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Functional characterization of Ih‐channel splice variants from Apis mellifera
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Zeitschriftentitel: | FEBS Letters |
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Personen und Körperschaften: | , , , |
In: | FEBS Letters, 575, 2004, 1-3, S. 99-104 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Wiley
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Schlagwörter: |
author_facet |
Gisselmann, Günter Wetzel, Christian H. Warnstedt, Maike Hatt, Hanns Gisselmann, Günter Wetzel, Christian H. Warnstedt, Maike Hatt, Hanns |
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author |
Gisselmann, Günter Wetzel, Christian H. Warnstedt, Maike Hatt, Hanns |
spellingShingle |
Gisselmann, Günter Wetzel, Christian H. Warnstedt, Maike Hatt, Hanns FEBS Letters Functional characterization of Ih‐channel splice variants from Apis mellifera Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
author_sort |
gisselmann, günter |
spelling |
Gisselmann, Günter Wetzel, Christian H. Warnstedt, Maike Hatt, Hanns 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2004.08.043 <jats:p>We isolated splice variants of the AMIH cDNA by means of polymerase chain reaction and homology screening. Splicing at one site generates at least four different channel transcripts (AMIH, AMIH<jats:sub>L</jats:sub>, AMIH<jats:sub>M</jats:sub> and AMIH<jats:sub>T</jats:sub>), which code for ion‐channel proteins that vary in the interloop regions between the membrane‐spanning domains S4 and S5. HEK293 cells in which the AMIH<jats:sub>L</jats:sub> splice variants were functionally expressed generated currents that were activated by hyperpolarizing voltage steps. Compared to AMIH, AMIH<jats:sub>L</jats:sub> cells showed pronounced differences in the voltage dependency of activation: the incorporation of 32 extra amino acids between S4 and S5 shifts the activation curve by +25 mV. Intracellular cAMP made the current‐activation potential still less negative and accelerated the activation more effectively than it does in AMIH cells. In vertebrates, functional diversity of <jats:italic>I</jats:italic> <jats:sub>h</jats:sub>‐channels is generated by four different genes. In <jats:italic>Apis mellifera</jats:italic>, splice variants coded by the single gene <jats:italic>AMIH</jats:italic> could generate a similar diversity.</jats:p> Functional characterization of <i>I</i><sub>h</sub>‐channel splice variants from <i>Apis mellifera</i> FEBS Letters |
doi_str_mv |
10.1016/j.febslet.2004.08.043 |
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Online Free |
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Chemie und Pharmazie Physik Biologie |
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Wiley, 2004 |
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Wiley, 2004 |
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2004 |
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Wiley |
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FEBS Letters |
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49 |
title |
Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_unstemmed |
Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_full |
Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_fullStr |
Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_full_unstemmed |
Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_short |
Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_sort |
functional characterization of <i>i</i><sub>h</sub>‐channel splice variants from <i>apis mellifera</i> |
topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
url |
http://dx.doi.org/10.1016/j.febslet.2004.08.043 |
publishDate |
2004 |
physical |
99-104 |
description |
<jats:p>We isolated splice variants of the AMIH cDNA by means of polymerase chain reaction and homology screening. Splicing at one site generates at least four different channel transcripts (AMIH, AMIH<jats:sub>L</jats:sub>, AMIH<jats:sub>M</jats:sub> and AMIH<jats:sub>T</jats:sub>), which code for ion‐channel proteins that vary in the interloop regions between the membrane‐spanning domains S4 and S5. HEK293 cells in which the AMIH<jats:sub>L</jats:sub> splice variants were functionally expressed generated currents that were activated by hyperpolarizing voltage steps. Compared to AMIH, AMIH<jats:sub>L</jats:sub> cells showed pronounced differences in the voltage dependency of activation: the incorporation of 32 extra amino acids between S4 and S5 shifts the activation curve by +25 mV. Intracellular cAMP made the current‐activation potential still less negative and accelerated the activation more effectively than it does in AMIH cells. In vertebrates, functional diversity of <jats:italic>I</jats:italic>
