Acta Histochemica · 2022 · 17 citations · 21 references
Life SciencesBiochemistryMolecular BiologyCarbohydrate BiochemistryGlycobiologyImmunotechnologyCell-surface GlycansGlycan AnalysisGlycan StructureGlycan-protein InteractionsGlycosylation PathwaysImmunohistochemistryGlycosylation AnalysisLectin Binding SpecificityLectin-based Glycan AnalysisLectin-carbohydrate InteractionsLectinsNasal-associated Lymphoid TissueRespiratory Tract AnatomyVomeronasal System
Lectins are naturally occurring molecules which bind to specific carbohydrates of glycoconjugates. The binding specificity of lectins can therefore be used to specifically elucidate the glycosylation pattern in various tissues. While lectin histochemistry is usually carried out manually on single slides, a fully automated immunostaining system offers an easy, standardized, and high throughput system. In this study lectin histochemistry was implemented and optimized on a fully automated immunostaining system to investigate glycosylation patterns in the murine respiratory tract and the primary olfactory pathway. We tested 22 commercially available biotinylated lectins for their labelling-profiles to specifically identify morphologic structures. The results showed that lectin staining profiles using the implemented protocol on the automated system were constant and suitable for high throughput morphological studies. Further, the morphological evaluation of the stained slides revealed a complete characterization of the murine respiratory tract and primary olfactory pathway including the lectin binding profiles for the olfactory bulb, the vomeronasal organ and the nasal-associated lymphoid tissue.
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Carbohydrate–Aromatic Interactions in Proteins
Kieran L. Hudson, Gail J. Bartlett, Roger C. Diehl et al. · Journal of the American Chemical Society · 2015 · 412 citations · Full text
Kenji Kondo, Keigo Suzukawa, Takashi Sakamoto et al. · The Journal of Comparative Neurology · 2010 · 93 citations