Please use this identifier to cite or link to this item: http://hdl.handle.net/10201/18725

Title: Mosaic lectin labelling in the quail collecting ducts
Issue Date: 22-Feb-2011
Publisher: Murcia : F. Hernández
ISSN: 0213-3911
Related subjects: CDU::5 - Ciencias puras y naturales::57 - Biología
Keywords: Quail
Kidney
Abstract: -Morphological and histoenzymological differences have been observed between intercalated and principal cells of the quail Coturnix coturnix japonica collecting ducts. The present study was designed to shed light on the lectin affinity of the collecting duct cells within cortex and medulla by the use of HRP-labelled lectins combined with glycosidase degradation. Binding of PNA and RCA-1 lectins consequent to enzymatic release of sialic acid revealed abundant sialylated carbohydrate moieties within the principal cell cytoplasm. This characteristic binding pattern differed considerably from the staining observed in the intercalated cells. Interesting information also emerged about the presence of sialoglycoconjugates having the terminal disaccharide sialic acid-B-N-acetylgalactosamine originating from the increased SBA binding and the unmodified DBA labelling after removal of sialic acid. Sequential degradation by sialidase1B-galactosidase followed by incubation with DBA offered the possibility to suspect that the receptor sugar for the penultimate Bgalactose may be N-acetylgalactosarnine. Conversely, we were not able to define the acceptor sugar for penultimate B-GalNAc owing to the lack of availability of B-N-acetylgalactosaminidase enzyme. When although further studies are clearly needed to elucidate the physiological role of the cellular sialoglycoconjugates detected, the present results already provide valuable insight into the carbohydrate composition of intercalated and principal cells in the quail collecting ducts.
Primary author: Menghi, Giovanna
Gabrielli, M.G.
Accili, Daniela
Published in: Histology and histopathology
URI: http://hdl.handle.net/10201/18725
Document type: info:eu-repo/semantics/article
Number of pages / Extensions: 8
Rights: info:eu-repo/semantics/openAccess
Appears in Collections:Vol.10, nº 2 (1995)

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