Related Experiment Video
Updated: Aug 8, 2026
08:59
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Cellular function of calcium-independent phospholipase A2
1Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Kyoto, Japan.
Biological & Pharmaceutical Bulletin
|August 12, 2004
Summary
Calcium-independent phospholipase A2 (iPLA2) regulates cellular functions by generating signaling molecules like arachidonic acid. This review focuses on iPLA2
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Calcium-independent phospholipase A2 (iPLA2), a group VI PLA2, is regulated by kinases, calmodulin, and reactive oxygen species.
- iPLA2 plays a role in stimulus-induced arachidonic acid release and lysophospholipid generation, varying by cell type and stimulus.
- While iPLA2 is involved in phospholipid remodeling, its products also function as crucial signaling molecules.
Purpose of the Study:
- To review the functional roles of iPLA2 in cellular responses to stimulation.
- To highlight the significance of iPLA2-generated signaling molecules in various cellular processes.
Main Methods:
- Literature review of existing research on iPLA2.
- Analysis of studies investigating iPLA2's involvement in cellular signaling pathways.
Main Results:
- iPLA2-derived arachidonic acid and lysophospholipids act as signaling molecules.
- These molecules are implicated in diverse cellular functions including eicosanoid production, insulin secretion, apoptosis, proliferation, membrane trafficking, and myocardial ischemia.
Conclusions:
- iPLA2 is a key enzyme in cellular signaling, mediating responses to various stimuli.
- Understanding iPLA2's function is critical for elucidating cellular mechanisms in health and disease.
More Related Videos
08:49Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
Published on: March 14, 2021
10:31A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
Published on: September 26, 2025
Related Concept Videos
01:12What are Second Messengers?
Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
01:42Phosphoinositides and PIPs
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
01:15Amplifying Signals via Second Messengers
Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
01:11IP3/DAG Signaling Pathway
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
01:27Feedback Regulation of Calcium Concentration
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
01:16Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...