Monoclonal antibodies to ciliary glycoproteins of frog olfactory neurons

Zehava Chen, Dov Ophir, Doron Lancet*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Monoclonal antibodies were produced against isolated frog olfactory cilia, a preparation enriched in dendritic extensions of the chemosensory neurons. Two antibodies, 18.1 and 35.6, were found to react against specific glycoproteins of the sensory organelles. These glycoproteins were identified by their differential binding to the lectins wheat germ agglutinin and Concanavalin A. The antibodies fluorescently labeled isolated olfactory cilia, as well as the ciliary surface layer of olfactory epithelium, whose extent was defined by anti-tubulin and anti-keratin antibodies. Respiratory epithelium (or other tissues) as well as isolated respiratory cilia were not labeled by antibodies 18.1 and 35.6, indicating tissue specificity. The olfactory-specific antibodies can be used as markers of the sensory epithelium and of the sensory regions of olfactory dendritic membranes. Antibody 18.1 recognized gp95, a specific and major integral membrane glycoprotein of frog olfactory cilia. Since gp95 has been suggested as candidate olfactory receptor protein (Chen, Z. and Lancet, D., Proc. Natl. Acad. Sci. U.S.A., 84 (1984) 1859-1863), antibody 18.1 could also be useful for functional studies.

Original languageEnglish
Pages (from-to)329-338
Number of pages10
JournalBrain Research
Volume368
Issue number2
DOIs
StatePublished - 19 Mar 1986
Externally publishedYes

Keywords

  • cytoskeletal protein
  • glycoprotein immunofluorescence
  • immunoblotting
  • lectin
  • olfactory cilia
  • sensory neuron
  • tubulin

Fingerprint

Dive into the research topics of 'Monoclonal antibodies to ciliary glycoproteins of frog olfactory neurons'. Together they form a unique fingerprint.

Cite this