Publication: Nuclear and cytoplasmic lectin receptor sites in rat Pyla osteoblasts
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Date
2000
Authors
Sabbieti, M.G. ; Marchetti, L. ; Hurley, M.H. ; Menghi, Giovanna
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
The intracellular distribution of lectin
receptor sites was studied in the rat Pyla osteoblasts
using immunofluorescence at the confocal microscopy
level. This immortalized cell line was found to represent
a satisfactory model to study the occurrence and
distribution of sugar moieties. Our data showed distinct
affinity patterns of lectins recognizing different terminal
or internal sugar residues. For some lectins, the binding
patterns appeared to be cell cycle-independent, whereas
for PNA the cell cycle greatly influenced the nuclear
binding. By combining lectin affinity with sialidase
degradation and alcoholic saponification the sialic acid
acceptor sugars and derivatives were also visualized. In
particular, glycoconjugates with sialic acids linked to Bgalactose,
and mainly C4 acetylated, were located in the
cytoplasm, while glycoconjugates characterized by sialic
acids linked to a-N-acetylgalactosamine, and devoid of
acetyl groups at C4, were almost exclusively found in
the nucleus. The comparison of lectin affinities, with and
without prior glycosidase digestions, allowed us to gain
further insight into the chemical composition of
glycoconjugates that act as the lectin receptor sites that
appeared to belong to 0- and N-linked glycoconjugates.
The use of additional enzymatic treatments were useful
to better establish the localization of nuclear receptor
sites and results were compared with previous studies
about endogenous and exogenous lectins in an attempt to
reconcile the association of lectins and sugars within the
nucleus and their possible involvement in modulation of
cell proliferation andlor response to chemical signals. The above digestions also provided information about
the cytoplasmic binding patterns.
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