Ontogeny of brush border carbohydrate digestion and uptake in the chick

David Sklan, Asaf Geyra, Elad Tako, Orit Gal-Gerber, Zehava Uni
2003 British Journal of Nutrition  
Ingestion of carbohydrates from the small intestine is the major route of energy supply in animals. In mammals these functions develop both pre-and postnatally and are coordinated for the sucking period. In birds, the physiological requirements are different and hatchlings ingest diets rich in complex carbohydrates soon after hatching. The present study examined the ontogeny of intestinal carbohydrate uptake in the chicken. The expression of mRNA for a brush border enzyme, sucrase -isomaltase
more » ... crase -isomaltase (SI), which is critical in disaccharide digestion, was determined, together with that of the Na -glucose transporter (SGLT)-1, which is the major apical glucose transporter, In addition, the homeobox gene cdx, which is involved in inducing SI expression in mammals was examined. It was found that the expression of cdxA mRNA and cdxA protein increased from day 15 of incubation until hatch, after which further changes were small. CdxA protein was shown to bind to the promoter region of SI in the chick indicating that cdxA is similar to the mammalian cdx2. The mRNA of SI was observed at 15 d incubation, increased from 17 d of incubation to a peak on day 19, decreased at hatch and had a further peak of expression 2 d post-hatch. In contrast, the mRNA of SGLT-1 was not detected until 19 d of incubation when a major peak of expression was observed followed by a decrease to low levels at hatch and small increases post-hatch. It appears that both SI and SGLT-1 mRNA are expressed before hatch in the chick, but the ontogeny of expression is controlled by different mechanisms. Small intestine: Ontogeny: Carbohydrate: Chick * Corresponding author: Professor D. Sklan, fax +972 8 9489865, email sklan@agri.huji.ac.il Abbreviations: cdx, homeobox gene of the caudal family; EMSA, electrophoretic mobility shift assay; SGLT, Na -glucose transporter; SI, sucrase -isomaltase.
doi:10.1079/bjn2003853 pmid:12828791 fatcat:fg6lkcvmgbfujfcij7kyjfzgze