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Published on: August 10, 2013
Internalization of odorant-binding proteins into the mouse olfactory epithelium
1Institute of Physiology, University of Hohenheim, Stuttgart, Germany. strotman@uni-hohenheim.de
Odorant-binding proteins (OBPs) carrying odorants are rapidly internalized by sustentacular cells in the nose. This uptake is mediated by the low-density lipoprotein receptor 2 (Megalin), clearing odorants efficiently.
Area of Science:
- Olfactory system biology
- Cellular transport mechanisms
- Chemosensation research
Background:
- Vertebrate odor detection relies on olfactory neurons and odorant-binding proteins (OBPs) in nasal mucus.
- Rapid clearance of odorants is crucial for sustained olfactory receptor responsiveness.
Purpose of the Study:
- To investigate the cellular fate and clearance mechanisms of OBP/odorant complexes in the olfactory epithelium.
- To identify the molecular transporters involved in OBP uptake.
Main Methods:
- Fluorescently labeling recombinant OBPs and applying them to mouse noses.
- Utilizing cell lines expressing candidate transporters for in vitro uptake studies.
- Employing Megalin inhibitors to assess transporter function.
Main Results:
- Fluorescently labeled OBPs were rapidly internalized into sustentacular cells, specifically when bound to odorants.
- The low-density lipoprotein receptor 2 (Megalin) was identified as a key transporter in sustentacular cells.
- Megalin inhibition blocked OBP/odorant complex uptake in both cell lines and the olfactory epithelium.
Conclusions:
- Megalin-mediated internalization into sustentacular cells is a primary mechanism for rapid, local clearance of OBP/odorant complexes.
- This process is vital for maintaining olfactory sensitivity and function.
- The findings elucidate a novel cellular pathway in odorant clearance.
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