Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate

  title={Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate},
  author={Holger Streb and Robin F. Irvine and Michael John Berridge and Irene Schulz},
Activation of receptors for a wide variety of hormones and neurotransmitters leads to an increase in the intracellular level of calcium. Much of this calcium is released from intracellular stores but the link between surface receptors and this internal calcium reservoir is unknown. Hydrolysis of the phosphoinositides, which is another characteristic feature of these receptors1–3, has been implicated in calcium mobilization1. The primary lipid substrates for the receptor mechanism seem to be two… 

Inositol phosphate metabolism and signal transduction.

A recent proposal that (1,4,5)IP3, by emptying an intracellular Ca2+ pool, secondarily elicits Ca2- entry will be considered.

Ion channels activated by inositol 1,4,5-trisphosphate in plasma membrane of human T-lymphocytes

It is suggested that Ins(1,4,5)P3 acts as the second messenger mediating transmembrane Ca2+ influx through specific Ca2-permeable channels in mitogen-stimulated T-cell activation.

Specific Receptors for Inositol 1,4,5-Trisphosphate in Endocrine Target Tissues

The properties of specific binding sites for IP3 are described in subcellular preparations of the adrenal cortex, the anterior pituitary gland, and the liver to describe the physiological relevance of these putative receptors.

Inositol phosphate formation and its relationship to calcium signaling.

Current understanding of the mechanisms by which inositol phosphates regulate cytoplasmic Ca2+ concentrations is summarized.

Activation of the Inositol-1,4,5-Trisphosphate Signaling System by Acute Ethanol Treatment of Rat Hepatocytes

It is now widely accepted that the primary event following receptor activation is the stimulation of an inositol lipid-specific phospholipase C that cleaves phosphatidylinositol-4,5-bisphosphate to yield inositolic Ca2+ and diacylglycerol, and a GTP-binding protein (G protein) is probably involved in coupling the occupied receptor to the phospholIPase C.

Inositol 1,4,5-trisphosphate releases Ca2+ from a nonmitochondrial store site in permeabilized rat cortical kidney cells.

Investigation of the effect of angiotensin II-amide and IP3 on intracellular Ca2 stores in saponin-treated cells and homogenate from rat kidney cortex suggests that IP3, one of their hydrolysis products, increases during hormonal stimulation.

Control of intracellular calcium redistribution by guanine nucleotides and inositol 1,4,5-trisphosphate in permeabilized GH4C1 cells.

It is concluded that, in permeabilized GH4C1 cells, GTP gamma S as well as TRH cause intracellular Ca2+ release; however, their mechanisms of action are, at least in part, distinct.

The role of phosphoinositide metabolism in signal transduction in secretory cells.

  • J. Putney
  • Biology, Computer Science
    The Journal of experimental biology
  • 1988
This review summarizes the current understanding of the mechanisms by which inositol phosphates regulate cytoplasmic Ca2+ concentrations.



Receptor-mediated net breakdown of phosphatidylinositol 4,5-bisphosphate in parotid acinar cells.

Results may suggest that net PtdIns(4,5)P2 breakdown is an early event in the stimulus-response pathway of the parotid acinar cell and could be directly involved in the mechanism of agonist-induced Ca2+ release from the plasma membrane.

Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides.

The results suggest that the earliest event in the stimulus-response pathway is the hydrolysis of polyphosphoinositides by a phosphodiesterase to yield inositol 1,4,5-trisphosphate and inositl 1, 4-bisph phosphate, which are subsequently hydrolysed to inositoli 1-phosphates and inposol.

Rapid accumulation of inositol trisphosphate reveals that agonists hydrolyse polyphosphoinositides instead of phosphatidylinositol.

  • M. Berridge
  • Biology, Computer Science
    The Biochemical journal
  • 1983
The primary action of 5-hydroxytryptamine is to stimulate the hydrolysis of PtdIns(4,5)P2 to yield diacylglycerol and Ins(1,4,4)P3, which suggests that they could function as second messengers, perhaps to control the release of calcium from internal pools.

Hormone-stimulated metabolism of inositol lipids and its relationship to hepatic receptor function.

It seems that vasopressin-stimulated PtdIns degradation in hepatocytes is not a consequence of intracellular Ca2+-mobilization and it appears instead to be intimately coupled to receptor occupation.

Effects of secretagogues on [32P]phosphatidylinositol 4,5-bisphosphate metabolism in the exocrine pancreas.

The results suggest that agonist-induced PtdIns(4,5)P2 breakdown in the exocrine pancreas may be an early step in the stimulus-response coupling pathway and also suggest that this breakdown is not dependent on Ca2+-mobilization.

The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane.

It is suggested that this enzyme is selective for the 5-phosphate in those water-soluble phosphate esters of inositol that possess the vicinal pair of 4,5-ph phosphates but that it may also interact less strongly with other water- soluble compounds that have pairs of vicinal phosphates.

The hydrolysis of phosphatidylinositol by lysosomal enzymes of rat liver and brain.

Evidence is presented that an EDTA-insensitive phospholipase C degrading phosphatidylinositol is present in rat brain.