Confocal evaluation of native and induced lectin binding contributes to discriminate between lingual gland glycocomponents in quail

• Bondi, A.M. ^[1] ; Gabrielli, M.G. ^[1] ; Accili, Daniela ^[1] ; Sabbieti, M.G. ^[1] ; Menghi, Giovanna ^[1]
  1. [1] Università di Camerino

     Università di Camerino

     Camerino, Italia

     
• Localización: Histology and histopathology: cellular and molecular biology, ISSN-e 1699-5848, ISSN 0213-3911, Vol. 15, Nº. 4, 2000, págs. 1119-1125
• Idioma: inglés
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  • A confocal analysis was performed on the qu ail (Co turnix coturnix japonica) lingual sa li va ry glands where the carbohydrate chains were studied by lectin histochemistry. Fo r this purpose, appropri ate FITC- and T RITC-conjugates we re used for doubl e binding also accomplished with sialidase digestion. The glycosidi c components of the qu ail lingual sa liva ry glands were fo und to be heterogeneously distributed on the different secretory structures as well as on the single secretory e lements of each adenomere. The rostra l portion of the anterior lingual gland was found to only secrete neutral glycocomponent , c harac te ri zed by terminal B-galactose, N-acetylgalactosamine and fucose residues in contrast to the caudal portion that was shown to be extremely heterogeneous and to produce sialylated glycoconjugates characterized by the terminal sequences sialic acid-B-ga lactose-N- ace tylgalactosamine, sialic acid-B-galactose-N-acetylglucosamine, and sialic acido.-N-acetylga lactosamine partl y codistributed within secretory adenomeres. The posterior lingual gland was observed to be the major contributor to the secretion of salivary mucins containing sialoglycoconjuga tes with terminal sialic acid residues linked to B-galactose-Nacetylgalactosamine or o.-N-acetylgalactosamine often located in distinct secretory elements