Title:
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The molecular basis of thiol odorant sensitivity in the mammalian olfactory system
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This thesis is an investigation into the potential mechanisms that could explain the
olfactory sensitivity to thiol compounds ~ought to be conserved across mammalian
species. Proteomics techniques were employed as unbiased tools to search for highly
conserved proteins in olfactory cilia theoretically capable of strong interactions with thiol
odorants. Comparisons of the protein profiles and directed protein labelling studies of
olfactory cilia from three mammalian species - the house mouse (Mus musculus), the rat
(Rattus norvegicus) and the sheep (Ovis aries) - and respiratory cilia preparations from
the rat enabled the identification of cytoskeletal proteins and olfactory receptors as
potential targets for sulphydryl-mediated thiol odorant interactions. It is therefore
predicted that olfactory detection of thiol odorants utilises a traditional olfactory receptor
conserved across mammalian. species, the observed thiol sensitivity potentially a byproduct
of a strong interaction between odorant and receptor.
This study also represents the first broad ranging study of the protein complement
of mammalian olfactory cilia derived from the three model species. The characterisation
of olfactory and respiratory cilia proteomes from multiple mammalian species has
highlighted a novel family of putative pheromone binding proteins uniquely associated
with mouse olfactory cilia preparations. It has also provided further evidence for the
ongoing investigations of the functions of odorant-binding proteins and annexins.
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