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Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1
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| Zeitschriftentitel: | American Journal of Physiology-Gastrointestinal and Liver Physiology |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | American Journal of Physiology-Gastrointestinal and Liver Physiology, 301, 2011, 1, S. G128-G137 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
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| Schlagwörter: |
| author_facet |
Nässl, Anna-Maria Rubio-Aliaga, Isabel Fenselau, Henning Marth, Mena Katharina Kottra, Gabor Daniel, Hannelore Nässl, Anna-Maria Rubio-Aliaga, Isabel Fenselau, Henning Marth, Mena Katharina Kottra, Gabor Daniel, Hannelore |
|---|---|
| author |
Nässl, Anna-Maria Rubio-Aliaga, Isabel Fenselau, Henning Marth, Mena Katharina Kottra, Gabor Daniel, Hannelore |
| spellingShingle |
Nässl, Anna-Maria Rubio-Aliaga, Isabel Fenselau, Henning Marth, Mena Katharina Kottra, Gabor Daniel, Hannelore American Journal of Physiology-Gastrointestinal and Liver Physiology Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 Physiology (medical) Gastroenterology Hepatology Physiology |
| author_sort |
nässl, anna-maria |
| spelling |
Nässl, Anna-Maria Rubio-Aliaga, Isabel Fenselau, Henning Marth, Mena Katharina Kottra, Gabor Daniel, Hannelore 0193-1857 1522-1547 American Physiological Society Physiology (medical) Gastroenterology Hepatology Physiology http://dx.doi.org/10.1152/ajpgi.00017.2011 <jats:p>The intestinal peptide transporter PEPT1 mediates the uptake of di- and tripeptides derived from dietary protein breakdown into epithelial cells. Whereas the transporter appears to be essential to compensate for the reduced amino acid delivery in patients with mutations in amino acid transporter genes, such as in cystinuria or Hartnup disease, its physiological role in overall amino acid absorption is still not known. To assess the quantitative importance of PEPT1 in overall amino acid absorption and metabolism, PEPT1-deficient mice were studied by using brush border membrane vesicles, everted gut sacs, and Ussing chambers, as well as by transcriptome and proteome analysis of intestinal tissue samples. Neither gene expression nor proteome profiling nor functional analysis revealed evidence for any compensatory changes in the levels and/or function of transporters for free amino acids in the intestine. However, most plasma amino acid levels were increased in Pept1<jats:sup>−/−</jats:sup>compared with Pept1<jats:sup>+/+</jats:sup>animals, suggesting that amino acid handling is altered. Plasma appearance rates of<jats:sup>15</jats:sup>N-labeled amino acids determined after intragastric administration of a low dose of protein remained unchanged, whereas administration of a large protein load via gavage revealed marked differences in plasma appearance of selected amino acids. PEPT1 seems, therefore, important for overall amino acid absorption only after high dietary protein intake when amino acid transport processes are saturated and PEPT1 can provide additional absorption capacity. Since renal amino acid excretion remained unchanged, elevated basal concentrations of plasma amino acids in PEPT1-deficient animals seem to arise mainly from alterations in hepatic amino acid metabolism.</jats:p> Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 American Journal of Physiology-Gastrointestinal and Liver Physiology |
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| title |
Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_unstemmed |
Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_full |
Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_fullStr |
Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_full_unstemmed |
Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_short |
Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_sort |
amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter pept1 |
| topic |
Physiology (medical) Gastroenterology Hepatology Physiology |
| url |
http://dx.doi.org/10.1152/ajpgi.00017.2011 |
| publishDate |
2011 |
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G128-G137 |
| description |
<jats:p>The intestinal peptide transporter PEPT1 mediates the uptake of di- and tripeptides derived from dietary protein breakdown into epithelial cells. Whereas the transporter appears to be essential to compensate for the reduced amino acid delivery in patients with mutations in amino acid transporter genes, such as in cystinuria or Hartnup disease, its physiological role in overall amino acid absorption is still not known. To assess the quantitative importance of PEPT1 in overall amino acid absorption and metabolism, PEPT1-deficient mice were studied by using brush border membrane vesicles, everted gut sacs, and Ussing chambers, as well as by transcriptome and proteome analysis of intestinal tissue samples. Neither gene expression nor proteome profiling nor functional analysis revealed evidence for any compensatory changes in the levels and/or function of transporters for free amino acids in the intestine. However, most plasma amino acid levels were increased in Pept1<jats:sup>−/−</jats:sup>compared with Pept1<jats:sup>+/+</jats:sup>animals, suggesting that amino acid handling is altered. Plasma appearance rates of<jats:sup>15</jats:sup>N-labeled amino acids determined after intragastric administration of a low dose of protein remained unchanged, whereas administration of a large protein load via gavage revealed marked differences in plasma appearance of selected amino acids. PEPT1 seems, therefore, important for overall amino acid absorption only after high dietary protein intake when amino acid transport processes are saturated and PEPT1 can provide additional absorption capacity. Since renal amino acid excretion remained unchanged, elevated basal concentrations of plasma amino acids in PEPT1-deficient animals seem to arise mainly from alterations in hepatic amino acid metabolism.</jats:p> |
