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Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein
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| Zeitschriftentitel: | American Journal of Physiology-Endocrinology and Metabolism |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | American Journal of Physiology-Endocrinology and Metabolism, 282, 2002, 5, S. E1172-E1179 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
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| Schlagwörter: |
| author_facet |
Groneberg, David A. Döring, Frank Theis, Stephan Nickolaus, Monika Fischer, Axel Daniel, Hannelore Groneberg, David A. Döring, Frank Theis, Stephan Nickolaus, Monika Fischer, Axel Daniel, Hannelore |
|---|---|
| author |
Groneberg, David A. Döring, Frank Theis, Stephan Nickolaus, Monika Fischer, Axel Daniel, Hannelore |
| spellingShingle |
Groneberg, David A. Döring, Frank Theis, Stephan Nickolaus, Monika Fischer, Axel Daniel, Hannelore American Journal of Physiology-Endocrinology and Metabolism Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein Physiology (medical) Physiology Endocrinology, Diabetes and Metabolism |
| author_sort |
groneberg, david a. |
| spelling |
Groneberg, David A. Döring, Frank Theis, Stephan Nickolaus, Monika Fischer, Axel Daniel, Hannelore 0193-1849 1522-1555 American Physiological Society Physiology (medical) Physiology Endocrinology, Diabetes and Metabolism http://dx.doi.org/10.1152/ajpendo.00381.2001 <jats:p>The lactating mammary gland utilizes free plasma amino acids as well as those derived by hydrolysis from circulating short-chain peptides for protein synthesis. Apart from the major route of amino acid nitrogen delivery to the gland by the various transporters for free amino acids, it has been suggested that dipeptides may also be taken up in intact form to serve as a source of amino acids. The identification of peptide transporters in the mammary gland may therefore provide new insights into protein metabolism and secretion by the gland. The expression and distribution of the high-affinity type proton-coupled peptide transporter PEPT2 were investigated in rat lactating mammary gland as well as in human epithelial cells derived from breast milk. By use of RT-PCR, PEPT2 mRNA was detected in rat mammary gland extracts and human milk epithelial cells. The expression pattern of PEPT2 mRNA revealed a localization in epithelial cells of ducts and glands by nonisotopic high resolution in situ hybridization. In addition, immunohistochemistry was carried out and showed transporter immunoreactivity in the same epithelial cells of the glands and ducts. In addition, two-electrode voltage clamp recordings using PEPT2-expressing Xenopus laevis oocytes demonstrated positive inward currents induced by selected dipeptides that may play a role in aminonitrogen handling in mammalian mammary gland. Taken together, these data suggest that PEPT2 is expressed in mammary gland epithelia, in which it may contribute to the reuptake of short-chain peptides derived from hydrolysis of milk proteins secreted into the lumen. Whereas PEPT2 also transports a variety of drugs, such as selected β-lactams, angiotensin-converting enzyme inhibitors, and antiviral and anticancer metabolites, their efficient reabsorption via PEPT2 may reduce the burden of xenobiotics in milk.</jats:p> Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein American Journal of Physiology-Endocrinology and Metabolism |
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| title |
Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_unstemmed |
Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_full |
Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_fullStr |
Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_full_unstemmed |
Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_short |
Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_sort |
peptide transport in the mammary gland: expression and distribution of pept2 mrna and protein |
| topic |
Physiology (medical) Physiology Endocrinology, Diabetes and Metabolism |
| url |
http://dx.doi.org/10.1152/ajpendo.00381.2001 |
| publishDate |
2002 |
| physical |
E1172-E1179 |
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<jats:p>The lactating mammary gland utilizes free plasma amino acids as well as those derived by hydrolysis from circulating short-chain peptides for protein synthesis. Apart from the major route of amino acid nitrogen delivery to the gland by the various transporters for free amino acids, it has been suggested that dipeptides may also be taken up in intact form to serve as a source of amino acids. The identification of peptide transporters in the mammary gland may therefore provide new insights into protein metabolism and secretion by the gland. The expression and distribution of the high-affinity type proton-coupled peptide transporter PEPT2 were investigated in rat lactating mammary gland as well as in human epithelial cells derived from breast milk. By use of RT-PCR, PEPT2 mRNA was detected in rat mammary gland extracts and human milk epithelial cells. The expression pattern of PEPT2 mRNA revealed a localization in epithelial cells of ducts and glands by nonisotopic high resolution in situ hybridization. In addition, immunohistochemistry was carried out and showed transporter immunoreactivity in the same epithelial cells of the glands and ducts. In addition, two-electrode voltage clamp recordings using PEPT2-expressing Xenopus laevis oocytes demonstrated positive inward currents induced by selected dipeptides that may play a role in aminonitrogen handling in mammalian mammary gland. Taken together, these data suggest that PEPT2 is expressed in mammary gland epithelia, in which it may contribute to the reuptake of short-chain peptides derived from hydrolysis of milk proteins secreted into the lumen. Whereas PEPT2 also transports a variety of drugs, such as selected β-lactams, angiotensin-converting enzyme inhibitors, and antiviral and anticancer metabolites, their efficient reabsorption via PEPT2 may reduce the burden of xenobiotics in milk.</jats:p> |
