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Updated: Aug 18, 2025
07:48
Tracking Drug-induced Changes in Receptor Post-internalization Trafficking by Colocalizational Analysis
Published on: July 3, 2015
8.8K
Molecular methods to study protein trafficking between organs.
Felix K Kreissl1, Michael A Banki2, Ilia A Droujinine2
1Department of Immunology and Microbiology, Scripps Research, La Jolla, California, USA.
Proteomics
|December 8, 2022
Summary
This study introduces a novel method for tracking secreted proteins in vivo, identifying their origins and destinations. This advance in protein secretion analysis aids in understanding organismal homeostasis and disease pathologies.
Area of Science:
- Biochemistry
- Molecular Biology
- Physiology
Background:
- Interorgan communication is vital for homeostasis, but dysregulation links to pathologies.
- Proteomics identifies circulating proteins but not their tissue origins or destinations.
- In vitro methods for studying protein secretion lack in vivo complexity.
Purpose of the Study:
- To develop a method for identifying the tissue of origin and destination of secreted proteins in vivo.
- To overcome limitations of current proteomics and in vitro techniques for studying secreted proteins.
- To enable the study of low-abundance hormone proteins.
Main Methods:
- Utilized engineered promiscuous BirA* biotin ligase derivatives for in vivo protein tagging.
- Employed biotin as a molecular tag to label secreted proteins within specific tissues.
- Developed a method for tissue-specific labeling of cellular secreted proteomes.
Main Results:
- Successfully enabled tissue-specific tagging of secreted proteomes in vivo.
- Demonstrated that biotin tagging provides information on protein origin and destination.
- Facilitated the enrichment of low-abundance hormone proteins.
Conclusions:
- Promiscuous protein biotinylation is a powerful tool for in vivo secreted protein analysis.
- This technique enhances the understanding of interorgan communication and its role in health and disease.
- Offers a novel approach to investigate the complex secretome in a physiological context.
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