElsevier
Pages285-311
Number of pages27
ISBN (Print)9780080448596
DOIs
Publication statusPublished - 1 Dec 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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