Publication: Correspondence of gradual developmental increases of expression of galectin-reactive glycoconjugates with alterations of the total contents of the two differentially
regulated galectins in chicken intestine and liver as
indication for overlapping functions
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Date
1999
Authors
Lips, K.S. ; Kaltner, H. ; Reuter, G. ; Stierstorfer, B. ; 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 duplication of genes for recognition
molecules and the ensuing diversification of the
members of such families generate complex groups of
homologous proteins. One example are galactosidespecific
lectins whose sequences display constant
features related to sugar binding, the galectins. Based on
the inverse abundance of the chicken galectins CG-14
and CG-16 in adult intestine and liver, these two lectins
represent a model to comparatively study expression of
the related proteins and the galectin-reactive sites
(glycoproteins and glycolipids) biochemically and
histochemically. Functional overlap andtor acquisition of
distinct functions would be reflected in qualitative
andlor quantitative aspects of ligand display. Using five
different stages of embryogenesis, differential regulation
of the two galectins was detected in liver and intestine.
The clear preference for one galectin (CC-14) was
observed in intestine already at rather early stages,
whereas equivalence for both proteins was noted in liver
from day 12 to day 18 prior to hatching, as seen by
ELISA assays and Western blot analysis. Presentation of
galectin-reactive glycoproteins showed a tendency for
gradual increase in both organs. Galectin-blotting
analysis revealed primarily very similar patterns of
positive bands at the different stages of development and
only few quantitative and qualitative changes. The
reactivity of glycolipids in a solid-phase assay was more
variable, even surpassing the response of extracts of the
adult organ at several embryonic stages. While the
localization patterns of the galectins and galectinreactive
sites were nearly indistinguishable in the liver,
intestinal tissue differed with respect to the placement and accessibility of binding sites. Thus, the results
suggest a differential regulation of galectin activities in
the two organs. As a sum they resemble the course of
development of availability of glycoprotein ligands in
vitro. These findings support the notion for a partial
functional redundancy in this family. The described
approach to employ galectin-specific antibodies and the
labeled galectins as tools to assess presentation of
ligands is suggested to be of general relevance to address
the question of distinct vs. overlapping functions of
related recognition molecules.
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