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Molecular and Integrative Physiology of Intestinal Peptide Transport
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| Zeitschriftentitel: | Annual Review of Physiology |
|---|---|
| Personen und Körperschaften: | |
| In: | Annual Review of Physiology, 66, 2004, 1, S. 361-384 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Annual Reviews
|
| Schlagwörter: |
| author_facet |
Daniel, Hannelore Daniel, Hannelore |
|---|---|
| author |
Daniel, Hannelore |
| spellingShingle |
Daniel, Hannelore Annual Review of Physiology Molecular and Integrative Physiology of Intestinal Peptide Transport Physiology |
| author_sort |
daniel, hannelore |
| spelling |
Daniel, Hannelore 0066-4278 1545-1585 Annual Reviews Physiology http://dx.doi.org/10.1146/annurev.physiol.66.032102.144149 <jats:p> ▪ Abstract Intestinal protein digestion generates a huge variety and quantity of short chain peptides that are absorbed into intestinal epithelial cells by the PEPT1 transporter in the apical membrane of enterocytes. PEPT1 operates as an electrogenic proton/peptide symporter with the ability to transport essentially every possible di- and tripeptide. Transport is enantio-selective and involves a variable proton-to-substrate stoichiometry for uptake of neutral and mono- or polyvalently charged peptides. Neither free amino acids nor peptides containing four or more amino acids are accepted as substrates. The structural similarity of a variety of drugs with the basic structure of di- or tripeptides explains the transport of aminocephalosporins and aminopenicillins, selected angiotensin-converting inhibitors, and amino acid–conjugated nucleoside-based antiviral agents by PEPT1. The high transport capacity of PEPT1 allows fast and efficient intestinal uptake of the drugs but also of amino acid nitrogen even in states of impaired mucosal functions. Transcriptional and post-transcriptional regulation of PEPT1 occurs in response to alterations in the nutritional status and in disease states, suggesting a prime role of this transporter in amino acid absorption. </jats:p> Molecular and Integrative Physiology of Intestinal Peptide Transport Annual Review of Physiology |
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Annual Reviews, 2004 |
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Annual Reviews, 2004 |
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0066-4278 1545-1585 |
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2004 |
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Annual Reviews |
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Annual Review of Physiology |
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| title |
Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_unstemmed |
Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_full |
Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_fullStr |
Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_full_unstemmed |
Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_short |
Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_sort |
molecular and integrative physiology of intestinal peptide transport |
| topic |
Physiology |
| url |
http://dx.doi.org/10.1146/annurev.physiol.66.032102.144149 |
| publishDate |
2004 |
| physical |
361-384 |
| description |
<jats:p> ▪ Abstract Intestinal protein digestion generates a huge variety and quantity of short chain peptides that are absorbed into intestinal epithelial cells by the PEPT1 transporter in the apical membrane of enterocytes. PEPT1 operates as an electrogenic proton/peptide symporter with the ability to transport essentially every possible di- and tripeptide. Transport is enantio-selective and involves a variable proton-to-substrate stoichiometry for uptake of neutral and mono- or polyvalently charged peptides. Neither free amino acids nor peptides containing four or more amino acids are accepted as substrates. The structural similarity of a variety of drugs with the basic structure of di- or tripeptides explains the transport of aminocephalosporins and aminopenicillins, selected angiotensin-converting inhibitors, and amino acid–conjugated nucleoside-based antiviral agents by PEPT1. The high transport capacity of PEPT1 allows fast and efficient intestinal uptake of the drugs but also of amino acid nitrogen even in states of impaired mucosal functions. Transcriptional and post-transcriptional regulation of PEPT1 occurs in response to alterations in the nutritional status and in disease states, suggesting a prime role of this transporter in amino acid absorption. </jats:p> |
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| container_title | Annual Review of Physiology |
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| description | <jats:p> ▪ Abstract Intestinal protein digestion generates a huge variety and quantity of short chain peptides that are absorbed into intestinal epithelial cells by the PEPT1 transporter in the apical membrane of enterocytes. PEPT1 operates as an electrogenic proton/peptide symporter with the ability to transport essentially every possible di- and tripeptide. Transport is enantio-selective and involves a variable proton-to-substrate stoichiometry for uptake of neutral and mono- or polyvalently charged peptides. Neither free amino acids nor peptides containing four or more amino acids are accepted as substrates. The structural similarity of a variety of drugs with the basic structure of di- or tripeptides explains the transport of aminocephalosporins and aminopenicillins, selected angiotensin-converting inhibitors, and amino acid–conjugated nucleoside-based antiviral agents by PEPT1. The high transport capacity of PEPT1 allows fast and efficient intestinal uptake of the drugs but also of amino acid nitrogen even in states of impaired mucosal functions. Transcriptional and post-transcriptional regulation of PEPT1 occurs in response to alterations in the nutritional status and in disease states, suggesting a prime role of this transporter in amino acid absorption. </jats:p> |
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| imprint_str_mv | Annual Reviews, 2004 |
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| physical | 361-384 |
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| series | Annual Review of Physiology |
| source_id | 49 |
| spelling | Daniel, Hannelore 0066-4278 1545-1585 Annual Reviews Physiology http://dx.doi.org/10.1146/annurev.physiol.66.032102.144149 <jats:p> ▪ Abstract Intestinal protein digestion generates a huge variety and quantity of short chain peptides that are absorbed into intestinal epithelial cells by the PEPT1 transporter in the apical membrane of enterocytes. PEPT1 operates as an electrogenic proton/peptide symporter with the ability to transport essentially every possible di- and tripeptide. Transport is enantio-selective and involves a variable proton-to-substrate stoichiometry for uptake of neutral and mono- or polyvalently charged peptides. Neither free amino acids nor peptides containing four or more amino acids are accepted as substrates. The structural similarity of a variety of drugs with the basic structure of di- or tripeptides explains the transport of aminocephalosporins and aminopenicillins, selected angiotensin-converting inhibitors, and amino acid–conjugated nucleoside-based antiviral agents by PEPT1. The high transport capacity of PEPT1 allows fast and efficient intestinal uptake of the drugs but also of amino acid nitrogen even in states of impaired mucosal functions. Transcriptional and post-transcriptional regulation of PEPT1 occurs in response to alterations in the nutritional status and in disease states, suggesting a prime role of this transporter in amino acid absorption. </jats:p> Molecular and Integrative Physiology of Intestinal Peptide Transport Annual Review of Physiology |
| spellingShingle | Daniel, Hannelore, Annual Review of Physiology, Molecular and Integrative Physiology of Intestinal Peptide Transport, Physiology |
| title | Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_full | Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_fullStr | Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_full_unstemmed | Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_short | Molecular and Integrative Physiology of Intestinal Peptide Transport |
| title_sort | molecular and integrative physiology of intestinal peptide transport |
| title_unstemmed | Molecular and Integrative Physiology of Intestinal Peptide Transport |
| topic | Physiology |
| url | http://dx.doi.org/10.1146/annurev.physiol.66.032102.144149 |