Ginseng root water-extracted pectic polysaccharides originate from secretory cavities

Yu, Li; Zhou, Yifa; Knox, John

doi:10.1007/s00425-011-1417-9

Cited by 26 publications

(9 citation statements)

References 45 publications

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“…This is in line with our previous estimation of 1.87 residues per chain (34). To evaluate the chain length, we used an antibody, LM5, which recognizes ␤1,4-galactan chains with at least four consecutive Gal residues (41). In this study, we classified ␤1,4-galactan side chains that contain Ն4 consecutive Gal residues as long chains and those containing Յ3 consecutive Gal residues as short chains.…”

Section: Preparation and Structural Analysis Of Pectic Samplessupporting

confidence: 69%

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The Inhibitory Effects of a Rhamnogalacturonan Ι (RG-I) Domain from Ginseng Pectin on Galectin-3 and Its Structure-Activity Relationship

Gao

Yang

Sun

et al. 2013

Journal of Biological Chemistry

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115

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Background: Structural elements in pectin that inhibit galectin-3, a ␤-galactoside-binding protein associated with cancer progression, are poorly defined. Results: Both backbone and side chains of pectin RG-I-4 were important for its anti-galectin-3 activity. Conclusion: High activity of RG-I-4 was due to cooperation between short ␤1,4-galactan side chains. Significance: The results are valuable for producing highly active pectin-based galectin-3 inhibitors.

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Section: Preparation and Structural Analysis Of Pectic Samplessupporting

confidence: 69%

“…The ␤1,4-galactan epitope was identified with monoclonal antibody LM5 according to a published method (41). Each experiment was repeated at least three times.…”

Section: Enzyme-linked Immunosorbent Assay (Elisa)mentioning

confidence: 99%

The Inhibitory Effects of a Rhamnogalacturonan Ι (RG-I) Domain from Ginseng Pectin on Galectin-3 and Its Structure-Activity Relationship

Gao

Yang

Sun

et al. 2013

Journal of Biological Chemistry

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115

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“…Carbohydrate microarrays were performed according to the protocol described [24], [67]. The sequentially fractionated rice cell-wall residues, including TFA-insoluble and Updegraff-insoluble residues, were prepared as described [68], [69].…”

Section: Methodsmentioning

confidence: 99%

Brittle Culm1, a COBRA-Like Protein, Functions in Cellulose Assembly through Binding Cellulose Microfibrils

et al. 2013

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Cellulose represents the most abundant biopolymer in nature and has great economic importance. Cellulose chains pack laterally into crystalline forms, stacking into a complicated crystallographic structure. However, the mechanism of cellulose crystallization is poorly understood. Here, via functional characterization, we report that Brittle Culm1 (BC1), a COBRA-like protein in rice, modifies cellulose crystallinity. BC1 was demonstrated to be a glycosylphosphatidylinositol (GPI) anchored protein and can be released into cell walls by removal of the GPI anchor. BC1 possesses a carbohydrate-binding module (CBM) at its N-terminus. In vitro binding assays showed that this CBM interacts specifically with crystalline cellulose, and several aromatic residues in this domain are essential for binding. It was further demonstrated that cell wall-localized BC1 via the CBM and GPI anchor is one functional form of BC1. X-ray diffraction (XRD) assays revealed that mutations in BC1 and knockdown of BC1 expression decrease the crystallite width of cellulose; overexpression of BC1 and the CBM-mutated BC1s caused varied crystallinity with results that were consistent with the in vitro binding assay. Moreover, interaction between the CBM and cellulose microfibrils was largely repressed when the cell wall residues were pre-stained with two cellulose dyes. Treating wild-type and bc1 seedlings with the dyes resulted in insensitive root growth responses in bc1 plants. Combined with the evidence that BC1 and three secondary wall cellulose synthases (CESAs) function in different steps of cellulose production as revealed by genetic analysis, we conclude that BC1 modulates cellulose assembly by interacting with cellulose and affecting microfibril crystallinity.

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“…ELISA was performed as previously described (Yu et al, 2011). In all cases, mucilage extractions were coated onto microtiter plates (3599; Costa) at 100 mg mL 21 concentrations.…”

Section: Elisa and Immunolabeling Proceduresmentioning

confidence: 99%

CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed

Shi

et al. 2014

Plant Physiol.

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126

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Mannans are hemicellulosic polysaccharides that are considered to have both structural and storage functions in the plant cell wall. However, it is not yet known how mannans function in Arabidopsis (Arabidopsis thaliana) seed mucilage. In this study, CELLULOSE SYNTHASE-LIKE A2 (CSLA2; At5g22740) expression was observed in several seed tissues, including the epidermal cells of developing seed coats. Disruption of CSLA2 resulted in thinner adherent mucilage halos, although the total amount of the adherent mucilage did not change compared with the wild type. This suggested that the adherent mucilage in the mutant was more compact compared with that of the wild type. In accordance with the role of CSLA2 in glucomannan synthesis, csla2-1 mucilage contained 30% less mannosyl and glucosyl content than did the wild type. No appreciable changes in the composition, structure, or macromolecular properties were observed for nonmannan polysaccharides in mutant mucilage. Biochemical analysis revealed that cellulose crystallinity was substantially reduced in csla2-1 mucilage; this was supported by the removal of most mucilage cellulose through treatment of csla2-1 seeds with endo-b-glucanase. Mutation in CSLA2 also resulted in altered spatial distribution of cellulose and an absence of birefringent cellulose microfibrils within the adherent mucilage. As with the observed changes in crystalline cellulose, the spatial distribution of pectin was also modified in csla2-1 mucilage. Taken together, our results demonstrate that glucomannans synthesized by CSLA2 are involved in modulating the structure of adherent mucilage, potentially through altering cellulose organization and crystallization.Mannan polysaccharides are a complex set of hemicellulosic cell wall polymers that are considered to have both structural and storage functions. Based on the particular chemical composition of the backbone and the side chains, mannan polysaccharides are classified into four types: pure mannan, glucomannan, galactomannan, and galactoglucomannan (Moreira and Filho, 2008;Wang et al., 2012;Pauly et al., 2013). Each of these polysaccharides is composed of a b-1,4-linked backbone containing Man or a combination of Glc and Man residues. In addition, the mannan backbone can be substituted with side chains of a-1,6-linked Gal residues. Mannan polysaccharides have been proposed to cross link with cellulose and other hemicelluloses via hydrogen bonds (Fry, 1986;Iiyama et al., 1994;Obel et al., 2007;Scheller and Ulvskov, 2010). Furthermore, it has been reported that heteromannans with different levels of substitution can interact with cellulose in diverse ways (Whitney et al., 1998). Together, these observations indicate the complexity of mannan polysaccharides in the context of cell wall architecture.CELLULOSE SYNTHASE-LIKE A (CSLA) enzymes have been shown to have mannan synthase activity in vitro. These enzymes polymerize the b-1,4-linked backbone of mannans or glucomannans, depending on the substrates (GDP-Man and/or GDP-Glc) provided (Richmond and Some...

show abstract

Ginseng root water-extracted pectic polysaccharides originate from secretory cavities

Cited by 26 publications

References 45 publications

The Inhibitory Effects of a Rhamnogalacturonan Ι (RG-I) Domain from Ginseng Pectin on Galectin-3 and Its Structure-Activity Relationship

The Inhibitory Effects of a Rhamnogalacturonan Ι (RG-I) Domain from Ginseng Pectin on Galectin-3 and Its Structure-Activity Relationship

Brittle Culm1, a COBRA-Like Protein, Functions in Cellulose Assembly through Binding Cellulose Microfibrils

CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed

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