Eintrag weiter verarbeiten
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2
Gespeichert in:
| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | European Journal of Biochemistry, 271, 2004, 16, S. 3340-3347 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Foltz, Martin Oechsler, Carmen Boll, Michael Kottra, Gabor Daniel, Hannelore Foltz, Martin Oechsler, Carmen Boll, Michael Kottra, Gabor Daniel, Hannelore |
|---|---|
| author |
Foltz, Martin Oechsler, Carmen Boll, Michael Kottra, Gabor Daniel, Hannelore |
| spellingShingle |
Foltz, Martin Oechsler, Carmen Boll, Michael Kottra, Gabor Daniel, Hannelore European Journal of Biochemistry Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 Biochemistry |
| author_sort |
foltz, martin |
| spelling |
Foltz, Martin Oechsler, Carmen Boll, Michael Kottra, Gabor Daniel, Hannelore 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.2004.04268.x <jats:p>The PAT2 transporter has been shown to act as an electrogenic proton/amino acid symporter. The PAT2 cDNA has been cloned from various human, mouse and rat tissues and belongs to a group of four genes (<jats:italic>pat1</jats:italic> to <jats:italic>pat4</jats:italic>) with PAT3 and PAT4 still resembling orphan transporters. The first immunolocalization studies demonstrated that the PAT2 protein is found in the murine central nervous system in neuronal cells with a proposed role in the intra and/or intercellular amino acid transport. Here we provide a detailed analysis of the transport mode and substrate specificity of the murine PAT2 transporter after expression in <jats:italic>Xenopus laevis</jats:italic> oocytes, by electrophysiological techniques and flux studies. The structural requirements to the PAT2 substrates – when considering both low and high affinity type substrates – are similar to those reported for the PAT1 protein with the essential features of a free carboxy group and a small side chain. For high affinity binding, however, PAT2 requires the amino group to be located in an α‐position, tolerates only one methyl function attached to the amino group and is highly selective for the <jats:sc>l</jats:sc>‐enantiomers. Electrophysiological analysis revealed pronounced effects of membrane potential on proton binding affinity, but substrate affinities and maximal transport currents only modestly respond to changes in membrane voltage. Whereas substrate affinity is dependent on extracellular pH, proton binding affinity to PAT2 is substrate‐independent, favouring a sequential binding of proton followed by substrate. Maximal transport currents are substrate‐dependent which suggests that the translocation of the loaded carrier to the internal side is the rate‐limiting step.</jats:p> Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 European Journal of Biochemistry |
| doi_str_mv |
10.1111/j.1432-1033.2004.04268.x |
| facet_avail |
Online Free |
| finc_class_facet |
Chemie und Pharmazie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4yMDA0LjA0MjY4Lng |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4yMDA0LjA0MjY4Lng |
| institution |
DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 |
| imprint |
Wiley, 2004 |
| imprint_str_mv |
Wiley, 2004 |
| issn |
0014-2956 1432-1033 |
| issn_str_mv |
0014-2956 1432-1033 |
| language |
English |
| mega_collection |
Wiley (CrossRef) |
| match_str |
foltz2004substratespecificityandtransportmodeoftheprotondependentaminoacidtransportermpat2 |
| publishDateSort |
2004 |
| publisher |
Wiley |
| recordtype |
ai |
| record_format |
ai |
| series |
European Journal of Biochemistry |
| source_id |
49 |
| title |
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_unstemmed |
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_full |
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_fullStr |
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_full_unstemmed |
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_short |
Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_sort |
substrate specificity and transport mode of the proton‐dependent amino acid transporter mpat2 |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.2004.04268.x |
| publishDate |
2004 |
| physical |
3340-3347 |
| description |
<jats:p>The PAT2 transporter has been shown to act as an electrogenic proton/amino acid symporter. The PAT2 cDNA has been cloned from various human, mouse and rat tissues and belongs to a group of four genes (<jats:italic>pat1</jats:italic> to <jats:italic>pat4</jats:italic>) with PAT3 and PAT4 still resembling orphan transporters. The first immunolocalization studies demonstrated that the PAT2 protein is found in the murine central nervous system in neuronal cells with a proposed role in the intra and/or intercellular amino acid transport. Here we provide a detailed analysis of the transport mode and substrate specificity of the murine PAT2 transporter after expression in <jats:italic>Xenopus laevis</jats:italic> oocytes, by electrophysiological techniques and flux studies. The structural requirements to the PAT2 substrates – when considering both low and high affinity type substrates – are similar to those reported for the PAT1 protein with the essential features of a free carboxy group and a small side chain. For high affinity binding, however, PAT2 requires the amino group to be located in an α‐position, tolerates only one methyl function attached to the amino group and is highly selective for the <jats:sc>l</jats:sc>‐enantiomers. Electrophysiological analysis revealed pronounced effects of membrane potential on proton binding affinity, but substrate affinities and maximal transport currents only modestly respond to changes in membrane voltage. Whereas substrate affinity is dependent on extracellular pH, proton binding affinity to PAT2 is substrate‐independent, favouring a sequential binding of proton followed by substrate. Maximal transport currents are substrate‐dependent which suggests that the translocation of the loaded carrier to the internal side is the rate‐limiting step.</jats:p> |
| container_issue |
16 |
| container_start_page |
3340 |
| container_title |
European Journal of Biochemistry |
| container_volume |
