title: Polypeptide gp95. A unique glycoprotein of olfactory cilia with transmembrane receptor properties.
abstract: Polypeptide gp95 is a major glycoprotein present in preparations of isolated ciliary extensions from frog olfactory sensory neurons (Chen, Z., and Lancet, D. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 1859-1863). We report here that gp95 is distinct among the ciliary polypeptides in having several properties that make it a plausible receptor candidate: it is specific to olfactory cilia, it has the appropriate bilayer density, and it is a transmembrane protein. Polypeptide gp95 has a uniquely high content of complex type oligosaccharides compared to other ciliary glycoproteins, a property which is used for its partial purification and can also serve as a probe for functional identification. The present biochemical characterization of frog gp95 and of its putative homologs from other species may open the way to a future assignment of its role in chemosensory reception.
mesh_terms: D000818:Animals; D002025:Bufonidae; D002417:Cattle; D002846:Chromatography, Affinity; D002923:Cilia / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006020:Glycopeptides / Q000378:metabolism*; D007526:Isoelectric Point; D008565:Membrane Proteins / Q000032:analysis; D009475:Neurons, Afferent / Q000032:analysis; D009830:Olfactory Bulb / Q000166:cytology*; D011895:Rana ridibunda; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D006020:Glycopeptides; D008565:Membrane Proteins; C047800:glycopeptide gp95