Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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Glycosaminoglycans from fish swim bladder: isolation, structural characterization and bioactive potential, Y. Pan, P. Wang, F. Zhang, Y. Yu, X. Zhang, L. Lin, R. J. Linhardt, Glycoconjugate Journal, 35, 87–94, 2018
The swim bladder of fish is an internal gas-filled organ that allows fish to control their buoyancy and swimming depth. Fish maws (the dried swim bladders of fish) have been used over many centuries as traditional medicines, tonics and a luxurious gourmet food in China and Southeast Asia. Little is known about the structural information of polysaccharides comprising this important functional material of fish tissue. In the present study, the total glycosaminoglycan (GAG) from fish maw was characterized. Two GAGs were identified, chondroitin sulfate (CS, having a molecular weight of 18-40 kDa) and heparan sulfate (HS), corresponding to 95% and 5% of the total GAG, respectively. Chondroitinase digestion showed that the major CS GAG was composed of ΔUA-1 → 3-GalNAc4S (59.7%), ΔUA-1 → 3-GalNAc4,6S (36.5%), ΔUA-1 → 3-GalNAc6S (2.2%) and ΔUA-1 → 3-GalNAc (1.6%) disaccharide units. 1H-NMR analysis and degradation with specific chondroitinases, both CS-type A/C and CS-type B were present in a ratio of 1.4:1. Analysis using surface plasmon resonance showed that fibroblast growth factor (FGF)-2 bound to the CS fraction (KD = 136 nM). These results suggest that this CS may be involved in FGF-signal pathway, mediating tissue repair, regeneration and wound healing. The CS, as the major GAG in fish maw, may have potential pharmacological activity in accelerating wound healing.;
Glycoconjugate Journal, 35, 87–94; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Glycoconjugate Journal; https://harc.rpi.edu/;