Characterization of the interaction between hydroxypropyl guar galactomannan and galectin-3

Woodward, Ashley M.; Senchyna, Michelle; Williams, Ravaughn; Argüeso, Pablo

doi:10.1016/j.bbrc.2012.05.160

Cited by 6 publications

(5 citation statements)

References 31 publications

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“…xylanases, xylanases A and B from Antarctic krill (Euphausia superba Dana) have the highest optimum temperature (37-40 C) [23] and Xyn8 from an environmental DNA library, the lowest optimum temperature (20 C) [8]. Xyn27 in the present study showed optimal activity at 35 C, which is the same as xylanases XynAHJ2 from Bacillus sp.…”

Section: Effects Of Ph and Temperature On The Activity Of Recombinantsupporting

confidence: 58%

Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil

Qiu

Wang

et al. 2017

Biotechnology & Biotechnological Equipment

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A novel xylanase gene of family 10 (xyn27) was obtained from the genomic DNA of frozen soil of Daxinganling in China by Touchdown polymerase chain reaction (PCR) and thermal asymmetric interlaced (TAIL) PCR methods. Xyn27 contained a putative signal peptide (20 residues) and a catalytic motif of GH10 (327 residues) and shared the highest similarity (83%) with the reported GH10 xylanase (XM ç 003662144). The recombinant xyn27 was successfully expressed in Pichia pastoris GS115 and the optimal induction condition was 30 C for 48 h. Xyn27 was demonstrated to be a cold-active xylanase, which shows its highest activity at 35 C and still had 60.25%, 38.70% and 10.8% relative activity at 20 C, 10 C and 0 C. Further analysis showed that Xyn27 has fewer arginine and more alanine residues compared with its mesophilic or thermophilic counterparts. The optimal pH of Xyn27 was 7.0, and it was stable after incubating under the pH range from 3.0 to 9.0 for 1 h. Besides, Xyn27 exhibited superior metal ion tolerance than other GH10 cold-active xylanases, being tolerant to most metal ions and organic solvents, and significantly enhanced by Ca 2+ , Mn 2+ and Zn 2+ metal ions. In addition, the K m , V max , k cat and k cat K m ¡1 against beechwood xylan were 13.42 mg mL ¡1 , 9.07 mmol min ¡1 mg ¡1 , 192.98 min ¡1 and 14.38 mL min ¡1 mg ¡1 , and Xyn27 could completely degrade xylan into xylobiose. The features of cold activity and metal-ion tolerance suggested that xylanase Xyn27 could have potential application in basic research and various industries like food possessing.

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Section: Effects Of Ph and Temperature On The Activity Of Recombinantsupporting

confidence: 58%

Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil

Qiu

Wang

et al. 2017

Biotechnology & Biotechnological Equipment

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“…In human corneal epithelial cells, competitive inhibition of galectin binding and abrogation of c1galt1—a critical galactosyltransferase required for the synthesis of core 1 mucin O-glycans—has been associated with loss of barrier function [10], [31]. In addition to galectin-3, several members of the galectin family, such as galectins -8 and -9 [20], [32] and galectins -1 and -7 [33], have been detected in human and mouse ocular surface epithelial cells, respectively. In our experiments, selective abrogation of galectin-3 biosynthesis in vitro and in vivo resulted in increased permeability to the rose bengal diagnostic dye (Figures 1,2), indicating a role for this galectin in maintaining glycocalyx barrier function.…”

Section: Discussionmentioning

confidence: 99%

Modulation of Ocular Surface Glycocalyx Barrier Function by a Galectin-3 N-terminal Deletion Mutant and Membrane-Anchored Synthetic Glycopolymers

et al. 2013

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BackgroundInteraction of transmembrane mucins with the multivalent carbohydrate-binding protein galectin-3 is critical to maintaining the integrity of the ocular surface epithelial glycocalyx. This study aimed to determine whether disruption of galectin-3 multimerization and insertion of synthetic glycopolymers in the plasma membrane could be used to modulate glycocalyx barrier function in corneal epithelial cells.Methodology/Principal FindingsAbrogation of galectin-3 biosynthesis in multilayered cultures of human corneal epithelial cells using siRNA, and in galectin-3 null mice, resulted in significant loss of corneal barrier function, as indicated by increased permeability to the rose bengal diagnostic dye. Addition of β-lactose, a competitive carbohydrate inhibitor of galectin-3 binding activity, to the cell culture system, transiently disrupted barrier function. In these experiments, treatment with a dominant negative inhibitor of galectin-3 polymerization lacking the N-terminal domain, but not full-length galectin-3, prevented the recovery of barrier function to basal levels. As determined by fluorescence microscopy, both cellobiose- and lactose-containing glycopolymers incorporated into apical membranes of corneal epithelial cells, independently of the chain length distribution of the densely glycosylated, polymeric backbones. Membrane incorporation of cellobiose glycopolymers impaired barrier function in corneal epithelial cells, contrary to their lactose-containing counterparts, which bound to galectin-3 in pull-down assays.Conclusions/SignificanceThese results indicate that galectin-3 multimerization and surface recognition of lactosyl residues is required to maintain glycocalyx barrier function at the ocular surface. Transient modification of galectin-3 binding could be therapeutically used to enhance the efficiency of topical drug delivery.

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“…Galactose-containing polysaccharides were investigated as potential ligands for targeting galectins, [40][41][42][43][44] and therefore can be a good candidates for targeting Gal-3 on the reactive gliosis membrane. Pectin is a non-toxic and biocompatible natural polysaccharide which contains galactose.…”

Section: A Cooh-terminal Carbohydrate Recognition Domain (Crd)mentioning

confidence: 99%

Pectic Galactan Polysaccharide‐Based Gene Delivery System for Targeting Neuroinflammation

Buaron

Mangraviti

Volpin

et al. 2021

Adv Funct Materials

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Treating neuroinflammation-related injuries and disorders through manipulation of neuroinflammation functions is being heralded as a new therapeutic strategy. In this study, a novel pectic galactan (PG) polysaccharide based gene therapy approach is developed for targeting reactive gliosis in neuroinflammation. Galectin-3 (Gal-3) is a cell protein with a high affinity to β-galactoside sugars and is highly expressed in reactive gliosis. Since PG carries galactans, it can target reactive gliosis via specific carbohydrate interaction between galactan and Gal-3 on the cell membrane, and therefore can be utilized as a carrier for delivering genes to these cells. The carrier is synthesized by modifying quaternary ammonium groups on the PG. The resulting quaternized PG (QPG) is found to form complexes with plasmid DNA with a mean diameter of 100 nm and have the characteristics required for targeted gene therapy. The complexes efficiently condense large amounts of plasmid per particle and successfully bind to Gal-3. The in vivo study shows that the complexes are biocompatible and safe for administration and can selectively transfect reactive glial cells of an induced cortical lesion. The results confirm that this PG-based delivery system is a promising platform for targeting Gal-3 overexpressing neuroinflammation cells for treating neuroinflammation-related injuries and neurodegenerative diseases.

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Characterization of the interaction between hydroxypropyl guar galactomannan and galectin-3

Cited by 6 publications

References 31 publications

Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil

Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil

Modulation of Ocular Surface Glycocalyx Barrier Function by a Galectin-3 N-terminal Deletion Mutant and Membrane-Anchored Synthetic Glycopolymers

Pectic Galactan Polysaccharide‐Based Gene Delivery System for Targeting Neuroinflammation

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