Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate

Olof Larsson; Christopher J. Barker; Åke Sjöholm; Håkan Carlqvist; Robert H. Michell; Alejandro Bertorello; Thomas Nilsson; Richard E. Honkanen; Georg W. Mayr; Jean Zwiller; Per Olof Berggren

doi:10.1126/science.278.5337.471

Inhibition of phosphatases and increased Ca²⁺ channel activity by inositol hexakisphosphate

Olof Larsson, Christopher J. Barker, Åke Sjöholm, Håkan Carlqvist, Robert H. Michell, Alejandro Bertorello, Thomas Nilsson, Richard E. Honkanen, Georg W. Mayr, Jean Zwiller, Per Olof Berggren^*

^*Corresponding author for this work

Biosciences

Research output: Contribution to journal › Article › peer-review

119 Citations (Scopus)

Abstract

Inositol hexakisphosphate (InsP₆), the dominant inositol phosphate in insulin-secreting pancreatic β cells, inhibited the serine-threonine protein phosphatases type 1, type 2A, and type 3 in a concentration-dependent manner. The activity of voltage-gated L-type calcium channels is increased in cells treated with inhibitors of serine-threonine protein phosphatases. Thus, the increased calcium channel activity obtained in the presence of InsP₆ might result from the inhibition of phosphatase activity. Glucose elicited a transient increase in InsP₆ concentration, which indicates that this inositol polyphosphate may modulate calcium influx over the plasma membrane and serve as a signal in the pancreatic β cell stimulus-secretion coupling.

Original language	English
Pages (from-to)	471-474
Number of pages	4
Journal	Science
Volume	278
Issue number	5337
DOIs	https://doi.org/10.1126/science.278.5337.471
Publication status	Published - 17 Oct 1997

ASJC Scopus subject areas

General

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10.1126/science.278.5337.471

Cite this

@article{03cab15eab9049d0b7f938ffc71a0b61,

title = "Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate",

abstract = "Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic β cells, inhibited the serine-threonine protein phosphatases type 1, type 2A, and type 3 in a concentration-dependent manner. The activity of voltage-gated L-type calcium channels is increased in cells treated with inhibitors of serine-threonine protein phosphatases. Thus, the increased calcium channel activity obtained in the presence of InsP6 might result from the inhibition of phosphatase activity. Glucose elicited a transient increase in InsP6 concentration, which indicates that this inositol polyphosphate may modulate calcium influx over the plasma membrane and serve as a signal in the pancreatic β cell stimulus-secretion coupling.",

author = "Olof Larsson and Barker, {Christopher J.} and {\AA}ke Sj{\"o}holm and H{\aa}kan Carlqvist and Michell, {Robert H.} and Alejandro Bertorello and Thomas Nilsson and Honkanen, {Richard E.} and Mayr, {Georg W.} and Jean Zwiller and Berggren, {Per Olof}",

year = "1997",

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doi = "10.1126/science.278.5337.471",

language = "English",

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TY - JOUR

T1 - Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate

AU - Larsson, Olof

AU - Barker, Christopher J.

AU - Sjöholm, Åke

AU - Carlqvist, Håkan

AU - Michell, Robert H.

AU - Bertorello, Alejandro

AU - Nilsson, Thomas

AU - Honkanen, Richard E.

AU - Mayr, Georg W.

AU - Zwiller, Jean

AU - Berggren, Per Olof

PY - 1997/10/17

Y1 - 1997/10/17

N2 - Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic β cells, inhibited the serine-threonine protein phosphatases type 1, type 2A, and type 3 in a concentration-dependent manner. The activity of voltage-gated L-type calcium channels is increased in cells treated with inhibitors of serine-threonine protein phosphatases. Thus, the increased calcium channel activity obtained in the presence of InsP6 might result from the inhibition of phosphatase activity. Glucose elicited a transient increase in InsP6 concentration, which indicates that this inositol polyphosphate may modulate calcium influx over the plasma membrane and serve as a signal in the pancreatic β cell stimulus-secretion coupling.

AB - Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic β cells, inhibited the serine-threonine protein phosphatases type 1, type 2A, and type 3 in a concentration-dependent manner. The activity of voltage-gated L-type calcium channels is increased in cells treated with inhibitors of serine-threonine protein phosphatases. Thus, the increased calcium channel activity obtained in the presence of InsP6 might result from the inhibition of phosphatase activity. Glucose elicited a transient increase in InsP6 concentration, which indicates that this inositol polyphosphate may modulate calcium influx over the plasma membrane and serve as a signal in the pancreatic β cell stimulus-secretion coupling.

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