Study of S100A4 Protein Variants and Their Modifications
Author Information
Author(s): Haugen Mads H, Flatmark Kjersti, Mikalsen Svein-Ole, Malandsmo Gunhild M
Primary Institution: Norwegian Radium Hospital, Rikshospitalet University Hospital
Hypothesis
Can posttranslational modifications of S100A4 affect its localization and function?
Conclusion
S100A4 exists in several charge variants due to posttranslational modifications, which are present across different tissues and cellular compartments.
Supporting Evidence
- S100A4 was found in multiple forms across different tissues.
- Charge variants of S100A4 were confirmed by mass spectrometry.
- Similar patterns of S100A4 were observed in both cancerous and normal cells.
Takeaway
The S100A4 protein can change its form in different ways, which might help it do different jobs in the body.
Methodology
S100A4 was isolated from various sources and analyzed using 2D-PAGE and mass spectrometry.
Limitations
The specific posttranslational modifications of S100A4 were not identified.
Participant Demographics
Colorectal cancer patients with varying TP53 status.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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