Skip to content

Research at St Andrews

The enzymatic degradation of heparan sulfate

Research output: Contribution to journalReview articlepeer-review

Author(s)

Laura Susan Griffin, Tracey Maureen Gloster

School/Research organisations

Abstract

Glycosaminoglycans (GAGs) such as heparan sulfate (HS) interact with a number of factors in the extracellular matrix (ECM) and as a consequence play a key role in the metabolic processes occurring within the cell. The dynamic synthesis and degradation of HS (and all GAGs) are necessary for ensuring that optimal chains are present for these functions. The degradation of HS begins at the cell surface and finishes in the lysosome, after which components can be recycled. Deficiencies or mutations in the lysosomal enzymes that process GAGs result in rare Mucopolysaccharidoses disorders (MPSs). There are few treatments available for these genetically inherited diseases and those that are available often do not treat the neurological symptoms of the disease. In this review, we discuss the enzymes involved in the degradation of HS and their related diseases, with emphasis on those located in the lysosome.
Close

Details

Original languageEnglish
Pages (from-to)710-722
JournalProtein & Peptide Letters
Volume24
Issue number8
DOIs
Publication statusPublished - 1 Aug 2017

    Research areas

  • Glycosaminoglycan, Heparan sulfate, Degradation, Lysosome, Mucopolysaccharidoses, Enzymes

Discover related content
Find related publications, people, projects and more using interactive charts.

View graph of relations

Related by author

  1. Dissecting the mechanism of (R)-3-hydroxybutyrate dehydrogenase by kinetic isotope effects, protein crystallography, and computational chemistry

    G. Machado, T. F., Purg, M., McMahon, S., Read, B., Oehler, V., Åqvist, J., Gloster, T. & da Silva, R. G., 18 Dec 2020, In: ACS Catalysis. 10, 24, p. 15019–15032

    Research output: Contribution to journalArticlepeer-review

  2. Analysis of the product streams obtained on butanosolv pretreatment of draff

    Foltanyi, F., Hawkins, J. E., Panovic, I., Bird, E. J., Gloster, T., Lancefield, C. S. & Westwood, N. J., Oct 2020, In: Biomass and Bioenergy. 141, 105680.

    Research output: Contribution to journalArticlepeer-review

  3. Tetramerisation of the CRISPR ring nuclease Crn3/Csx3 facilitates cyclic oligoadenylate cleavage

    Athukoralage, J. S., McQuarrie, S. J., Gruschow, S., Graham, S., Gloster, T. & White, M., 20 Jul 2020, In: eLife. 9, 19 p., e57627.

    Research output: Contribution to journalArticlepeer-review

  4. Exploitation of carbohydrate processing enzymes in biocatalysis

    Gloster, T. M., Apr 2020, In: Current Opinion in Chemical Biology. 55, p. 180-188 9 p.

    Research output: Contribution to journalReview articlepeer-review

  5. Structure and mechanism of a Type III CRISPR defence DNA nuclease activated by cyclic oligoadenylate

    McMahon, S., Zhu, W., Graham, S., Rambo, R., White, M. & Gloster, T., 24 Jan 2020, In: Nature Communications. 11, 11 p., 500.

    Research output: Contribution to journalArticlepeer-review

Related by journal

  1. On the interaction between human IQGAP1 and actin

    Magill, D., Hamilton, E., Shirran, S. L., Botting, C. H. & Timson, D., 2016, In: Protein & Peptide Letters. 23, 4

    Research output: Contribution to journalArticlepeer-review

  2. Composition and Functions of the Influenza Fusion Peptide

    Cross, K., Langley, WA., Russell, R. J. M., Skehel, JJ. & Steinhauer, DA., Jul 2009, In: Protein & Peptide Letters. 16, 7, p. 766-778 13 p.

    Research output: Contribution to journalArticlepeer-review

ID: 255285491

Top