Description
Clonality: Monoclonal
Host: Mouse
Purification: Supernatant
In neurons, the plasma membrane is functionally separated into several distinct segments. Neurons form these domains by delivering selected components to and by confining them within each segment of the membrane. Although some mechanisms of the delivery are elucidated, that of the confinement is unclear.We show here that 1-oleoyl-2-palmitoyl-phosphatidylcholine (OPPC),a unique molecular species of phospholipids, is concentrated at the protrusion tips of several neuronal culture cells and the presynaptic area of neuronal synapses of the mouse brain. InPC12 cells, NGF-stimulated neuronal differentiation induces a phospholipase A1 activity at the protrusion tips, which co-localizes with the OPPC domain. Inhibition of the phospholipase A1activity leads to suppression of phospholipid remodeling in the tip membrane and results in disappearance of the OPPC at the tips. In these cells, confinement of dopamine transporter and G0 proteins to the tip was also disrupted. These findings link the lateral distribution of the molecular species of phospholipids to the formation of functional segments in the plasma membrane of neurons and to the mechanism of protein confinement at the synapse.
The Cosmobio Antibody Collection (CAC) has registered a monoclonal antibody (clone 15-3C1) that specifically recognizes the phospholipid 1-Oleoyl-Palmitoyl-Phosphatidylcholine (OPPC) localized at neurite tips. Recently, Kuge et al found that OPPC controls protein localization (dopamine transport protein and G protein). This suggests that phospholipid remodeling is performed in the cell membrane, and that OPPC may play an important role in neurotransmission and be related to pathologies such as Parkinson's disease and dementia.
Antibody Source: Professor Koichi Honke of Kochi University School of Medicine.
[from: Kuge, H., Akahori, K., Yagyu K., Honke K. Functional Compartmentalization of the Plasma Membrane of Neurons by a Unique Acyl Chain Composition of Phospholipids The Journal Of Biological Chemistry (2014) 289(39): 26783–26793.
