Fractalkine, also known as CX3CL1, is a unique chemokine that plays a crucial role in the immune system. It is the only member of the CX3C subfamily of chemokines and is known for its dual function as both a chemoattractant and an adhesion molecule . This article delves into the background, structure, function, and significance of Fractalkine, particularly focusing on its recombinant form in rats.
Fractalkine was discovered over two decades ago and has since been extensively studied for its role in various physiological and pathological processes . Unlike other chemokines, Fractalkine is synthesized as a transmembrane protein, which can be cleaved to produce a soluble form . This dual form allows it to function in both cell-cell adhesion and signaling.
Fractalkine is predominantly released by neurons and facilitates communication between neurons and glial cells . It binds to its receptor, CX3CR1, which is expressed on various immune cells, including monocytes, natural killer cells, and T cells . This interaction plays a significant role in the recruitment and adhesion of these cells to sites of inflammation or injury.
The CX3CL1-CX3CR1 axis has been implicated in several diseases, including chronic kidney disease (CKD), neuroinflammation, and cardiovascular diseases . In CKD, for instance, the signaling pathway is involved in the recruitment of innate immune cells into the kidney, contributing to inflammation and fibrosis . Similarly, in neuroinflammation, Fractalkine signaling is considered a potential target for alleviating symptoms .
Given its significant role in various diseases, Fractalkine and its receptor have been explored as potential therapeutic targets. Research suggests that targeting the CX3CL1-CX3CR1 axis could benefit patients with conditions like CKD and neuroinflammation . However, despite promising preclinical data, there have been no human trials of targeted therapeutic agents to date .