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

Research output: Contribution to journalArticle

115 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 languageEnglish
Pages (from-to)471-474
Number of pages4
JournalScience
Volume278
Issue number5337
DOIs
StatePublished - Oct 17 1997
Externally publishedYes

Fingerprint

Phytic Acid
Phosphoric Monoester Hydrolases
Protein Phosphatase 2
Polyphosphates
L-Type Calcium Channels
Inositol Phosphates
Phosphoprotein Phosphatases
Insulin-Secreting Cells
Inositol
Threonine
Calcium Channels
Serine
Cell Membrane
Calcium
Glucose

ASJC Scopus subject areas

  • General

Cite this

Larsson, O., Barker, C. J., Sjöholm, Å., Carlqvist, H., Michell, R. H., Bertorello, A., ... Berggren, P. O. (1997). Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. Science, 278(5337), 471-474. https://doi.org/10.1126/science.278.5337.471

Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. / Larsson, Olof; Barker, Christopher J.; Sjöholm, Åke; Carlqvist, Håkan; Michell, Robert H.; Bertorello, Alejandro; Nilsson, Thomas; Honkanen, Richard E.; Mayr, Georg W.; Zwiller, Jean; Berggren, Per Olof.

In: Science, Vol. 278, No. 5337, 17.10.1997, p. 471-474.

Research output: Contribution to journalArticle

Larsson, O, Barker, CJ, Sjöholm, Å, Carlqvist, H, Michell, RH, Bertorello, A, Nilsson, T, Honkanen, RE, Mayr, GW, Zwiller, J & Berggren, PO 1997, 'Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate', Science, vol. 278, no. 5337, pp. 471-474. https://doi.org/10.1126/science.278.5337.471
Larsson O, Barker CJ, Sjöholm Å, Carlqvist H, Michell RH, Bertorello A et al. Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. Science. 1997 Oct 17;278(5337):471-474. https://doi.org/10.1126/science.278.5337.471
Larsson, Olof ; Barker, Christopher J. ; Sjöholm, Åke ; Carlqvist, Håkan ; Michell, Robert H. ; Bertorello, Alejandro ; Nilsson, Thomas ; Honkanen, Richard E. ; Mayr, Georg W. ; Zwiller, Jean ; Berggren, Per Olof. / Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. In: Science. 1997 ; Vol. 278, No. 5337. pp. 471-474.
@article{6f52666ced5142a49957a1067b32f26b,
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",
month = "10",
day = "17",
doi = "10.1126/science.278.5337.471",
language = "English",
volume = "278",
pages = "471--474",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5337",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0030667979&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030667979&partnerID=8YFLogxK

U2 - 10.1126/science.278.5337.471

DO - 10.1126/science.278.5337.471

M3 - Article

C2 - 9334307

AN - SCOPUS:0030667979

VL - 278

SP - 471

EP - 474

JO - Science

JF - Science

SN - 0036-8075

IS - 5337

ER -