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High-throughput Analysis of Mammalian Olfactory Receptors: Measurement of Receptor Activation via Luciferase Activity
Published on: June 2, 2014
Identification of a third rat odorant-binding protein (OBP3)
D Löbel1, J Strotmann, M Jacob
1Institute of Physiology, University of Hohenheim, Stuttgart, Germany.
Chemical Senses
|July 28, 2001
Summary
Researchers identified a novel rat lipocalin, OBP3, in the olfactory epithelium. This protein binds odorants with high affinity, suggesting a role in olfaction.
Area of Science:
- Biochemistry
- Molecular Biology
- Olfactory Science
Background:
- Lipocalins are a diverse protein family involved in binding and transporting small hydrophobic molecules.
- Odorant-binding proteins (OBPs) are crucial for olfaction, facilitating odorant transport to olfactory receptors.
Purpose of the Study:
- To isolate and characterize a novel lipocalin from the rat olfactory epithelium.
- To investigate the odorant-binding properties and potential function of the newly identified protein.
Main Methods:
- cDNA library screening and molecular cloning.
- In situ hybridization for expression pattern analysis.
- Heterologous protein expression and spectroscopic binding assays.
- Isothermal titration calorimetry for thermodynamic analysis.
Main Results:
- A lipocalin gene, designated OBP3, was isolated from rat olfactory epithelium cDNA.
- OBP3 exhibited strong expression in nasal glands, similar to rat OBP1.
- Recombinant OBP3 bound fluorescent probes (1-AMA) and competed with high-affinity odorants.
- Thermodynamic parameters of OBP3-odorant interactions were determined.
Conclusions:
- OBP3 is a novel rat odorant-binding protein with characteristics suggesting a role in the olfactory system.
- The protein's nasal expression and demonstrated odorant-binding capabilities support its involvement in olfaction.
