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The Peptidoglycan recognition protein 1–S100 calcium-binding protein A4 complex (Tag7–Mts1) is a secreted heterodimeric protein complex that plays a significant role in the innate immune system's anti-tumor activity (Sashchenko et al., 2004, J Biol Chem). It consists of Tag7 (PGLYRP1), a protein that recognizes bacterial peptidoglycans, and Mts1 (S100A4), a member of the S100 family involved in cell motility (UniProt O75594, P26447). This complex is produced by monocytes and natural killer (NK) cells and acts as a ligand for the Tumor Necrosis Factor Receptor 1 (TNFR1) (Yarovaya et al., 2021, Int J Mol Sci). Unlike TNF-alpha, the Tag7–Mts1 complex triggers apoptosis in target cells through TNFR1 without activating the NF-kappaB survival pathway, potentially offering a more direct apoptotic signal (Georgiev et al., 2013, Cell Cycle). Furthermore, the complex functions as a chemoattractant for immune effector cells, facilitating their migration to tumor sites (Dukhanina et al., 2009, Dokl Biol Sci). Its dual capacity to induce cell death and recruit immune cells makes it a promising candidate for cancer immunotherapy research.
Induction of apoptosis via TNFR1 binding and chemoattraction of immune effector cells
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