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| author | Nässl, Anna-Maria, Rubio-Aliaga, Isabel, Fenselau, Henning, Marth, Mena Katharina, Kottra, Gabor, Daniel, Hannelore |
| author_facet | Nässl, Anna-Maria, Rubio-Aliaga, Isabel, Fenselau, Henning, Marth, Mena Katharina, Kottra, Gabor, Daniel, Hannelore, Nässl, Anna-Maria, Rubio-Aliaga, Isabel, Fenselau, Henning, Marth, Mena Katharina, Kottra, Gabor, Daniel, Hannelore |
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| description | <jats:p>The intestinal peptide transporter PEPT1 mediates the uptake of di- and tripeptides derived from dietary protein breakdown into epithelial cells. Whereas the transporter appears to be essential to compensate for the reduced amino acid delivery in patients with mutations in amino acid transporter genes, such as in cystinuria or Hartnup disease, its physiological role in overall amino acid absorption is still not known. To assess the quantitative importance of PEPT1 in overall amino acid absorption and metabolism, PEPT1-deficient mice were studied by using brush border membrane vesicles, everted gut sacs, and Ussing chambers, as well as by transcriptome and proteome analysis of intestinal tissue samples. Neither gene expression nor proteome profiling nor functional analysis revealed evidence for any compensatory changes in the levels and/or function of transporters for free amino acids in the intestine. However, most plasma amino acid levels were increased in Pept1<jats:sup>−/−</jats:sup>compared with Pept1<jats:sup>+/+</jats:sup>animals, suggesting that amino acid handling is altered. Plasma appearance rates of<jats:sup>15</jats:sup>N-labeled amino acids determined after intragastric administration of a low dose of protein remained unchanged, whereas administration of a large protein load via gavage revealed marked differences in plasma appearance of selected amino acids. PEPT1 seems, therefore, important for overall amino acid absorption only after high dietary protein intake when amino acid transport processes are saturated and PEPT1 can provide additional absorption capacity. Since renal amino acid excretion remained unchanged, elevated basal concentrations of plasma amino acids in PEPT1-deficient animals seem to arise mainly from alterations in hepatic amino acid metabolism.</jats:p> |
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| spelling | Nässl, Anna-Maria Rubio-Aliaga, Isabel Fenselau, Henning Marth, Mena Katharina Kottra, Gabor Daniel, Hannelore 0193-1857 1522-1547 American Physiological Society Physiology (medical) Gastroenterology Hepatology Physiology http://dx.doi.org/10.1152/ajpgi.00017.2011 <jats:p>The intestinal peptide transporter PEPT1 mediates the uptake of di- and tripeptides derived from dietary protein breakdown into epithelial cells. Whereas the transporter appears to be essential to compensate for the reduced amino acid delivery in patients with mutations in amino acid transporter genes, such as in cystinuria or Hartnup disease, its physiological role in overall amino acid absorption is still not known. To assess the quantitative importance of PEPT1 in overall amino acid absorption and metabolism, PEPT1-deficient mice were studied by using brush border membrane vesicles, everted gut sacs, and Ussing chambers, as well as by transcriptome and proteome analysis of intestinal tissue samples. Neither gene expression nor proteome profiling nor functional analysis revealed evidence for any compensatory changes in the levels and/or function of transporters for free amino acids in the intestine. However, most plasma amino acid levels were increased in Pept1<jats:sup>−/−</jats:sup>compared with Pept1<jats:sup>+/+</jats:sup>animals, suggesting that amino acid handling is altered. Plasma appearance rates of<jats:sup>15</jats:sup>N-labeled amino acids determined after intragastric administration of a low dose of protein remained unchanged, whereas administration of a large protein load via gavage revealed marked differences in plasma appearance of selected amino acids. PEPT1 seems, therefore, important for overall amino acid absorption only after high dietary protein intake when amino acid transport processes are saturated and PEPT1 can provide additional absorption capacity. Since renal amino acid excretion remained unchanged, elevated basal concentrations of plasma amino acids in PEPT1-deficient animals seem to arise mainly from alterations in hepatic amino acid metabolism.</jats:p> Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 American Journal of Physiology-Gastrointestinal and Liver Physiology |
| spellingShingle | Nässl, Anna-Maria, Rubio-Aliaga, Isabel, Fenselau, Henning, Marth, Mena Katharina, Kottra, Gabor, Daniel, Hannelore, American Journal of Physiology-Gastrointestinal and Liver Physiology, Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1, Physiology (medical), Gastroenterology, Hepatology, Physiology |
| title | Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_full | Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_fullStr | Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_full_unstemmed | Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_short | Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| title_sort | amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter pept1 |
| title_unstemmed | Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 |
| topic | Physiology (medical), Gastroenterology, Hepatology, Physiology |
| url | http://dx.doi.org/10.1152/ajpgi.00017.2011 |