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Updated: Jul 5, 2026
12:55
Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation
Published on: September 29, 2019
Human S100A12: a novel key player in inflammation?
Jens Pietzsch1, Susan Hoppmann
1Department of Radiopharmaceutical Biology, Institute of Radiopharmacy, Research Center Dresden-Rossendorf, POB 51 01 19, 01314 Dresden, Germany. j.pietzsch@fzd.de
Amino Acids
|April 30, 2008
Summary
S100A12, a calcium-binding protein, is overexpressed in inflammatory diseases. Its interaction with RAGE suggests S100A12 is a promising diagnostic marker for localized inflammation.
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- S100A12 is an EF-hand calcium-binding protein predominantly secreted by neutrophils.
- It functions intracellularly as a homodimer and extracellularly with cytokine-like properties, playing a role in innate immunity and autoimmune reactions.
Purpose of the Study:
- To investigate the role of S100A12 in inflammatory processes.
- To explore the diagnostic potential of S100A12 in various disorders.
Main Methods:
- The study focuses on the expression, structure, and interactions of S100A12.
- Emphasis is placed on its interaction with the receptor for advanced glycation endproducts (RAGE) and its soluble form (sRAGE).
Main Results:
- S100A12 is markedly overexpressed in inflammatory conditions.
- Elevated serum S100A12 levels are observed in inflammatory, neurodegenerative, metabolic, and neoplastic disorders.
- The interaction between calcium-activated S100A12 and RAGE is a key pathogenetic factor.
Conclusions:
- S100A12 plays a significant role in the pathogenesis of various diseases.
- S100A12 demonstrates high potential as a sensitive and specific diagnostic marker for localized inflammatory processes.
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