Protein S100-A12

Also known as: CGRP, Calcium-binding protein in amniotic fluid 1, Calgranulin-C, Extracellular newly identified RAGE-binding protein, Migration inhibitory factor-related protein 6, Neutrophil S100 protein, S100 calcium-binding protein A12, S100A12, P80511

**Mechanism of Action** Protein S100-A12 (Calgranulin-C) is a member of the S100 family of calcium-binding proteins, predominantly expressed in neutrophils and monocytes. Upon calcium binding, it undergoes conformational changes that enable interaction with the receptor for advanced glycation end products (RAGE) and Toll-like receptor 4 (TLR4). This triggers downstream pro-inflammatory signaling cascades, including NF-κB activation, leading to cytokine release (e.g., IL-6, TNF-α) and chemotaxis. Additionally, S100A12 chelates zinc and copper, contributing to antimicrobial activity and modulation of metal-dependent enzymatic processes. **Key Research Findings** Elevated S100A12 levels are documented in inflammatory conditions such as rheumatoid arthritis, inflammatory bowel disease, and sepsis, correlating with disease activity. Experimental studies demonstrate its role in amplifying neutrophil recruitment and oxidative burst. In murine models, S100A12 blockade reduces inflammation and tissue damage. Its extracellular functions as a damage-associated molecular pattern (DAMP) highlight its dual role in host defense and chronic inflammation. **Clinical Relevance** S100A12 is under investigation as a biomarker for inflammatory disease severity and therapeutic target. Serum levels may aid in distinguishing active inflammation from remission in conditions like Crohn’s disease. However, its clinical utility remains experimental, with no approved therapies targeting S100A12. Further research is needed to validate its diagnostic specificity and therapeutic potential. For research purposes only — not medical advice.

Key data

Mechanism of action

S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C.albicans and is also active against E.coli and P.aeruginosa but not L.monocytogenes and S.aureus

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