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Granulocyte surface proteins refer to a diverse group of proteins expressed on the plasma membrane of granulocytes, including neutrophils, eosinophils, and basophils [1, 5]. This category encompasses various functional molecules such as adhesion molecules (e.g., CD11b/CD18), Fc receptors (e.g., CD16, CD32, CD64), and lineage-specific antigens (e.g., CD66b, CD15, CD177) [2, 5]. These proteins are essential for the innate immune response, mediating processes such as cell activation, adhesion to vascular endothelium, chemotaxis toward inflammatory sites, and phagocytosis of pathogens [4, 5]. In clinical pharmacology, these proteins are primarily targeted by radiolabeled monoclonal antibodies, such as Besilesomab and Sulesomab, which bind to CD66 antigens to image infections and inflammatory foci [1, 2]. Additionally, receptors like the Granulocyte colony-stimulating factor receptor (G-CSFR) are targeted by drugs like Filgrastim to stimulate neutrophil production [5]. They also serve as vital biomarkers for immunophenotyping and are involved in the pathogenesis of conditions like Transfusion-Related Acute Lung Injury (TRALI) [4]. While not a single therapeutic target, the detection and modulation of these surface proteins are central to the diagnosis and management of inflammatory and hematologic disorders [1, 3].
Binding to specific surface antigens (e.g., CD66b, CD66c, CD15) on granulocytes to facilitate diagnostic imaging of inflammatory sites, or activation of specific receptors (e.g., G-CSFR, GM-CSFR) to stimulate granulocyte production and function.
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