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J Theor Biol. 2013 Nov 21;337:174-80. doi: 10.1016/j.jtbi.2013.08.022. Epub 2013 Aug 31.

Modeling sphingomyelin synthase 1 driven reaction at the Golgi apparatus can explain data by inclusion of a positive feedback mechanism.

Author information

  • 1Institute for Systems Theory and Automatic Control, University of Stuttgart, Pfaffenwaldring 9, 70569 Stuttgart, Germany. Electronic address: caterina.thomaseth@ist.uni-stuttgart.de.

Abstract

Here we present a minimal mathematical model for the sphingomyelin synthase 1 (SMS1) driven conversion of ceramide to sphingomyelin based on chemical reaction kinetics. We demonstrate via mathematical analysis that this model is not able to qualitatively reproduce experimental measurements on lipid compositions after altering SMS1 activity. We prove that a positive feedback mechanism from the products to the reactants of the reaction is one possible model extension to explain these specific experimental data. The proposed mechanism in fact exists in vivo via protein kinase D and the ceramide transfer protein CERT. The model is further evaluated by additional observations from the literature.

© 2013 The Authors. Published by Elsevier Ltd. All rights reserved.

KEYWORDS:

CHO Cells; Cer; Chinese hamster ovary cells; DAG; ER; Feedback control; IFT; PC; PH Domain; PI; PI4KIIIβ; PI4P; PKD; SM; SMS; Sphingomyelin synthase 1; Sphingomyelin synthesis; TGN; ceramide; diacylglycerol; endoplasmic Reticulum; implicit function theorem; phosphatidylcholine; phosphatidylinositol; phosphatidylinositol(4)-Phosphat; phosphatidylinositol-4-Kinase IIIβ; pleckstrin homology domain; protein kinase D; sphingomyelin; sphingomyelin synthase; trans-Golgi network

PMID:
24001971
[PubMed - indexed for MEDLINE]
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