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Milk glucosidase activity enables suckled pup starch digestion.
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.
Affiliation
  • Nichols BL; Children's Nutrition Research Center, Baylor College of Medicine and Texas Children's Hospital, Houston, TX, USA. blnjr@sbcglobal.net.
  • Diaz-Sotomayor M; Children's Nutrition Research Center, Baylor College of Medicine and Texas Children's Hospital, Houston, TX, USA. marlinda76@hotmail.com.
  • Avery SE; Children's Nutrition Research Center, Baylor College of Medicine and Texas Children's Hospital, Houston, TX, USA. seavery@texaschildrens.org.
  • Chacko SK; Children's Nutrition Research Center, Baylor College of Medicine and Texas Children's Hospital, Houston, TX, USA. schacko@bcm.edu.
  • Hadsell DL; Children's Nutrition Research Center, Baylor College of Medicine and Texas Children's Hospital, Houston, TX, USA. dhadsell@bcm.edu.
  • Baker SS; Department of Pediatrics, State University of New York, Buffalo, NY, USA. sbaker@upa.chob.edu.
  • Hamaker BR; Whistler Center for Carbohydrate Research, Purdue University, West Lafayette, IN, USA. hamakerb@purdue.edu.
  • Yan LK; Whistler Center for Carbohydrate Research, Purdue University, West Lafayette, IN, USA. like.yan.2011@gmail.com.
  • Lin HM; Whistler Center for Carbohydrate Research, Purdue University, West Lafayette, IN, USA. amylin@uidaho.edu.
  • Quezada-Calvillo R; University of Idaho, Moscow, ID, USA. amylin@uidaho.edu.
Mol Cell Pediatr ; 3(1): 4, 2016 Dec.
Article in En | MEDLINE | ID: mdl-26830109
ABSTRACT
UNLABELLED 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.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Mol Cell Pediatr Year: 2016 Document type: Article Affiliation country: Estados Unidos

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Mol Cell Pediatr Year: 2016 Document type: Article Affiliation country: Estados Unidos