Open AccessA Putative Lipophilic Stimulant Carrier Protein Commonly Found in the Taste and Olfactory Systems
Author(s) -
Ozaki Mamiko,
Morisaki Kazuyo,
Idei Wataru,
Ozaki Koichi,
Tokunaga Fumio
Publication year - 1995
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1995.0298i.x
Subject(s) - odorant binding protein , taste , biology , olfaction , drosophila melanogaster , insect , subfamily , biochemistry , g protein coupled receptor , olfactory system , taste receptor , ligand (biochemistry) , olfactory receptor , manduca sexta , receptor , microbiology and biotechnology , gene , botany , neuroscience
In chemosensory systems, a variety of lipophilic ligand‐binding proteins have been found in saliva or nasal mucus. Lipophilic stimulants reach the receptor membrane, carried by these proteins. An acidic 14‐kDa protein purified in the blowfly, Phormia regina , belongs to the insect pheromone‐binding protein superfamily, but unlike other lipohilic ligand‐binding proteins in insect or vertebrate chemosensory systems, it was distributed in both taste and olfactory organs. A similar protein was also isolated in Drosophila melanogaster. Considering their distributions, cDNA sequences and structural features, we concluded that these proteins belong to a unique subfamily whose members have convergently evolved for a common function required for both senses of taste and olfaction. By an electrophysiological experiment using antiserum, we also suggested that these proteins carry fragrant components of natural foods in taste systems as well as in olfactory systems.