Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell
Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar conc...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: FEBS Letters - Amsterdam : Elsevier, 319(1993), 1-2, Seite 128-132 |
| Übergeordnetes Werk: |
volume:319 ; year:1993 ; number:1-2 ; pages:128-132 |
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| 245 | 1 | 0 | |a Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell |
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| 520 | |a Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. | ||
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(DE-627)NLEJ173302211 (DE-599)GBVNLZ173302211 DE-627 ger DE-627 rakwb eng Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Islam, M.S. oth Berggren, P.-O. oth Larsson, O. oth in FEBS Letters Amsterdam : Elsevier 319(1993), 1-2, Seite 128-132 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:319 year:1993 number:1-2 pages:128-132 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80051-U GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 319 1993 1-2 128-132 |
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(DE-627)NLEJ173302211 (DE-599)GBVNLZ173302211 DE-627 ger DE-627 rakwb eng Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Islam, M.S. oth Berggren, P.-O. oth Larsson, O. oth in FEBS Letters Amsterdam : Elsevier 319(1993), 1-2, Seite 128-132 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:319 year:1993 number:1-2 pages:128-132 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80051-U GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 319 1993 1-2 128-132 |
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(DE-627)NLEJ173302211 (DE-599)GBVNLZ173302211 DE-627 ger DE-627 rakwb eng Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Islam, M.S. oth Berggren, P.-O. oth Larsson, O. oth in FEBS Letters Amsterdam : Elsevier 319(1993), 1-2, Seite 128-132 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:319 year:1993 number:1-2 pages:128-132 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80051-U GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 319 1993 1-2 128-132 |
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(DE-627)NLEJ173302211 (DE-599)GBVNLZ173302211 DE-627 ger DE-627 rakwb eng Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Islam, M.S. oth Berggren, P.-O. oth Larsson, O. oth in FEBS Letters Amsterdam : Elsevier 319(1993), 1-2, Seite 128-132 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:319 year:1993 number:1-2 pages:128-132 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80051-U GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 319 1993 1-2 128-132 |
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(DE-627)NLEJ173302211 (DE-599)GBVNLZ173302211 DE-627 ger DE-627 rakwb eng Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Islam, M.S. oth Berggren, P.-O. oth Larsson, O. oth in FEBS Letters Amsterdam : Elsevier 319(1993), 1-2, Seite 128-132 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:319 year:1993 number:1-2 pages:128-132 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80051-U GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 319 1993 1-2 128-132 |
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sulfhydryl oxidation induces rapid and reversible closure of the atp-regulated k^+ channel in the pancreatic β-cell |
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Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell |
| abstract |
Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. |
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Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. |
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Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ173302211</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705183719.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070505s1993 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ173302211</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ173302211</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Sulfhydryl oxidation induces rapid and reversible closure of the ATP-regulated K^+ channel in the pancreatic β-cell</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1993</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Effects of sulfhydryl modification on the ATP regulated K^1 channel (K"A"T"P channel) in the pancreatic β-cell were studied, using the patch clamp technique. Application of the sulfhydryl oxidizing agents thimerosal and 2,2'-dithio-bis(5-nitropyridine) (DTBNP), in micromolar concentrations, caused complete inhibition of the k"A"T"P channel, in inside-out patches. The inhibition was rapid and was reversed by the disulfide reducing agents dithiothreitol and cysteine. Thimerosal, which is poorly membrane permeable, inhibited channel activity, only when applied to the intracellular face of the plasma membrane. In contrast, DTBNP, which is highly lipophilic, caused closure of the k"A"T"P channel and consequent depolarization of the membrane potential, also when applied extracellularly. Our results indicate the presence of accessible free SH groups on the cytoplasmic side of the k"A"T"P channel in the pancreatic β-cell. These SH groups are essential for channel function and it is possible that thiol-dependent redox mechanisms can modulate K"A"T"P channel activity.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Islam, M.S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berggren, P.-O.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Larsson, O.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">FEBS Letters</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">319(1993), 1-2, Seite 128-132</subfield><subfield code="w">(DE-627)NLEJ173141048</subfield><subfield code="w">(DE-600)1460391-3</subfield><subfield code="x">0014-5793</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:319</subfield><subfield code="g">year:1993</subfield><subfield code="g">number:1-2</subfield><subfield code="g">pages:128-132</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80051-U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">319</subfield><subfield code="j">1993</subfield><subfield code="e">1-2</subfield><subfield code="h">128-132</subfield></datafield></record></collection>
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7.4011765 |