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dc.contributor.authorZhang, Wenjing
dc.contributor.authorWu, Wanli
dc.contributor.authorBao, Yizhong
dc.contributor.authorYan, Xiaojun
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorJin, Weihua
dc.contributor.authorMao, Genxiang
dc.date2021
dc.date.accessioned2022-06-27T15:36:07Z
dc.date.available2022-06-27T15:36:07Z
dc.date.issued2021-11-07
dc.identifier.citationComparative study on the mechanisms of anti-lung cancer activities of three sulfated galactofucans, W. Zhang, W. Wu, Y. Bao, X. Yan, F. Zhang, R.J. Linhardt, W. Jin, G. Mao, Food and Function, 10644-10657, 2021.
dc.identifier.issn2042650X
dc.identifier.issn20426496
dc.identifier.urihttps://doi.org/10.1039/d1fo02062e
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5439
dc.descriptionFood and Function, 10644-10657
dc.descriptionNote : 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.
dc.description.abstractSulfated galactofucans, as the active compositions of fucoidan, were reported to exhibit antitumor activity. In the current study, a sulfated galactofucan (SGF) from Sargassum thunbergii and its three derivatives (SGF-H, SGF-L, and SGF-S) were prepared for structural analysis. Structural analysis showed that SGF-H was a high molecular weight sulfated galactofucan (51.5/17.8 kDa) with a high molar ratio of galactose (Gal) to fucose (Fuc) (0.66 : 1), SGF-L was a low molecular weight sulfated galactofucan (17.7 kDa) with a low molar ratio of Gal to Fuc (0.20 : 1), and SGF-S was a mixture (1.7 kDa) of sulfated galacto-fuco-oligomers or fuco-oligomers. It was noteworthy that the linkage of Gal residues in SGF-H was a β-linkage while SGF-L was an α-linkage. A comparative study on the anti-lung cancer activity in vitro and in vivo, antimetastatic effects, the metastasis-associated protein expression, and binding abilities to fibroblast growth factors (FGFs) of SGF, SGF-H, and SGF-L was performed to understand the structure–activity relationship. To some extent, SGF-L showed the strongest activity in the inhibition of human lung cancer cells A549 cell proliferation, while SGF-H exhibited the strongest activity in the inhibition of human bronchial epithelial cells BEAS-2B cell proliferation. SGF-L showed the strongest antimetastatic activity, followed by SGF-H and SGF. The expression of metastasis-associated proteins showed only a small difference. The in vivo tumor inhibition of SGF, SGF-H, and SGF-L was 45%, 41%, and 31%, respectively. SPR analysis showed SGF-H binds preferentially to FGF1 and FGF2, while SGF-L preferentially binds to FGF7 and FGF10, suggesting that the anti-lung cancer activity from sulfated galactofucan could involve the FGF-FAK/mTOR pathway.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1039/d1fo02062e
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofFood and Function
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleComparative study on the mechanisms of anti-lung cancer activities of three sulfated galactofucans
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1039/d1fo02062e
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1039/d1fo02062e
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages10644-10657
rpi.description.volume12


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