Abstract
Microglia are immune brain cells involved in neuroinflammation. They express a lot of proteins on their surface such as receptors that can be activated by mediators released in the microglial environment. Among these receptors, purinergic receptor expression could be modified depending on the activation status of microglia. In this review, we focus on P2Y receptors and more specifically on P2RY12 that is involved in microglial motility and migration, the first step of neuroinflammation process. We describe the purinergic receptor families, P2RY12 structure, expression and physiological functions. The pharmacological and genetic tools for studying this receptor are detailed thereafter. Last but not least, we report the contribution of microglial P2RY12 to neuroinflammation in acute and chronic brain pathologies in order to better understand P2RY12 microglial role.
Highlights
Microglia are the main immune cells in the brain
We have attempted to give an overview of the importance of microglial P2RY12 in neuroinflammation
P2RY12 expression was used as a marker of non-activated/homeostatic microglia, the key cell of neuroinflammation, and a decreased expression was associated with proinflammatory activated microglia
Summary
Microglia are the main immune cells in the brain. These plastic cells display a variety of morphological and functional states in both healthy and pathologic conditions. Microglia express a variety of cell-surface proteins that mediate their functions. Among these proteins, one can find some purinergic receptors. Purinergic signaling plays an important role in regulating microglial activity. As microglia are involved in neuroinflammation, increasing studies have described the role of microglial purinergic receptors in brain inflammatory processes. After a brief description of purinergic receptor families, we review P2RY12 structure, expression and functions, especially the microglial one. In this structure, both disulfide bonds are part of the agonist bound structure [6]. Both disulfide bonds are part of the agonist bound structure [6] When it is antagonized, the receptor binding pocket is wide open and consists. The disulfide bond between the first and the second extracellular loop is missing
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