| Literature DB >> 9334307 |
O Larsson1, C J Barker, A Sjöholm, H Carlqvist, R H Michell, A Bertorello, T Nilsson, R E Honkanen, G W Mayr, J Zwiller, P O Berggren.
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.Entities:
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Year: 1997 PMID: 9334307 DOI: 10.1126/science.278.5337.471
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728