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| author | Groneberg, David A., Döring, Frank, Theis, Stephan, Nickolaus, Monika, Fischer, Axel, Daniel, Hannelore |
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| description | <jats:p>The lactating mammary gland utilizes free plasma amino acids as well as those derived by hydrolysis from circulating short-chain peptides for protein synthesis. Apart from the major route of amino acid nitrogen delivery to the gland by the various transporters for free amino acids, it has been suggested that dipeptides may also be taken up in intact form to serve as a source of amino acids. The identification of peptide transporters in the mammary gland may therefore provide new insights into protein metabolism and secretion by the gland. The expression and distribution of the high-affinity type proton-coupled peptide transporter PEPT2 were investigated in rat lactating mammary gland as well as in human epithelial cells derived from breast milk. By use of RT-PCR, PEPT2 mRNA was detected in rat mammary gland extracts and human milk epithelial cells. The expression pattern of PEPT2 mRNA revealed a localization in epithelial cells of ducts and glands by nonisotopic high resolution in situ hybridization. In addition, immunohistochemistry was carried out and showed transporter immunoreactivity in the same epithelial cells of the glands and ducts. In addition, two-electrode voltage clamp recordings using PEPT2-expressing Xenopus laevis oocytes demonstrated positive inward currents induced by selected dipeptides that may play a role in aminonitrogen handling in mammalian mammary gland. Taken together, these data suggest that PEPT2 is expressed in mammary gland epithelia, in which it may contribute to the reuptake of short-chain peptides derived from hydrolysis of milk proteins secreted into the lumen. Whereas PEPT2 also transports a variety of drugs, such as selected β-lactams, angiotensin-converting enzyme inhibitors, and antiviral and anticancer metabolites, their efficient reabsorption via PEPT2 may reduce the burden of xenobiotics in milk.</jats:p> |
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| spelling | Groneberg, David A. Döring, Frank Theis, Stephan Nickolaus, Monika Fischer, Axel Daniel, Hannelore 0193-1849 1522-1555 American Physiological Society Physiology (medical) Physiology Endocrinology, Diabetes and Metabolism http://dx.doi.org/10.1152/ajpendo.00381.2001 <jats:p>The lactating mammary gland utilizes free plasma amino acids as well as those derived by hydrolysis from circulating short-chain peptides for protein synthesis. Apart from the major route of amino acid nitrogen delivery to the gland by the various transporters for free amino acids, it has been suggested that dipeptides may also be taken up in intact form to serve as a source of amino acids. The identification of peptide transporters in the mammary gland may therefore provide new insights into protein metabolism and secretion by the gland. The expression and distribution of the high-affinity type proton-coupled peptide transporter PEPT2 were investigated in rat lactating mammary gland as well as in human epithelial cells derived from breast milk. By use of RT-PCR, PEPT2 mRNA was detected in rat mammary gland extracts and human milk epithelial cells. The expression pattern of PEPT2 mRNA revealed a localization in epithelial cells of ducts and glands by nonisotopic high resolution in situ hybridization. In addition, immunohistochemistry was carried out and showed transporter immunoreactivity in the same epithelial cells of the glands and ducts. In addition, two-electrode voltage clamp recordings using PEPT2-expressing Xenopus laevis oocytes demonstrated positive inward currents induced by selected dipeptides that may play a role in aminonitrogen handling in mammalian mammary gland. Taken together, these data suggest that PEPT2 is expressed in mammary gland epithelia, in which it may contribute to the reuptake of short-chain peptides derived from hydrolysis of milk proteins secreted into the lumen. Whereas PEPT2 also transports a variety of drugs, such as selected β-lactams, angiotensin-converting enzyme inhibitors, and antiviral and anticancer metabolites, their efficient reabsorption via PEPT2 may reduce the burden of xenobiotics in milk.</jats:p> Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein American Journal of Physiology-Endocrinology and Metabolism |
| spellingShingle | Groneberg, David A., Döring, Frank, Theis, Stephan, Nickolaus, Monika, Fischer, Axel, Daniel, Hannelore, American Journal of Physiology-Endocrinology and Metabolism, Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein, Physiology (medical), Physiology, Endocrinology, Diabetes and Metabolism |
| title | Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_full | Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_fullStr | Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_full_unstemmed | Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_short | Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| title_sort | peptide transport in the mammary gland: expression and distribution of pept2 mrna and protein |
| title_unstemmed | Peptide transport in the mammary gland: expression and distribution of PEPT2 mRNA and protein |
| topic | Physiology (medical), Physiology, Endocrinology, Diabetes and Metabolism |
| url | http://dx.doi.org/10.1152/ajpendo.00381.2001 |