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Int. J. Mol. Sci. 2017, 18(5), 1052;

Isolation of Rice Bran Lectins and Characterization of Their Unique Behavior in Caco-2 Cells

Graduate School of Life Sciences, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan
National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Ibaraki 305-8568, Japan
Author to whom correspondence should be addressed.
Academic Editor: Els Van Damme
Received: 29 March 2017 / Revised: 5 May 2017 / Accepted: 10 May 2017 / Published: 13 May 2017
(This article belongs to the Special Issue Plant Lectins: From Model Species to Crop Plants)
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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. View Full-Text
Keywords: Oryza sativa; lectin; rice bran lectin; Caco-2 cells Oryza sativa; lectin; rice bran lectin; Caco-2 cells

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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.

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