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.
Highlights
Glycosaminoglycans (GAGs) are found covalently attached to proteins, creating conjugates known as proteoglycans
Of the N-sulphated disaccharides found in CK-1, compared with 61–62% present in commercial heparan sulphate (HS), in terms of individual disaccharide, which suggested that ∆HexA2S-GlcNS and ∆HexA2SGlcNS6S
Disaccharide analysis confirmed the presence of chondroitin sulphate (CS) chains in the whelk samples CK-1, CK-2 and CK-3, and the amount of individual CS disaccharide was determined by Glycan Reductive Isotope Labelling (GRIL) LCQ-MS GAGs disaccharide analysis
Summary
Glycosaminoglycans (GAGs) are found covalently attached to proteins, creating conjugates known as proteoglycans. It was thought that GAGs only existed in mammals. They are found in a wide variety of organisms, including fishes, insects, fungi, yeast, and bacteria. It is a rich component in the muscle of shellfish [1]. Glycosaminoglycans have remarkable biological activities as co-receptors for a variety of growth factors, cytokines, and chemokines [2]. The biological function of proteoglycans includes the regulation of cell proliferation through the interaction of the GAGs chains in proteoglycans with proteins, such as growth factors and their receptors [4]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
