Expression of the putative pheromone and odorant transporter vomeromodulin mRNA and protein in nasal chemosensory mucosae.
In nasal chemosensory systems, glandular proteins associated with the vomeronasal and olfactory epithelia perform specific perireceptor functions associated with sensory transduction. Vomeromodulin, a recently identified glycoprotein synthesized by the lateral nasal glands, is proposed to be a pheromone transporter (Khew-Goodall et al., FASEB J 5:2976-2982, 1991). In our study, we have investigated its expression in vomeronasal, olfactory, and respiratory nasal mucosae of rats and humans using in situ hybridization and immunocytochemical techniques. In the rat, vomeromodulin mRNA and protein were localized abundantly in the glandular acini of the maxillary sinus component of the lateral nasal glands. In addition, the vomeronasal and posterior glands of the nasal septum also expressed vomeromodulin mRNA and protein. Vomeromodulin immunoreactivity was localized extracellularly in the mucus of the sensory and non-sensory epithelia of the vomeronasal organ, and in the mucociliary complex of the olfactory, respiratory, and associated nasal epithelia. In human nasal mucosae, vomeromodulin immunoreactivity was localized in the mucociliary complex of the vomeronasal and respiratory epithelia. Comparison of the localization of vomeromodulin with that of odorant-binding protein, which is also synthesized in the lateral nasal glands of rats, revealed that odorant-binding protein was expressed in a completely separate glandular region, namely the ventral component. In the septal glands, vomeromodulin was expressed in the posterior glands whereas odorant-binding protein was localized in the anterior glands. Odorant-binding protein immunoreactivity was not observed in the vomeronasal glands. In contrast, both proteins were localized in the mucus of vomeronasal, olfactory, and respiratory epithelia. Our results suggest that vomeromodulin, like odorant-binding protein, functions as a chemosensory stimulus transporter associated with perireceptor processes in vomeronasal and olfactory transduction.
Krishna
N S
NS
Department of Physiology, (M.L.G., T.V.G.), University of Kentucky College of Medicine, Lexington, 40536.
Getchell
M L
ML
Getchell
T V
TV
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D004847:Epithelial Cells; D004848:Epithelium / Q000378:metabolism; D005088:Exocrine Glands / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis*; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D036341:Intercellular Signaling Peptides and Proteins; D026901:Membrane Transport Proteins; D009093:Mucus / Q000378:metabolism; D009831:Olfactory Mucosa / Q000378:metabolism*; D012333:RNA, Messenger / Q000096:biosynthesis*; D051381:Rats; D017207:Rats, Sprague-Dawley; D018035:Receptors, Odorant / Q000096:biosynthesis / Q000235:genetics; D015398:Signal Transduction / Q000502:physiology
D002352:Carrier Proteins; D006023:Glycoproteins; D036341:Intercellular Signaling Peptides and Proteins; C092201:LOC690507; D026901:Membrane Transport Proteins; D012333:RNA, Messenger; D018035:Receptors, Odorant; C045648:odorant-binding protein