Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells

Laura Bianchi, Mary Louise Roy, Maurizio Taglialatela, David W. Lundgren, Arthur M. Brown, Eckhard Ficker

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Polyamines have been shown to participate in the rectification of cloned inwardly rectifying potassium channels, a class of potassium channel proteins that conducts inward current more readily than outward current. Here, basophil leukemia cells were used to determine the effects of polyamines on a native, inwardly rectifying potassium current. Rat basophil leukemia cells were cultured in the presence of two different polyamine biosynthesis inhibitors, and both the electrophysiological properties and the polyamine levels were monitored. Treatment with α-difluoromethylornithine, a specific ornithine decarboxylase inhibitor, resulted in no significant change of electrophysiological properties. In contrast, treatment with 5'-{[(Z)-4- amino-2-butenyl]-methyl-amino}-5'-deoxyadenosine (MDL73811), an inhibitor of S-adenosylmethionine decarboxylase, resulted in increased outward currents through inwardly rectifying potassium channels while intracellular putrescine was markedly increased and spermidine and spermine levels were decreased. Fluctuations of intracellular polyamine concentrations as imposed by MDL73811 were directly translated in an altered cell excitability. Based on these results we conclude that the rectification properties of native inwardly rectifying potassium channels are largely controlled by intracellular spermine.

Original languageEnglish
Pages (from-to)6114-6121
Number of pages8
JournalJournal of Biological Chemistry
Volume271
Issue number11
DOIs
StatePublished - Mar 15 1996
Externally publishedYes

Fingerprint

Inwardly Rectifying Potassium Channel
Spermine
Polyamines
Basophils
Leukemia
Adenosylmethionine Decarboxylase
Eflornithine
Putrescine
Spermidine
Potassium Channels
Biosynthesis
Rats
Cultured Cells
Potassium
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Bianchi, L., Roy, M. L., Taglialatela, M., Lundgren, D. W., Brown, A. M., & Ficker, E. (1996). Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells. Journal of Biological Chemistry, 271(11), 6114-6121. https://doi.org/10.1074/jbc.271.11.6114

Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells. / Bianchi, Laura; Roy, Mary Louise; Taglialatela, Maurizio; Lundgren, David W.; Brown, Arthur M.; Ficker, Eckhard.

In: Journal of Biological Chemistry, Vol. 271, No. 11, 15.03.1996, p. 6114-6121.

Research output: Contribution to journalArticle

Bianchi, L, Roy, ML, Taglialatela, M, Lundgren, DW, Brown, AM & Ficker, E 1996, 'Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells', Journal of Biological Chemistry, vol. 271, no. 11, pp. 6114-6121. https://doi.org/10.1074/jbc.271.11.6114
Bianchi, Laura ; Roy, Mary Louise ; Taglialatela, Maurizio ; Lundgren, David W. ; Brown, Arthur M. ; Ficker, Eckhard. / Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 11. pp. 6114-6121.
@article{bc2ebf99a0434f41b9d24a179b996cfe,
title = "Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells",
abstract = "Polyamines have been shown to participate in the rectification of cloned inwardly rectifying potassium channels, a class of potassium channel proteins that conducts inward current more readily than outward current. Here, basophil leukemia cells were used to determine the effects of polyamines on a native, inwardly rectifying potassium current. Rat basophil leukemia cells were cultured in the presence of two different polyamine biosynthesis inhibitors, and both the electrophysiological properties and the polyamine levels were monitored. Treatment with α-difluoromethylornithine, a specific ornithine decarboxylase inhibitor, resulted in no significant change of electrophysiological properties. In contrast, treatment with 5'-{[(Z)-4- amino-2-butenyl]-methyl-amino}-5'-deoxyadenosine (MDL73811), an inhibitor of S-adenosylmethionine decarboxylase, resulted in increased outward currents through inwardly rectifying potassium channels while intracellular putrescine was markedly increased and spermidine and spermine levels were decreased. Fluctuations of intracellular polyamine concentrations as imposed by MDL73811 were directly translated in an altered cell excitability. Based on these results we conclude that the rectification properties of native inwardly rectifying potassium channels are largely controlled by intracellular spermine.",
author = "Laura Bianchi and Roy, {Mary Louise} and Maurizio Taglialatela and Lundgren, {David W.} and Brown, {Arthur M.} and Eckhard Ficker",
year = "1996",
month = "3",
day = "15",
doi = "10.1074/jbc.271.11.6114",
language = "English",
volume = "271",
pages = "6114--6121",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "11",

}

TY - JOUR

T1 - Regulation by spermine of native inward rectifier K+ channels in RBL-1 cells

AU - Bianchi, Laura

AU - Roy, Mary Louise

AU - Taglialatela, Maurizio

AU - Lundgren, David W.

AU - Brown, Arthur M.

AU - Ficker, Eckhard

PY - 1996/3/15

Y1 - 1996/3/15

N2 - Polyamines have been shown to participate in the rectification of cloned inwardly rectifying potassium channels, a class of potassium channel proteins that conducts inward current more readily than outward current. Here, basophil leukemia cells were used to determine the effects of polyamines on a native, inwardly rectifying potassium current. Rat basophil leukemia cells were cultured in the presence of two different polyamine biosynthesis inhibitors, and both the electrophysiological properties and the polyamine levels were monitored. Treatment with α-difluoromethylornithine, a specific ornithine decarboxylase inhibitor, resulted in no significant change of electrophysiological properties. In contrast, treatment with 5'-{[(Z)-4- amino-2-butenyl]-methyl-amino}-5'-deoxyadenosine (MDL73811), an inhibitor of S-adenosylmethionine decarboxylase, resulted in increased outward currents through inwardly rectifying potassium channels while intracellular putrescine was markedly increased and spermidine and spermine levels were decreased. Fluctuations of intracellular polyamine concentrations as imposed by MDL73811 were directly translated in an altered cell excitability. Based on these results we conclude that the rectification properties of native inwardly rectifying potassium channels are largely controlled by intracellular spermine.

AB - Polyamines have been shown to participate in the rectification of cloned inwardly rectifying potassium channels, a class of potassium channel proteins that conducts inward current more readily than outward current. Here, basophil leukemia cells were used to determine the effects of polyamines on a native, inwardly rectifying potassium current. Rat basophil leukemia cells were cultured in the presence of two different polyamine biosynthesis inhibitors, and both the electrophysiological properties and the polyamine levels were monitored. Treatment with α-difluoromethylornithine, a specific ornithine decarboxylase inhibitor, resulted in no significant change of electrophysiological properties. In contrast, treatment with 5'-{[(Z)-4- amino-2-butenyl]-methyl-amino}-5'-deoxyadenosine (MDL73811), an inhibitor of S-adenosylmethionine decarboxylase, resulted in increased outward currents through inwardly rectifying potassium channels while intracellular putrescine was markedly increased and spermidine and spermine levels were decreased. Fluctuations of intracellular polyamine concentrations as imposed by MDL73811 were directly translated in an altered cell excitability. Based on these results we conclude that the rectification properties of native inwardly rectifying potassium channels are largely controlled by intracellular spermine.

UR - http://www.scopus.com/inward/record.url?scp=0029865753&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029865753&partnerID=8YFLogxK

U2 - 10.1074/jbc.271.11.6114

DO - 10.1074/jbc.271.11.6114

M3 - Article

C2 - 8626398

AN - SCOPUS:0029865753

VL - 271

SP - 6114

EP - 6121

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 11

ER -