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Updated: May 23, 2026
11:10
Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Pro-inflammatory S100A8 and S100A9 proteins: self-assembly into multifunctional native and amyloid complexes
Thomas Vogl1, Anna L Gharibyan2, Ludmilla A Morozova-Roche2
1Institute of Immunology, University of Muenster, Röntgenstr. 21, 48149 Muenster, Germany.
International Journal of Molecular Sciences
|April 11, 2012
Summary
S100A8 and S100A9 proteins, crucial in cellular processes, exhibit diverse functions influenced by their structure and ion binding. Their amyloid-forming capacity may contribute to various diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- S100A8 and S100A9 are EF-hand calcium-binding proteins within the S100 family.
- Abundant in phagocyte cytosol, they regulate cellular motility and danger signaling by interacting with target proteins.
- Elevated S100A8/S100A9 expression is linked to cancer, neurodegenerative diseases, and inflammatory/autoimmune disorders.
Purpose of the Study:
- To review the functional diversity of S100A8/S100A9 proteins.
- To explore the role of their unique chemical and conformational properties, including quaternary structure plasticity.
- To investigate the impact of ion binding on protein conformation, oligomerization, and functional diversification.
Main Methods:
- Literature review focusing on S100A8 and S100A9.
- Analysis of protein structure-function relationships.
- Examination of the influence of calcium (Ca2+) and zinc (Zn2+) binding.
Main Results:
- S100A8/S100A9 exhibit functional diversity driven by their inherent properties and structural plasticity.
- Ion binding (Ca2+, Zn2+) significantly influences protein conformation, oligomerization (dimers, tetramers, etc.), and function.
- These proteins can form amyloid complexes, regulated by ion binding, which compete with native complex formation.
Conclusions:
- The structural plasticity and ion-binding capabilities of S100A8/S100A9 underpin their diverse cellular roles.
- The intrinsic amyloid-forming potential of S100A8/S100A9 may have significant pathological implications in diseases with elevated expression.
- Further research is warranted to fully elucidate the pathological significance of S100A8/S100A9 amyloid depositions.
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