Neutrophil surface and membrane-associated immune receptors

Neutrophils, the most abundant leukocytes in human blood, express a diverse array of surface and membrane-associated immune receptors that are essential for their role as the first line of defense in the innate immune system [1, 2]. These receptors include G protein-coupled receptors (GPCRs) for chemokines (e.g., CXCR1, CXCR2) and complement fragments (e.g., C5aR1), Fc receptors for antibody-coated pathogens, and adhesion molecules like integrins (e.g., Mac-1) and selectins [2, 6]. Activation of these receptors triggers critical functions such as chemotaxis, phagocytosis, degranulation, and the release of neutrophil extracellular traps (NETs) [4, 7]. While vital for host defense, dysregulated activation of these receptors contributes to the pathogenesis of various inflammatory and autoimmune diseases, including ARDS, COPD, and rheumatoid arthritis [1, 8]. Consequently, these receptors are significant therapeutic targets, with drugs like Avacopan (targeting C5aR1) and various CXCR1/2 antagonists being developed or used to modulate neutrophil-mediated tissue damage [5, 8]. However, therapeutic intervention must balance the reduction of pathological inflammation with the potential risk of compromising the patient's ability to fight infections [2, 8]. This entry describes a broad category of receptors rather than a single molecular target, which may lead to challenges in achieving specificity without broad immunosuppression.

Other names

Neutrophil surface receptorsNeutrophil membrane receptorsNeutrophil activation receptorsNeutrophil surface markers

Antagonism of chemokine receptors (e.g., CXCR1/2), inhibition of complement receptors (e.g., C5aR1), and blockade of adhesion molecules to prevent neutrophil recruitment and activation.