271 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792337028358078471 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T15:09:49.824Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Substrate+specificity+and+transport+mode+of+the+proton%E2%80%90dependent+amino+acid+transporter+mPAT2&rft.date=2004-08-01&genre=article&issn=1432-1033&volume=271&issue=16&spage=3340&epage=3347&pages=3340-3347&jtitle=European+Journal+of+Biochemistry&atitle=Substrate+specificity+and+transport+mode+of+the+proton%E2%80%90dependent+amino+acid+transporter+mPAT2&aulast=Daniel&aufirst=Hannelore&rft_id=info%3Adoi%2F10.1111%2Fj.1432-1033.2004.04268.x&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792337028358078471 |
| author | Foltz, Martin, Oechsler, Carmen, Boll, Michael, Kottra, Gabor, Daniel, Hannelore |
| author_facet | Foltz, Martin, Oechsler, Carmen, Boll, Michael, Kottra, Gabor, Daniel, Hannelore, Foltz, Martin, Oechsler, Carmen, Boll, Michael, Kottra, Gabor, Daniel, Hannelore |
| author_sort | foltz, martin |
| container_issue | 16 |
| container_start_page | 3340 |
| container_title | European Journal of Biochemistry |
| container_volume | 271 |
| description | <jats:p>The PAT2 transporter has been shown to act as an electrogenic proton/amino acid symporter. The PAT2 cDNA has been cloned from various human, mouse and rat tissues and belongs to a group of four genes (<jats:italic>pat1</jats:italic> to <jats:italic>pat4</jats:italic>) with PAT3 and PAT4 still resembling orphan transporters. The first immunolocalization studies demonstrated that the PAT2 protein is found in the murine central nervous system in neuronal cells with a proposed role in the intra and/or intercellular amino acid transport. Here we provide a detailed analysis of the transport mode and substrate specificity of the murine PAT2 transporter after expression in <jats:italic>Xenopus laevis</jats:italic> oocytes, by electrophysiological techniques and flux studies. The structural requirements to the PAT2 substrates – when considering both low and high affinity type substrates – are similar to those reported for the PAT1 protein with the essential features of a free carboxy group and a small side chain. For high affinity binding, however, PAT2 requires the amino group to be located in an α‐position, tolerates only one methyl function attached to the amino group and is highly selective for the <jats:sc>l</jats:sc>‐enantiomers. Electrophysiological analysis revealed pronounced effects of membrane potential on proton binding affinity, but substrate affinities and maximal transport currents only modestly respond to changes in membrane voltage. Whereas substrate affinity is dependent on extracellular pH, proton binding affinity to PAT2 is substrate‐independent, favouring a sequential binding of proton followed by substrate. Maximal transport currents are substrate‐dependent which suggests that the translocation of the loaded carrier to the internal side is the rate‐limiting step.</jats:p> |
| doi_str_mv | 10.1111/j.1432-1033.2004.04268.x |
| facet_avail | Online, Free |
| finc_class_facet | Chemie und Pharmazie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4yMDA0LjA0MjY4Lng |
| imprint | Wiley, 2004 |
| imprint_str_mv | Wiley, 2004 |
| institution | DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
| issn | 0014-2956, 1432-1033 |
| issn_str_mv | 0014-2956, 1432-1033 |
| language | English |
| last_indexed | 2024-03-01T15:09:49.824Z |
| match_str | foltz2004substratespecificityandtransportmodeoftheprotondependentaminoacidtransportermpat2 |
| mega_collection | Wiley (CrossRef) |
| physical | 3340-3347 |
| publishDate | 2004 |
| publishDateSort | 2004 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | Foltz, Martin Oechsler, Carmen Boll, Michael Kottra, Gabor Daniel, Hannelore 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.2004.04268.x <jats:p>The PAT2 transporter has been shown to act as an electrogenic proton/amino acid symporter. The PAT2 cDNA has been cloned from various human, mouse and rat tissues and belongs to a group of four genes (<jats:italic>pat1</jats:italic> to <jats:italic>pat4</jats:italic>) with PAT3 and PAT4 still resembling orphan transporters. The first immunolocalization studies demonstrated that the PAT2 protein is found in the murine central nervous system in neuronal cells with a proposed role in the intra and/or intercellular amino acid transport. Here we provide a detailed analysis of the transport mode and substrate specificity of the murine PAT2 transporter after expression in <jats:italic>Xenopus laevis</jats:italic> oocytes, by electrophysiological techniques and flux studies. The structural requirements to the PAT2 substrates – when considering both low and high affinity type substrates – are similar to those reported for the PAT1 protein with the essential features of a free carboxy group and a small side chain. For high affinity binding, however, PAT2 requires the amino group to be located in an α‐position, tolerates only one methyl function attached to the amino group and is highly selective for the <jats:sc>l</jats:sc>‐enantiomers. Electrophysiological analysis revealed pronounced effects of membrane potential on proton binding affinity, but substrate affinities and maximal transport currents only modestly respond to changes in membrane voltage. Whereas substrate affinity is dependent on extracellular pH, proton binding affinity to PAT2 is substrate‐independent, favouring a sequential binding of proton followed by substrate. Maximal transport currents are substrate‐dependent which suggests that the translocation of the loaded carrier to the internal side is the rate‐limiting step.</jats:p> Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 European Journal of Biochemistry |
| spellingShingle | Foltz, Martin, Oechsler, Carmen, Boll, Michael, Kottra, Gabor, Daniel, Hannelore, European Journal of Biochemistry, Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2, Biochemistry |
| title | Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_full | Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_fullStr | Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_full_unstemmed | Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_short | Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| title_sort | substrate specificity and transport mode of the proton‐dependent amino acid transporter mpat2 |
| title_unstemmed | Substrate specificity and transport mode of the proton‐dependent amino acid transporter mPAT2 |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.2004.04268.x |