Changes of enzyme activity in lipid signaling pathways related to substrate reordering

Dino G. Salinas, Milton De La Fuente, JUAN GUILLERMO REYES MARTINEZ

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

The static fluid mosaic model of biological membranes has been progressively complemented by a dynamic membrane model that includes phospholipid reordering in domains that are proposed to extend from nanometers to microns. Kinetic models for lipolytic enzymes have only been developed for homogeneous lipid phases. In this work, we develop a generalization of the well-known surface dilution kinetic theory to cases where, in a same lipid phase, both domain and nondomain phases coexist. Our model also allows understanding the changes in enzymatic activity due to a decrease of free substrate concentration when domains are induced by peptides. This lipid reordering and domain dynamics can affect the activity of lipolytic enzymes, and can provide a simple explanation for how basic peptides, with a strong direct interaction with acidic phospholipids (such as β-amyloid peptide), may cause a complex modulation of the activities of many important enzymes in lipid signaling pathways.

Original languageEnglish
Pages (from-to)885-894
Number of pages10
JournalBiophysical Journal
Volume89
Issue number2
DOIs
StatePublished - Aug 2005
Externally publishedYes

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