A PUTATIVE LIPOPHILIC STIMULANT CARRIER PROTEIN COMMONLY FOUND IN THETASTE AND OLFACTORY SYSTEMS - A UNIQUE MEMBER OF THE PHEROMONE-BINDING PROTEIN SUPERFAMILY
M. Ozaki et al., A PUTATIVE LIPOPHILIC STIMULANT CARRIER PROTEIN COMMONLY FOUND IN THETASTE AND OLFACTORY SYSTEMS - A UNIQUE MEMBER OF THE PHEROMONE-BINDING PROTEIN SUPERFAMILY, European journal of biochemistry, 230(1), 1995, pp. 298-308
In chemosensory systems, a variety of lipophilic ligand-binding protei
ns have been found in saliva or nasal mucus. Lipophilic stimulants rea
ch 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 lig
and-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 distri
butions, cDNA sequences and structural features, we concluded that the
se proteins belong to a unique subfamily whose members have convergent
ly 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 natura
l foods in taste systems as well as in olfactory systems.