Glycosylation Modification: A Key Regulator of Macrophage Polarization and Differentiation

Glycosylation modification plays a role in regulating macrophage polarization and differentiation. Many functionally important molecules on the surface of macrophages are N-glycosylated, including integrins, TNFα receptors (TNFR), TGFβ receptors (TGFβR), CD206, and CD301. Additionally, cell surface sialic acid may regulate the interaction between macrophages and tumor cells. For example, TAMs can induce M1 macrophage polarization and promote inflammation in the tumor microenvironment by binding to sialylated glycosaminoglycans on cancer cells via Siglec-9, thereby reducing tumor growth. [3]

The process of glycosylation modification is involved in regulating the polarization and differentiation of macrophages. Various crucial molecules on the surface of macrophages, such as integrins, TNFα receptors (TNFR), TGFβ receptors (TGFβR), CD206, and CD301, are N-glycosylated. Moreover, the presence of sialic acid on the cell surface may regulate the interaction between macrophages and tumor cells. For instance, TAMs can induce M1 macrophage polarization and promote inflammation in the tumor microenvironment by binding to sialylated glycosaminoglycans on cancer cells via Siglec-9, which leads to reduced tumor growth. [3]

The modification of glycosylation plays a significant role in regulating the polarization and differentiation of macrophages. Many essential molecules on the surface of macrophages, including integrins, TNFα receptors (TNFR), TGFβ receptors (TGFβR), CD206, and CD301, are N-glycosylated. Furthermore, the presence of sialic acid on the cell surface can regulate the interaction between macrophages and tumor cells. For example, TAMs can induce M1 macrophage polarization and promote inflammation in the tumor microenvironment by binding to sialylated glycosaminoglycans on cancer cells via Siglec-9, ultimately resulting in reduced tumor growth. [3]