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Odorant-sensitive adenylate cyclase may mediate olfactory reception.

U Pace, E Hanski, Y Salomon

|July 18, 1985

Summary

Researchers identified an odorant-sensitive adenylate cyclase in olfactory sensory neurons. This discovery provides a new method for isolating elusive olfactory receptor proteins and understanding smell.

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Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

The mechanism of smell perception has been debated, with stereospecific protein receptors proposed but not yet identified.
Conventional ligand-binding techniques have faced difficulties in isolating diverse olfactory receptor molecules.
An alternative approach involves studying common transductory components of olfactory receptors.

Purpose of the Study:

To identify a transductory molecular component common to olfactory receptors.
To investigate the role of cyclic nucleotides in olfactory signal transduction.
To provide new strategies for isolating olfactory receptor proteins.

Main Methods:

Identification of an odorant-sensitive adenylate cyclase in isolated dendritic membranes of olfactory sensory neurons.
Characterization of enzyme activation specificity (ligand, tissue, GTP dependence).
Independent identification of olfactory guanine nucleotide-binding proteins (G-proteins) using bacterial toxins.

Main Results:

An odorant-sensitive adenylate cyclase was identified in high concentrations in olfactory sensory neuron membranes.
Enzyme activation demonstrated ligand and tissue specificity, requiring GTP, suggesting G-protein involvement.
The olfactory G-protein was identified and found to be similar to stimulatory G-proteins in other systems.
Cyclic nucleotides are implicated in olfactory transduction, drawing parallels with other sensory systems.

Conclusions:

The findings reveal an odorant-sensitive adenylate cyclase as a key transductory component in olfaction.
The study suggests a molecular analogy between olfactory reception and other signaling pathways (visual, hormonal, neurotransmitter).
This research opens new avenues for identifying and isolating olfactory receptor proteins.

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