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  The role of phosphatidylinositides in stimulus-secretion coupling in the exocrine pancreas

Schulz, I., Schnefel, S., Banfić, H., Thévenod, F., Kemmer, T. P., & Eckhardt, L. (1987). The role of phosphatidylinositides in stimulus-secretion coupling in the exocrine pancreas. In Society of General Physiologists Series (pp. 117-131).

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 Creators:
Schulz, Irene1, Author           
Schnefel, Susanne1, Author           
Banfić, Hrvoje2, Author
Thévenod, Frank1, Author           
Kemmer, Thomas P.1, Author           
Eckhardt, Luise1, Author           
Affiliations:
1Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              
2Department of Physiology, Faculty of Medicine, University of Zagreb, Yugoslavia, ou_persistent22              

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 Abstract: Cell activation of different cell types is accompanied by receptor-mediated stimulation of phospholipase C and a consequent breakdown of phosphatidylinositol 4,5-bisphosphate. Evidence suggests that GTP-binding proteins are involved in this signal transduction mechanism, which couples receptors to phospholipase C. Both the hydrolysis products diacylglycerol (DG) and inositol 1,4,5-trisphosphate (IP3) are intracellular messengers for cellular responses such as secretion, as illustrated by the pancreatic acinar cell. IP3 releases Ca2+ from a nonmitochondrial Ca2+ pool likely to be the endoplasmic reticulum (ER). This Ca2+ release leads to a transient rise in the cytosolic free Ca2+ concentration from approximately 100 to approximately 800 nmol/liter, by which enzyme secretion is initiated. For sustained secretion, Ca2+ influx into the cell is necessary to keep the cytosolic free Ca2+ concentration at a slightly elevated level. Activation of protein kinase C by DG and Ca2+ seems to play a major role in the second, sustained phase of secretion. Ca2+ reuptake into the ER and Ca2+ extrusion from the cell are achieved by (Ca2+ + Mg2+)-ATPase in both the ER and the plasma membrane as well as by an Na+/Ca2+ exchange in the latter. In the final step of exocytosis, protein phosphorylation by Ca2+-, DG-, and cAMP-dependent protein kinases is probably involved.

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Language(s): eng - English
 Dates: 1987
 Publication Status: Issued
 Pages: 15
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: PMID: 3145561
 Degree: -

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Title: Society of General Physiologists Series
Source Genre: Series
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Pages: - Volume / Issue: 42 Sequence Number: - Start / End Page: 117 - 131 Identifier: -