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Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Pathologies involving the S100 proteins and RAGE
C W Heizmann1, G E Ackermann, A Galichet
1Division of Clinical Chemistry and Biochemistry, Department of Pediatrics, University of Zurich, Switzerland. Claus.Heizmann@kispi.unizh.ch
Sub-Cellular Biochemistry
|January 16, 2008
Summary
S100 proteins, a large family of calcium-binding proteins, function in diverse cellular processes and can be secreted to interact with RAGE. Their dysregulation is linked to diseases like cancer and inflammation, making them potential therapeutic targets.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- S100 proteins are the largest subgroup of EF-hand calcium-binding proteins, characterized by unique N-terminal pseudo EF-hands.
- They typically form homodimers or heterodimers, with conformational changes upon calcium binding exposing hydrophobic surfaces for target interaction.
Purpose of the Study:
- To review recent developments in S100 protein biological functions.
- To discuss S100-specific mouse models for human disease research.
- To explore the S100-RAGE interaction and its downstream cellular pathways.
Main Methods:
- Literature review of S100 protein research.
- Analysis of S100 gene organization and expression patterns.
- Examination of S100 protein oligomerization and metal ion binding properties.
Main Results:
- S100 proteins exhibit diverse functions, including extracellular activities via RAGE, acting as cytokines/chemokines.
- Oligomeric forms (hexamers, tetramers, octamers) are proposed as active extracellular species.
- S100 gene cluster on chromosome 1q21 is frequently rearranged in cancer.
Conclusions:
- S100 proteins are implicated in cardiomyopathy, cancer, inflammation, and brain diseases.
- Their roles in disease highlight their diagnostic potential and therapeutic value.
- Further research into S100-RAGE interactions and disease models is crucial for developing novel therapies.
