The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
-
Anja Gemeinhardt
Abstract
Phospholipase D (PLD) is a receptor-regulated signalling enzyme involved in biological functions, such as exocytosis, phagocytosis, actin dynamics, membrane trafficking, and is considered to be essential for stimulated degranulation of cells. The purpose of our investigation was to examine how the fatty acid pattern of cellular membranes influences the activities and cellular distribution of the PLD1 and PLD2 isoforms. Expression of GFP-tagged PLD1 and PLD2 in COS-1 cells that were stimulated with mastoparan after cultivation in 20 μmol linoleic (C18:2n6) or linolenic (C18:3n3) acid for 4 d demonstrated that PLD1 dramatically alters its cellular distribution and is redistributed from intracellular vesicles to the cell surface. PLD2, on the other hand, maintains its localisation at the plasma membrane. The activity of PLD, which corresponds to PLD1 and PLD2, significantly increased two- to three-fold in the presence of the fatty acids. We conclude that linoleic acid and linolenic acid supplementation affect the intracellular trafficking of the PLD1 isoform and the activity of PLD most likely due to alterations in the membrane lipid environment conferred by the fatty acids.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Review
- Glutathione dysregulation and the etiology and progression of human diseases
- Protein Structure and Function
- Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
- Role of catalytic and non-catalytic subsite residues in ribonuclease activity of human eosinophil-derived neurotoxin
- Cell Biology and Signaling
- Expression and localization of atypical PKC isoforms in liver parenchymal cells
- Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
- The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
- Proteolysis
- Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
- The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
Articles in the same Issue
- Review
- Glutathione dysregulation and the etiology and progression of human diseases
- Protein Structure and Function
- Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
- Role of catalytic and non-catalytic subsite residues in ribonuclease activity of human eosinophil-derived neurotoxin
- Cell Biology and Signaling
- Expression and localization of atypical PKC isoforms in liver parenchymal cells
- Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
- The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
- Proteolysis
- Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
- The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
