Publication: Quantitation and histochemical localization of galectin-1 and galectin-1 -reactive
glycoconjugates in fetal development of bovine organs
Authors
Kaltner, H. ; Lips, K.S. ; Reuter, G. ; Lippert, S. ; Sinowatz, F. ; Gabius, H.J.
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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 display of cellular oligosaccharide
chains is known to undergo marked developmental
changes, as monitored histochemically with plant lectins.
In conjunction with endogenous lectins respective ligand
structures may have a functional role during fetal
development. The assumption of a recognitive,
functionally productive interplay prompts the study of
the expression of a tissue lectin and of lectin-reactive
glycoconjugates concomitantiy. Focusing on comrnon Bgalactosides
as constituents of oligosaccharide chains
and the predominant member of the farnily of galectins
in marnrnals, namely galectin-1, the question therefore is
addressed as to whether expression of lectin and lectinreactive
glycoconjugates exhibits alterations, assessed in
three morphologically defined fetal stages and in adult
bovine organs. Using a sandwich ELISA, the leve1 of the
rather ubiquitous galectin-1 is mostly increased in adult
organs relative to respective fetal stages, except for the
case of kidney. This developmental course is seen rather
seldom, when the amounts of lectin-reactive glycoproteins
or glycolipids are quantitated in solid-phase
assays after tissue homogenization. Western blotting,
combined with probing by labeled galectin-1, discloses
primarily quantitative changes in the reactivity of
individual glycoproteins. Perforrning the same assays on extract aliquots with a plant agglutinin, namely the
galactoside-binding mistletoe lectin, whose fine
specificity is different @m galectin-1, its reduced extent
of binding in solid-phase assays and the disparate profile
of lectin-reactive glycoproteins reveal a non-uniform
developmental alteration within the group of stmctural
variants of B-galactosides. Although sample preparation
can affect ligand preservation andlor presentation and
thus restricts the comparability of biochemical and
histochemical results, especially for soluble reactants,
the histochemical studies on frozen and paraffinembedded
sections of bovine heart, kidney and liver demonstrate that the localization of the galectin and of
lectin-reactive epitopes can show a sirnilar distribution,
as seen in liver and heart, with organ-typical quantitative
changes of a rather similar staining profile (heart,
kidney) or notable changes in the spatial distribution
(liver) in the course of development. This report
emphasizes the potential value of combined monitoring
of the lectin and its potential in vivo ligands to contribute
to eventually unravel organ-related function(s) of a tissue
lectin.
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