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PMID: 3944087 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Polypeptide gp95. A unique glycoprotein of olfactory cilia with transmembrane receptor properties.

The Journal of biological chemistry ·Vol. 261 ·No. 3 ·1986-01-25 ·Pages 1299-305

Chen Z, Pace U, Ronen D, Lancet D

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
Animals Bufonidae Cattle Chromatography, Affinity Cilia/analysis Electrophoresis, Polyacrylamide Gel Glycopeptides/metabolism Isoelectric Point Membrane Proteins/analysis Neurons, Afferent/analysis Olfactory Bulb/cytology Rana ridibunda Rats Rats, Inbred Strains
Chemicals
Glycopeptides Membrane Proteins glycopeptide gp95
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chen Z
Pace U
Ronen D
Lancet D
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1986-01-25
Pages
1299-305
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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