Artículo de revista
Changes of enzyme activity in lipid signaling pathways related to substrate reordering
Fecha
2005-08Registro en:
BIOPHYSICAL JOURNAL 89 (2): 885-894 AUG 2005
0006-3495
Autor
Salinas, Dino
Fuente, Milton de la
Reyes Frías, Juan
Institución
Resumen
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 beta-amyloid peptide), may cause a complex modulation of the activities of many important enzymes in lipid signaling pathways.