Résumé
Salivary proteome patterns of healthy volunteers (n = 12) were compared before and after they tasted bitter solutions made of either urea (0.36M) or quinine-hydrochloride (40 µM). Relative abundance of 22 and 18 spots was modified 15 min after stimulation by urea and quinine, respectively. Only two spots were common to both tastants, indicating a molecule-specific response. Proteins, relative quantity of which was altered, were agents of the oral cavity defense (e.g., thioredoxin, cystatin, parotid secretory proteins, etc.) and markers of inflammation (transthyretin and transferrin) or enzymes. In particular, the relative abundance of carbonic anhydrase VI, a protein previously described as crucial to taste function, declined after tasting the urea solution.