101. Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells.
- Author
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Nakata H, Lin CY, Abolhassani M, Ogawa T, Tateno H, Hirabayashi J, and Muramoto K
- Subjects
- Caco-2 Cells drug effects, Carbohydrates chemistry, Colonic Neoplasms genetics, Colonic Neoplasms pathology, Fetuins metabolism, Glycoproteins metabolism, Humans, Oryza chemistry, Plant Lectins chemistry, Plant Lectins isolation & purification, Transferrin metabolism, Colonic Neoplasms drug therapy, Plant Lectins genetics, Plant Lectins metabolism
- Abstract
Rice bran lectins, named as RBA1 and RBA2, were isolated from Oryza sativa in two chromatography steps: affinity chromatography and cation-exchange chromatography. RBA1 was found to be composed of a covalently linked heterodimer of 20- and 12-kDa subunits, and RBA2 was a noncovalently linked dimer of 12-kDa subunits. Both RBA1 and RBA2 bound to desialylated complex glycoproteins such as fetuin, α1-acid glycoprotein, and transferrin, and agalactosylated complex glycoproteins such as agalacto fetuin, agalacto-α1-acid glycoprotein, and agalacto-transferrin, in addition to chitooligosacchrides. RBAs were heat stable up to 80 °C and stable at pH 4-10. RBA1 increased the transport of the fluorescent marker, rhodamine 123, which is known to be transported via the P-glycoprotein-mediated efflux pathway across human intestinal Caco-2 cell monolayers. Furthermore, RBA1 itself was transported to the basolateral side of the monolayers via an endocytotic pathway.
- Published
- 2017
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