The P2X7 receptor: A main player in inflammation
Elena Adinolfi1, Anna Lisa Giuliani1, Elena De Marchi1
1Department of Morphology, Surgery and Experimental Medicine, Section of Pathology, Oncology and Experimental Biology, University of Ferrara, Ferrara, Italy.
Biochemical Pharmacology
|December 31, 2017
Summary
Extracellular ATP, acting via the P2X7 receptor (P2X7R), drives inflammation and immune responses. P2X7R modulation is key for managing infections and chronic diseases, with potential therapeutic applications.
Area of Science:
- Immunology
- Cell Biology
- Molecular Medicine
Background:
- Damage-associated molecular patterns (DAMPs) signal cellular distress.
- Extracellular ATP is a conserved DAMP activating the P2X7 receptor (P2X7R).
- P2X7R is an ion channel expressed on immune cells, crucial for inflammatory processes.
Purpose of the Study:
- To review the established and emerging roles of P2X7R in septic and sterile inflammation.
- To explore P2X7R's function in infectious diseases, including bacterial, parasitic, and viral infections.
- To discuss P2X7R-mediated intracellular pathways and therapeutic potential.
Main Methods:
- Literature review of established and recent research.
- Focus on P2X7R's role in immune modulation.
- Analysis of P2X7R signaling pathways and disease involvement.
Main Results:
- P2X7R activation is central to inflammatory and reparatory responses.
- P2X7R modulates immune responses against Mycobacteria, Plasmodium, and HIV-1.
- P2X7R influences pathways like NLRP3 inflammasome, NF-kB, and VEGF, impacting chronic diseases.
Conclusions:
- P2X7R plays a significant role in diverse inflammatory conditions and infections.
- Understanding P2X7R signaling offers insights into chronic disease pathogenesis.
- P2X7R antagonists represent a promising therapeutic strategy.
Related Concept Videos
Inflammation
62.5K
Overview
62.5K
Internal Receptors
74.8K
Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
74.8K
Receptor-mediated Endocytosis
111.6K
Overview
111.6K
Enzyme-linked Receptors
86.8K
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
86.8K
G-protein Coupled Receptors
132.2K
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
132.2K
Types of Receptors: Internal Receptors
32.7K
Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism.
Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
32.7K


