Isolation and composition analysis of bioactive glycosaminoglycans from whelk

Khurshid, CA and Pye, DA ORCID: https://orcid.org/0000-0003-2036-2693 2018, 'Isolation and composition analysis of bioactive glycosaminoglycans from whelk' , Marine Drugs, 16 (5) , 0171.

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Abstract

Glycosaminoglycans (GAGs) are found covalently attached to proteins, which create conjugates known as proteoglycans. GAGs have remarkable biological activity as co-receptors for a variety of growth factors, cytokines, and chemokines. The present study identifies the key compositional differences between the GAGs isolated from whelk and mammalian GAGs. This polysaccharide represents a new, previously undescribed GAG with cytotoxic activity on cancer cells. Disaccharides were obtained by sample digestion with heparinases I, II, and III and chondroitinase ABC. The resistant oligosaccharides from whelk GAGs treated with heparinase I, II, and III and chondroitinase ABC were retained by the filter due to their larger size. Disaccharide analysis was performed using Glycan Reduction Isotope Labeling (GRIL LCQ-MS). The amounts of filter-retained fragments, as assessed by monosaccharides analysis, suggested that a proportion of the whelk GAG chains remained resistant to the enzymes used in the disaccharide analysis. Thus, the proportions of individual disaccharide produced in this analysis may not truly represent the overall proportions of disaccharide types within the intact whelk GAGs chain. However, they do serve as important descriptors for the classification and make-up of the anti-cancer GAGs chains. Furthermore, these data represent clear evidence of the compositional differences between whelk GAGs and commercial mammalian GAGs.

Item Type: Article
Schools: Schools > School of Environment and Life Sciences > Biomedical Research Centre
Schools > School of Environment and Life Sciences > Ecosystems and Environment Research Centre
Journal or Publication Title: Marine Drugs
Publisher: MDPI
ISSN: 1660-3397
Related URLs:
Depositing User: DA Pye
Date Deposited: 06 Jun 2018 12:48
Last Modified: 28 May 2019 13:43
URI: http://usir.salford.ac.uk/id/eprint/47258

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