Structural Study of Sulfated Fuco-Oligosaccharide Branched Glucuronomannan from<i>Kjellmaniella crassifolia</i>by ESI-CID-MS/MS

Wu, Jiandong; Lv, Yanna; Liu, Huan; Zhao, Xiaoliang; Jiao, Guangling; Tai, Wenjing; Wang, Peipei; Zhao, Xia; Cai, Chao; Yu, Guangli

doi:10.1080/07328303.2015.1050593

Cited by 20 publications

(11 citation statements)

References 34 publications

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“…According to our monosaccharide composition analysis, these three fucoidans were mainly composed of fucose, and the contents of fucose were similar in AnF and LjF, while KcF had a much higher fucose content ( p < 0.05). The above results were consistent with that reported in previous literatures [ 32 , 33 , 34 ]. In general, the main differences between these three fucoidans were the type of glycosidic linkages, MWs, and fucose content.…”

Section: Resultssupporting

confidence: 94%

“…To explore the relationship between the inhibitory effect of glucose absorption and fucoidan, it is necessary to rule out the other factors related to antihyperglycemia. Therefore, we prepared three fucoidans as follows: fucoidan from Ascophyllum nodosum (AnF) with a type II structure [ 32 ] and mild inhibition of α-glucosidase [ 31 ], and fucoidans from Laminaria japonica (LjF) and Kjellmaniella crassifolia (KcF) with type I structures [ 33 , 34 ]. Additionally, we investigated the pharmacological effects of the above fucoidans on alleviating postprandial hyperglycemia using in vitro (Caco-2 monolayer model), semi-in vivo (everted gut sac model), and in vivo (oral glucose tolerance test (OGTT) in Kunming and leptin receptor-deficient (db/db) mice) assays.…”

Section: Introductionmentioning

confidence: 99%

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Fucoidan from Ascophyllum nodosum Suppresses Postprandial Hyperglycemia by Inhibiting Na+/Glucose Cotransporter 1 Activity

et al. 2020

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We previously demonstrated that fucoidan with a type II structure inhibited postprandial hyperglycemia by suppressing glucose uptake, but the mechanism remains elusive. Here, we aimed to assess whether the effect of glucose absorption inhibition was related to the basic structure of fucoidans and preliminarily clarified the underlying mechanism. Fucoidans with type II structure and type I structure were prepared from Ascophyllumnodosum (AnF) or Laminariajaponica (LjF) and Kjellmaniellacrassifolia (KcF), respectively. The effects of various fucoidans on suppressing postprandial hyperglycemia were investigated using in vitro (Caco-2 monolayer model), semi-in vivo (everted gut sac model), and in vivo (oral glucose tolerance test, OGTT) assays. The results showed that only AnF with a type II structure, but not LjF or KcF with type I structure, could inhibit the glucose transport in the Caco-2 monolayer and everted gut sac models. A similar result was seen in the OGTT of Kunming mice and leptin receptor-deficient (db/db) mice, where only AnF could effectively inhibit glucose transport into the bloodstream. Furthermore, AnF (400 mg/kg/d) treatment decreased the fasting blood glucose, HbA1c, and fasting insulin levels, while increasing the serum glucagon-like peptide-1 (GLP-1) level in obese leptin receptor-deficient (db/db) mice. Furthermore, surface plasmon resonance (SPR) analysis revealed the specific binding of AnF to Na+/glucose cotransporter 1 (SGLT1), which indicated the effect of AnF on postprandial hyperglycemia could be due to its suppression on SGLT1 activity. Taken together, this study suggests that AnF with a type II structure can be a promising candidate for hyperglycemia treatment.

