Imidazoline I2 Receptor (I2)

The imidazoline I2 receptor (I2) is a subclass of imidazoline binding sites, originally identified by their high-affinity binding to radiolabeled ligands such as [^3H]-idazoxan and [^3H]-2-BFI. Unlike classical neurotransmitter receptors, the I2 receptor is not a single protein but refers to several different proteins that share this ligand-binding property. The molecular identity of these proteins remains incompletely defined, though one has been identified as brain creatine kinase. The primary function of the I2 receptor appears to be allosteric modulation of monoamine oxidase enzymes on mitochondria. It is not G protein-coupled; its transduction mechanism remains unknown or undefined. Some evidence suggests involvement in modulating body temperature and neuroprotection through mechanisms that are still being elucidated. Strong evidence supports a role in analgesia—especially persistent/chronic pain states such as neuropathic or inflammatory pain. Preclinical studies suggest neuroprotective effects potentially relevant to stroke or neurodegenerative diseases. Altered expression/distribution of these receptors has been observed in disorders like Alzheimer's disease (AD), Parkinson's disease (PD), Huntington’s disease, depression, etc.

Other names

Imidazoline binding site I2I2 receptorI2-IR

Allosteric modulation of monoamine oxidase enzymes on mitochondria