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Updated: Aug 14, 2026

Whole Mount Dissection and Immunofluorescence of the Adult Mouse Cochlea
Published on: January 1, 2016
Wheat germ agglutinin and Helix pomatia agglutinin lectin binding on cochlear hair cells
1INSERM-U.254, C.H.R., Hopital de St. Charles, Montpellier, France.
Abstract:
The fluorescein labelled lectins FITC-WGA and FITC-HPA were used to identify specific carbohydrates in cochlear hair cells. Wheat germ agglutinin (WGA) bound with the cell coat of both inner and outer hair cells (IHC and OHC) suggesting the presence of either N-acetyl-D-glucosamine or sialic acid. In contrast, glycoconjugates with terminal N-acetyl-D-galactosamine residues that bind with Helix pomatia agglutinin (HPA), were demonstrated inside the plasma membrane of outer hair cells. WGA and HPA lectin binding implies the presence of anionic glycoconjugates that furnish added negative charge on the membranes to which they are fixed. The presence of sialic acid or N-acetyl-D-glucosamine on the extracellular surface of cochlear hair cell plasma membrane is consistent with the normal distribution of these glycoconjugates in the cell coat. The presence of the membrane associated oligosaccharide N-acetyl-D-galactosamine within the outer hair cell is inconsistent with the distribution of glycoproteins in internal membrane systems of other cell types.
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