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Stimulation by Inositol Trisphosphate and Tetrakisphosphate of a Protein Phosphatase

  • Jean Zwiller
  • Stuart S. Nakamoto
  • Alton L. Boynton
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)

Abstract

Hormone-receptor coupling often results in the activation of phospholipase C which in turn hydrolyzes phosphatidylinositol 4,5-bisphosphate into two second messengers, 1,2-diacylglycerol (DAG) and inositol 1,4,5-trisphosphate [Ins(1,4,5)]P3. It is well known that DAG remains in the membrane domain and activates protein kinase C while Ins(1,4,5)P3 is soluble and is known to increase the intracellular level of Ca2+. 1,2 Ins(l,4,5)P3 may subsequently be converted to Ins(1,3,4,5)P4 by a soluble inositol trisphosphate 3-Phosphokinase.3 Both Ins(1,4,5)P3 and Ins(1,3,4,5)P4 are substrates of a membrane-bound 5-Phosphomonoesterase being degraded to Ins(1,4)P2 and Ins(1,3,4)P3 respectively.4,5 Ins(1,4,5)P3 and Ins(1,3,4)P3 both mobilize Ca2+,2,6 while the physiological function of Ins(1,3,4,5)P4 is unknown although indirect evidence suggests that it may affect plasma membrane Ca2+ channels.7,8

Keywords

Phosphatase Activity Protein Phosphatase Inositol Phosphate Inositol Trisphosphate Protein Phosphatase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Jean Zwiller
    • 1
  • Stuart S. Nakamoto
    • 1
  • Alton L. Boynton
    • 1
  1. 1.Cancer Research CenterUniversity of HawaiiHonoluluUSA

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