Different sucrose-isomaltase response of Caco-2 cells to glucose and maltose suggests dietary maltose sensing
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- Cheng Min-Wen
- Whistler Center for Carbohydrate Research, 745 Agriculture Mall Drive, Purdue University Department of Food Science, Purdue University
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- Chegeni Mohammad
- Whistler Center for Carbohydrate Research, 745 Agriculture Mall Drive, Purdue University Department of Food Science, Purdue University
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- Kim Kee-Hong
- Department of Food Science, Purdue University
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- Zhang Genyi
- School of Food Science and Technology, Jiangnan University
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- Benmoussa Mustapha
- School of Food Science and Technology, Jiangnan University
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- Quezada-Calvillo Roberto
- USDA/ARS Children’s Nutrition Research Center and the Department of Pediatrics, Baylor College of Medicine Department of Chemistry, Universidad Autonoma de San Luis Potosi
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- Nichols Buford L.
- USDA/ARS Children’s Nutrition Research Center and the Department of Pediatrics, Baylor College of Medicine
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- Hamaker Bruce R.
- Whistler Center for Carbohydrate Research, 745 Agriculture Mall Drive, Purdue University Department of Food Science, Purdue University
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抄録
Using the small intestine enterocyte Caco-2 cell model, sucrase-isomaltase (SI, the mucosal α-glucosidase complex) expression and modification were examined relative to exposure to different mono- and disaccharide glycemic carbohydrates. Caco-2/TC7 cells were grown on porous supports to post-confluence for complete differentiation, and dietary carbohydrate molecules of glucose, sucrose (disaccharide of glucose and fructose), maltose (disaccharide of two glucoses α-1,4 linked), and isomaltose (disaccharide of two glucoses α-1,6 linked) were used to treat the cells. qRT-PCR results showed that all the carbohydrate molecules induced the expression of the SI gene, though maltose (and isomaltose) showed an incremental increase in mRNA levels over time that glucose did not. Western blot analysis of the SI protein revealed that only maltose treatment induced a higher molecular weight band (Mw ~245 kDa), also at higher expression level, suggesting post-translational processing of SI, and more importantly a sensing of maltose. Further work is warranted regarding this putative sensing response as a potential control point for starch digestion and glucose generation in the small intestine.
収録刊行物
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- Ｊｏｕｒｎａｌ ｏｆ Ｃｌｉｎｉｃａｌ Ｂｉｏｃｈｅｍｉｓｔｒｙ ａｎｄ Ｎｕｔｒｉｔｉｏｎ
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Ｊｏｕｒｎａｌ ｏｆ Ｃｌｉｎｉｃａｌ Ｂｉｏｃｈｅｍｉｓｔｒｙ ａｎｄ Ｎｕｔｒｉｔｉｏｎ 54 (1), 55-60, 2014
一般社団法人 日本酸化ストレス学会
