Author:
Brun Lucas R.,Brance María L.,Rigalli Alfredo
Abstract
Intestinal alkaline phosphatase (IAP) is a brush-border phosphomonoesterase. Its location suggests an involvement in the uptake of nutrients, but its role has not yet been defined. IAP expression parallels that of other proteins involved in Ca absorption under vitamin D stimulation. Experiments carried outin vitrowith purified IAP have demonstrated an interaction between Ca and IAP. The gut is prepared to face different levels of Ca intake over time, but high Ca intake in a situation of a low-Ca diet over time would cause excessive entry of Ca into the enterocytes. The presence of a mechanism to block Ca entry and to avoid possible adverse effects is thus predictable. Thus, in the present study, Sprague–Dawley rats were fed with different amounts of Ca in the diet (0·2, 1 and 2 g%), and the percentage of Ca absorption (%Ca) in the presence and absence ofl-phenylalanine (Phe) was calculated. The presence of Phe caused a significant increase in %Ca (52·3 (sem6·5) % in the presence of Phev. 31·1 (sem8·9) % in the absence of Phe, regardless of the amount of Ca intake; pairedttest,P = 0·02). When data were analysed with respect to Ca intake, a significant difference was found only in the group with low Ca intake (pairedttest,P = 0·03). Additionally, IAP activity increased significantly (ANOVA,P < 0·05) as Ca concentrations increased in the duodenal lumen. The present study providesin vivoevidence that luminal Ca concentration increases the activity of IAP and simultaneously decreases %Ca, acting as a minute-to-minute regulatory mechanism of Ca entry.
Publisher
Cambridge University Press (CUP)
Subject
Nutrition and Dietetics,Medicine (miscellaneous)
Cited by
27 articles.
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