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The enzymatic degradation of heparan sulfate

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Griffin_2017_Enzymatic_degradation_PPL_AAM.pdf (580.3Kb)
Date
01/08/2017
Author
Griffin, Laura Susan
Gloster, Tracey Maureen
Funder
The Wellcome Trust
Grant ID
095828/Z/11/Z
Keywords
Glycosaminoglycan
Heparan sulfate
Degradation
Lysosome
Mucopolysaccharidoses
Enzymes
QD Chemistry
QH301 Biology
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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.
Citation
Griffin , L S & Gloster , T M 2017 , ' The enzymatic degradation of heparan sulfate ' , Protein & Peptide Letters , vol. 24 , no. 8 , pp. 710-722 . https://doi.org/10.2174/0929866524666170724113452
Publication
Protein & Peptide Letters
Status
Peer reviewed
DOI
https://doi.org/10.2174/0929866524666170724113452
ISSN
0929-8665
Type
Journal item
Rights
© 2017, Bentham Science Publishers. This work has been made available online in accordance with the publisher’s policies. This is the author created accepted version manuscript following peer review and as such may differ slightly from the final published version. The final published version of this work is available at https://doi.org/10.2174/0929866524666170724113452
Description
Funding: Wellcome Trust (Research Career Development Fellowship to TMG) and the BBSRC (studentship to LSG).
Collections
  • University of St Andrews Research
URI
http://hdl.handle.net/10023/15828

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