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

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Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. / Larsson, O; Barker, C J; Sjöholm, A; Carlqvist, H; Michell, R H; Bertorello, A; Nilsson, T; Honkanen, R E; Mayr, Georg W.; Zwiller, J; Berggren, P O.

in: SCIENCE, Jahrgang 278, Nr. 5337, 5337, 1997, S. 471-474.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Larsson, O, Barker, CJ, Sjöholm, A, 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, Jg. 278, Nr. 5337, 5337, S. 471-474. <http://www.ncbi.nlm.nih.gov/pubmed/9334307?dopt=Citation>

APA

Larsson, O., Barker, C. J., Sjöholm, A., Carlqvist, H., Michell, R. H., Bertorello, A., Nilsson, T., Honkanen, R. E., Mayr, G. W., Zwiller, J., & Berggren, P. O. (1997). Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. SCIENCE, 278(5337), 471-474. [5337]. http://www.ncbi.nlm.nih.gov/pubmed/9334307?dopt=Citation

Vancouver

Larsson O, Barker CJ, Sjöholm A, Carlqvist H, Michell RH, Bertorello A et al. Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate. SCIENCE. 1997;278(5337):471-474. 5337.

Bibtex

@article{80d5a7f68bf74ca288adc9db1305a44d,
title = "Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate.",
abstract = "Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic beta 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 beta cell stimulus-secretion coupling.",
author = "O Larsson and Barker, {C J} and A Sj{\"o}holm and H Carlqvist and Michell, {R H} and A Bertorello and T Nilsson and Honkanen, {R E} and Mayr, {Georg W.} and J Zwiller and Berggren, {P O}",
year = "1997",
language = "Deutsch",
volume = "278",
pages = "471--474",
journal = "SCIENCE",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5337",

}

RIS

TY - JOUR

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

AU - Larsson, O

AU - Barker, C J

AU - Sjöholm, A

AU - Carlqvist, H

AU - Michell, R H

AU - Bertorello, A

AU - Nilsson, T

AU - Honkanen, R E

AU - Mayr, Georg W.

AU - Zwiller, J

AU - Berggren, P O

PY - 1997

Y1 - 1997

N2 - Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic beta 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 beta cell stimulus-secretion coupling.

AB - Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic beta 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 beta cell stimulus-secretion coupling.

M3 - SCORING: Zeitschriftenaufsatz

VL - 278

SP - 471

EP - 474

JO - SCIENCE

JF - SCIENCE

SN - 0036-8075

IS - 5337

M1 - 5337

ER -