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Section: Resultssupporting

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Fucoidan from Ascophyllum nodosum Suppresses Postprandial Hyperglycemia by Inhibiting Na+/Glucose Cotransporter 1 Activity

et al. 2020

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“…Whereas GH families 2 and 3 are functionally diverse, GH88 enzymes are unsaturated β-glucuronyl hydrolases. This functional combination of CAZymes suggests degradation of α-glucomannans such as glucuronomannan, a polysaccharide that has been reported for diatoms [17, 19, 49] and brown algae [66] and thus should be abundant in the southern North Sea. Finally, co-located peptidases and a gene distantly related to GH99, a family that is reported to contain glycoprotein endo-α-mannosidases, indicate that this hypothesized glucuronomannan substrate might be a glycoprotein.…”

Section: Resultsmentioning

confidence: 71%

Polysaccharide utilization loci of North Sea Flavobacteriia as basis for using SusC/D-protein expression for predicting major phytoplankton glycans

et al. 2018

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Marine algae convert a substantial fraction of fixed carbon dioxide into various polysaccharides. Flavobacteriia that are specialized on algal polysaccharide degradation feature genomic clusters termed polysaccharide utilization loci (PULs). As knowledge on extant PUL diversity is sparse, we sequenced the genomes of 53 North Sea Flavobacteriia and obtained 400 PULs. Bioinformatic PUL annotations suggest usage of a large array of polysaccharides, including laminarin, α-glucans, and alginate as well as mannose-, fucose-, and xylose-rich substrates. Many of the PULs exhibit new genetic architectures and suggest substrates rarely described for marine environments. The isolates' PUL repertoires often differed considerably within genera, corroborating ecological niche-associated glycan partitioning. Polysaccharide uptake in Flavobacteriia is mediated by SusCD-like transporter complexes. Respective protein trees revealed clustering according to polysaccharide specificities predicted by PUL annotations. Using the trees, we analyzed expression of SusC/D homologs in multiyear phytoplankton bloom-associated metaproteomes and found indications for profound changes in microbial utilization of laminarin, α-glucans, β-mannan, and sulfated xylan. We hence suggest the suitability of SusC/D-like transporter protein expression within heterotrophic bacteria as a proxy for the temporal utilization of discrete polysaccharides.

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“…The structure of KW was determined by nuclear magnetic resonance spectroscopy (NMR) and electrospray ionization mass spectrometry (ESI-MS) analysis, which showed that KW is a 3-linked 2,4- O -disulfated fucooligosaccharide branched glucuronomannan (Fig. 1A)23.…”

Section: Resultsmentioning

confidence: 99%

Inhibition of Influenza A Virus Infection by Fucoidan Targeting Viral Neuraminidase and Cellular EGFR Pathway

Wang

Zhang

et al. 2017

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Development of novel anti-influenza A virus (IAV) drugs with high efficiency and low toxicity is critical for preparedness against influenza outbreaks. Herein, we investigated the anti-IAV activities and mechanisms of fucoidan in vitro and in vivo. The results showed that a fucoidan KW derived from brown algae Kjellmaniella crassifolia effectively blocked IAV infection in vitro with low toxicity. KW possessed broad anti-IAV spectrum and low tendency of induction of viral resistance, superior to the anti-IAV drug amantadine. KW was capable of inactivating virus particles before infection and blocked some stages after adsorption. KW could bind to viral neuraminidase (NA) and inhibit the activity of NA to block the release of IAV. KW also interfered with the activation of EGFR, PKCα, NF-κB, and Akt, and inhibited both IAV endocytosis and EGFR internalization in IAV-infected cells, suggesting that KW may also inhibit cellular EGFR pathway. Moreover, intranasal administration of KW markedly improved survival and decreased viral titers in IAV-infected mice. Therefore, fucoidan KW has the potential to be developed into a novel nasal drop or spray for prevention and treatment of influenza in the future.

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Structural Study of Sulfated Fuco-Oligosaccharide Branched Glucuronomannan fromKjellmaniella crassifoliaby ESI-CID-MS/MS

Cited by 20 publications

References 34 publications

Fucoidan from Ascophyllum nodosum Suppresses Postprandial Hyperglycemia by Inhibiting Na+/Glucose Cotransporter 1 Activity

Fucoidan from Ascophyllum nodosum Suppresses Postprandial Hyperglycemia by Inhibiting Na+/Glucose Cotransporter 1 Activity

Polysaccharide utilization loci of North Sea Flavobacteriia as basis for using SusC/D-protein expression for predicting major phytoplankton glycans

Inhibition of Influenza A Virus Infection by Fucoidan Targeting Viral Neuraminidase and Cellular EGFR Pathway

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