<jats:sub>h</jats:sub>‐channels is generated by four different genes. In <jats:italic>Apis mellifera</jats:italic>, splice variants coded by the single gene <jats:italic>AMIH</jats:italic> could generate a similar diversity.</jats:p> |
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author | Gisselmann, Günter, Wetzel, Christian H., Warnstedt, Maike, Hatt, Hanns |
author_facet | Gisselmann, Günter, Wetzel, Christian H., Warnstedt, Maike, Hatt, Hanns, Gisselmann, Günter, Wetzel, Christian H., Warnstedt, Maike, Hatt, Hanns |
author_sort | gisselmann, günter |
container_issue | 1-3 |
container_start_page | 99 |
container_title | FEBS Letters |
container_volume | 575 |
description | <jats:p>We isolated splice variants of the AMIH cDNA by means of polymerase chain reaction and homology screening. Splicing at one site generates at least four different channel transcripts (AMIH, AMIH<jats:sub>L</jats:sub>, AMIH<jats:sub>M</jats:sub> and AMIH<jats:sub>T</jats:sub>), which code for ion‐channel proteins that vary in the interloop regions between the membrane‐spanning domains S4 and S5. HEK293 cells in which the AMIH<jats:sub>L</jats:sub> splice variants were functionally expressed generated currents that were activated by hyperpolarizing voltage steps. Compared to AMIH, AMIH<jats:sub>L</jats:sub> cells showed pronounced differences in the voltage dependency of activation: the incorporation of 32 extra amino acids between S4 and S5 shifts the activation curve by +25 mV. Intracellular cAMP made the current‐activation potential still less negative and accelerated the activation more effectively than it does in AMIH cells. In vertebrates, functional diversity of <jats:italic>I</jats:italic> <jats:sub>h</jats:sub>‐channels is generated by four different genes. In <jats:italic>Apis mellifera</jats:italic>, splice variants coded by the single gene <jats:italic>AMIH</jats:italic> could generate a similar diversity.</jats:p> |
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spelling | Gisselmann, Günter Wetzel, Christian H. Warnstedt, Maike Hatt, Hanns 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2004.08.043 <jats:p>We isolated splice variants of the AMIH cDNA by means of polymerase chain reaction and homology screening. Splicing at one site generates at least four different channel transcripts (AMIH, AMIH<jats:sub>L</jats:sub>, AMIH<jats:sub>M</jats:sub> and AMIH<jats:sub>T</jats:sub>), which code for ion‐channel proteins that vary in the interloop regions between the membrane‐spanning domains S4 and S5. HEK293 cells in which the AMIH<jats:sub>L</jats:sub> splice variants were functionally expressed generated currents that were activated by hyperpolarizing voltage steps. Compared to AMIH, AMIH<jats:sub>L</jats:sub> cells showed pronounced differences in the voltage dependency of activation: the incorporation of 32 extra amino acids between S4 and S5 shifts the activation curve by +25 mV. Intracellular cAMP made the current‐activation potential still less negative and accelerated the activation more effectively than it does in AMIH cells. In vertebrates, functional diversity of <jats:italic>I</jats:italic> <jats:sub>h</jats:sub>‐channels is generated by four different genes. In <jats:italic>Apis mellifera</jats:italic>, splice variants coded by the single gene <jats:italic>AMIH</jats:italic> could generate a similar diversity.</jats:p> Functional characterization of <i>I</i><sub>h</sub>‐channel splice variants from <i>Apis mellifera</i> FEBS Letters |
spellingShingle | Gisselmann, Günter, Wetzel, Christian H., Warnstedt, Maike, Hatt, Hanns, FEBS Letters, Functional characterization of Ih‐channel splice variants from Apis mellifera, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
title | Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_full | Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_fullStr | Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_full_unstemmed | Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_short | Functional characterization of Ih‐channel splice variants from Apis mellifera |
title_sort | functional characterization of <i>i</i><sub>h</sub>‐channel splice variants from <i>apis mellifera</i> |
title_unstemmed | Functional characterization of Ih‐channel splice variants from Apis mellifera |
topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
url | http://dx.doi.org/10.1016/j.febslet.2004.08.043 |