Milk glucosidase activity enables suckled pup starch digestion

ᅟ Starch requires six enzymes for digestion to free glucose: two amylases (salivary and pancreatic) and four mucosal maltase activities; sucrase-isomaltase and maltase-glucoamylase. All are deficient in suckling rodents. Objective The objective of this study is to test 13 C-starch digestion before w...

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Veröffentlicht in:Molecular and cellular pediatrics 2016-02, Vol.3 (1), p.4-6, Article 4
Hauptverfasser: Nichols, B. L., Diaz-Sotomayor, M., Avery, S. E., Chacko, S. K., Hadsell, D. L., Baker, S. S., Hamaker, B. R., Yan, L. K., Lin, H. M., Quezada-Calvillo, R.
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Sprache:eng
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Zusammenfassung:ᅟ Starch requires six enzymes for digestion to free glucose: two amylases (salivary and pancreatic) and four mucosal maltase activities; sucrase-isomaltase and maltase-glucoamylase. All are deficient in suckling rodents. Objective The objective of this study is to test 13 C-starch digestion before weaning by measuring enrichment of blood 13 C-glucose in maltase-glucoamylase-null and wild-type mice. Methods Maltase-glucoamylase gene was ablated at the N-terminal. Dams were fed low 13 C-diet and litters kept on low 13 C-diet. Pups were weaned at 21 days. Digestion was tested at 13 and 25 days by intragastric feeding of amylase predigested 13 C-α-limit dextrins. Blood 13 C-glucose enrichment was measured by gas chromatography combustion isotope ratio mass spectrometry (GCRMS) using penta-acetate derivatives. Results Four hours after feeding, blood 13 C-glucose was enriched by 26 × 10 3 in null and 18 × 10 3 in wild-type mice at 13 days and 0.3 × 10 3 and 0.2 × 103 at 25 days (vs. fasting p  = 0.045 and p  = 0.045). By jejunal enzyme assay, immunohistochemistry, or Western blots, there was no maltase activity or brush border staining with maltase-glucoamylase antibodies at 13 days, but these were fully developed in the wild-type mice by 25 days. In 13-day null mice, luminal contents were stained by maltase-glucoamylase antibodies. Lactating the mammary gland revealed maltase-glucoamylase antibody staining of alveolar cells. Reverse transcription/polymerase chain reaction (RT/PCR) of lactating glands revealed a secreted form of maltase-glucoamylase. Conclusions (1) 13 C-α-limit dextrins were rapidly digested to 13 C-glucose in 13-day mice independent of maltase-glucoamylase genotype or mucosal maltase activity. (2) This experiment demonstrates that a soluble maltase activity is secreted in mouse mother’s milk which enables suckling pup starch digestion well before brush border enzyme development. (3) This experiment with 13 C-α-limit dextrins needs to be repeated in human breast fed infants.
ISSN:2194-7791
2194-7791
DOI:10.1186/s40348-016-0032-z