Isolation of rice bran lectins and characterization of their unique behavior in caco-2 cells

Hajime Nakata, Ching Yu Lin, Maryam Abolhassani, Tomohisa Ogawa, Hiroaki Tateno, Jun Hirabayashi, Koji Muramoto

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9 Citations (Scopus)


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 80C 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.

Original languageEnglish
Article number1052
JournalInternational Journal of Molecular Sciences
Issue number5
Publication statusPublished - 2017 May 13


  • Caco-2 cells
  • Lectin
  • Oryza sativa
  • Rice bran lectin


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