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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
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Exploring the glycosaminoglycan-protein interaction network by glycan-mediated pull-down proteomics
Bernd Gesslbauer1, Rupert Derler1, Claudia Handwerker2
1Institute of Pharmaceutical Sciences, University of Graz, Graz, Austria.
Electrophoresis
|March 13, 2016
Summary
This study identified 458 human glycosaminoglycan (GAG) binding proteins, revealing distinct binding specificities and affinities within the human plasma proteome. The findings expand our understanding of GAG-protein interactions in mammalian biology.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Glycosaminoglycans (GAGs) are crucial sulfated polysaccharides involved in diverse cellular functions.
- The human GAG-binding proteome remains largely unexplored, limiting understanding of GAG-mediated biological processes.
Purpose of the Study:
- To comprehensively investigate the human GAG-binding proteome from various sources.
- To characterize the GAG-binding selectivity and affinity of human plasma proteins.
Main Methods:
- Proteins were affinity-purified using immobilized low molecular weight heparin, heparan sulfate, and dermatan sulfate.
- Protein identification was performed using nano-liquid chromatography-tandem mass spectrometry (nano-LC/MS²).
- Differential binding and elution studies were employed to assess specificity and affinity.
Main Results:
- Identified 458 human GAG-binding proteins, including novel binders.
- Demonstrated distinct GAG-binding specificities and affinities within the human plasma proteome.
- Differentiated proteins binding to all GAG classes versus those with selective binding.
Conclusions:
- The developed method effectively identifies GAG-binding proteins and compares subproteomes.
- This work significantly expands the known human GAG-binding proteome.
- Findings provide a foundation for understanding GAG-protein interactions in various biological contexts.
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