Unknown

Dataset Information

0

Lactose and Galactose Promote the Crystallization of Human Galectin-10.


ABSTRACT: Galectin-10 (Gal-10) forms Charcot-Leyden crystals (CLCs), which play a key role in the symptoms of asthma and allergies and some other diseases. Gal-10 has a carbohydrate-binding site; however, neither the Gal-10 dimer nor the CLCs can bind sugars. To investigate the monomer-dimer equilibrium of Gal-10, high-performance size-exclusion chromatography (SEC) was employed to separate serial dilutions of Gal-10 with and without carbohydrates. We found that both the dimerization and crystallization of Gal-10 were promoted by lactose/galactose binding. A peak position shift for the monomer was observed after treatment with either lactose or galactose, implying that the polarity of the monomer was reduced by lactose/galactose binding. Further experiments indicated that alkaline conditions of pH 8.8 mimicked the lactose/galactose-binding environment, and the time interval between monomers and dimers in the chromatogram decreased from 0.8 min to 0.4 min. Subsequently, the electrostatic potential of the Gal-10 monomers was computed. After lactose/galactose binding, the top side of the monomer shifted from negatively charged to electrically neutral, allowing it to interact with the carbohydrate-binding site of the opposing subunit during dimerization. Since lactose/galactose promotes the crystallization of Gal-10, our findings implied that dairy-free diets (free of lactose/galactose) might be beneficial to patients with CLC-related diseases.

SUBMITTER: Fu YF 

PROVIDER: S-EPMC9966682 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Lactose and Galactose Promote the Crystallization of Human Galectin-10.

Fu Yu-Fan YF   Jiang Si-Cong SC   Zhang Zhong-Wei ZW   Yang Xin-Yue XY   Li Zi-Lin ZL   Hu Jing J   Yuan Shu S  

Molecules (Basel, Switzerland) 20230219 4


Galectin-10 (Gal-10) forms Charcot-Leyden crystals (CLCs), which play a key role in the symptoms of asthma and allergies and some other diseases. Gal-10 has a carbohydrate-binding site; however, neither the Gal-10 dimer nor the CLCs can bind sugars. To investigate the monomer-dimer equilibrium of Gal-10, high-performance size-exclusion chromatography (SEC) was employed to separate serial dilutions of Gal-10 with and without carbohydrates. We found that both the dimerization and crystallization o  ...[more]

Similar Datasets

| S-EPMC3328751 | biostudies-literature
| S-EPMC2443957 | biostudies-literature
| S-EPMC7889132 | biostudies-literature
| S-EPMC2339748 | biostudies-literature
| S-EPMC107515 | biostudies-literature
| S-EPMC4734333 | biostudies-literature
| S-EPMC161534 | biostudies-literature
| S-EPMC6596385 | biostudies-literature
2013-01-01 | GSE26772 | GEO
| S-EPMC9506588 | biostudies-literature