On the existence of receptors to the pheromonal steroid, 5α‐androst‐16‐en‐3‐one, in porcine nasal epithelium

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Abstract
The binding of the odorant, 5α‐androst‐16‐en‐3‐one, to porcine nasal tissues, has been investigated using methods normally employed for studying both cytosolic and membrane‐bound receptors. 5α‐Androst‐16‐en‐3‐one was generally taken up more avidly by homogenates of olfactory (nervous) tissue than by respiratory tissue, but binding to the former was only partially prevented by prior heating or by excess ligand, suggesting some degree of specific binding. At low protein concentration, saturable binding was noted but these data were not reproducible. The binding of a non‐odorant, DHA, was only 2% that of 5α‐androst‐16‐en‐3‐one. Using agarose gel electrophoresis, some evidence was obtained for binding protein(s) to the odorous 16‐adrostene in porcine respiratory tissues, that were absent from previously heated tissue. Experiments with SDS‐treated, or cell‐membrane‐enriched preparations, of nasal epithelium did not show improved binding of 5α‐androst‐16‐en‐3‐one. We conclude that the extreme hydrophobicity of 5α‐androst‐16‐en‐3‐one is probably responsible for the high degree of non‐specific binding noted and for variability in results. This is discussed in relation to other known odorous ligand/receptors in olfactory tissue, particularly that of 5α‐androstan‐3‐one [10].