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Updated: May 4, 2026
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Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation
Published on: September 29, 2019
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Membrane interactions of S100A12 (Calgranulin C)
Assuero F Garcia1, José L S Lopes2, Antonio J Costa-Filho1
1Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brasil ; Departamento de Física, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brasil.
Plos One
|December 25, 2013
Summary
Porcine S100A12 protein interacts with cell membranes, with its structure and binding significantly altered by calcium and zinc ions. This research clarifies protein-lipid interactions in inflammatory processes.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- S100A12 (Calgranulin C) is an acidic calcium-binding protein found in macrophages and lymphocytes, upregulated in inflammatory diseases.
- In pigs, S100A12 is abundant in granulocytes, modulating inflammatory signals.
- Understanding its membrane interactions is crucial for inflammatory disease research.
Purpose of the Study:
- Investigate porcine S100A12 interaction with phospholipid bilayers.
- Determine the effect of Ca(2+) and Zn(2+) ions on protein-lipid interactions.
- Analyze conformational changes and lipid preferences of S100A12.
Main Methods:
- Synchrotron radiation circular dichroism (SRCD) spectroscopy.
- Fluorescence spectroscopy.
- Surface plasmon resonance (SPR).
Main Results:
- Porcine S100A12 interacts with both lipids and ions.
- The presence of Ca(2+) and Zn(2+) ions modifies protein binding, conformation, and thermal stability with lipids.
- Combined ions and lipids induce specific conformational changes in S100A12.
Conclusions:
- S100A12 exhibits ion-dependent interactions with phospholipid bilayers.
- These findings enhance understanding of S100A12's role in inflammatory processes.
- The study complements existing crystal structure data with dynamic interaction insights.
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