Cargando…
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 befor...
Autores principales: | , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4735098/ https://www.ncbi.nlm.nih.gov/pubmed/26830109 http://dx.doi.org/10.1186/s40348-016-0032-z |
_version_ | 1782413016916033536 |
---|---|
author | 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. |
author_facet | 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. |
author_sort | Nichols, B. L. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4735098 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-47350982016-02-12 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. Mol Cell Pediatr Mini Review 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. Springer Berlin Heidelberg 2016-02-01 /pmc/articles/PMC4735098/ /pubmed/26830109 http://dx.doi.org/10.1186/s40348-016-0032-z Text en © Nichols et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Mini Review 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. Milk glucosidase activity enables suckled pup starch digestion |
title | Milk glucosidase activity enables suckled pup starch digestion |
title_full | Milk glucosidase activity enables suckled pup starch digestion |
title_fullStr | Milk glucosidase activity enables suckled pup starch digestion |
title_full_unstemmed | Milk glucosidase activity enables suckled pup starch digestion |
title_short | Milk glucosidase activity enables suckled pup starch digestion |
title_sort | milk glucosidase activity enables suckled pup starch digestion |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4735098/ https://www.ncbi.nlm.nih.gov/pubmed/26830109 http://dx.doi.org/10.1186/s40348-016-0032-z |
work_keys_str_mv | AT nicholsbl milkglucosidaseactivityenablessuckledpupstarchdigestion AT diazsotomayorm milkglucosidaseactivityenablessuckledpupstarchdigestion AT averyse milkglucosidaseactivityenablessuckledpupstarchdigestion AT chackosk milkglucosidaseactivityenablessuckledpupstarchdigestion AT hadselldl milkglucosidaseactivityenablessuckledpupstarchdigestion AT bakerss milkglucosidaseactivityenablessuckledpupstarchdigestion AT hamakerbr milkglucosidaseactivityenablessuckledpupstarchdigestion AT yanlk milkglucosidaseactivityenablessuckledpupstarchdigestion AT linhm milkglucosidaseactivityenablessuckledpupstarchdigestion AT quezadacalvillor milkglucosidaseactivityenablessuckledpupstarchdigestion |