Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells
AbstractRice 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. View Full-Text
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Nakata, H.; Lin, C.Y.; Abolhassani, M.; Ogawa, T.; Tateno, H.; Hirabayashi, J.; Muramoto, K. Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells. Int. J. Mol. Sci. 2017, 18, 1052.
Nakata H, Lin CY, Abolhassani M, Ogawa T, Tateno H, Hirabayashi J, Muramoto K. Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells. International Journal of Molecular Sciences. 2017; 18(5):1052.Chicago/Turabian Style
Nakata, Hajime; Lin, Ching Y.; Abolhassani, Maryam; Ogawa, Tomohisa; Tateno, Hiroaki; Hirabayashi, Jun; Muramoto, Koji. 2017. "Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells." Int. J. Mol. Sci. 18, no. 5: 1052.
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