Publication: Human galectin-2: expression profiling by RT-PCR/immunohistochemistry and its introduction
as a histochemical tool for ligand localization
Authors
Saal, I. ; Nagy, N. ; Lensch, M. ; Lohr, M. ; Manning, J.C. ; Decaestecker, C. ; André, S. ; Kiss, R. ; Salmon, I. ; 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
Sugar-encoded information of glycoconjugates
is translated into cellular responses by
endogenous lectins. Galectins stand out against other
lectin families due to their wide range of functions
including cell adhesion, tissue invasion or growth
regulation exerted at extracellular, membrane,
cytoplasmic and nuclear sites. This remarkable
versatility warrants close scrutiny of their emerging
network, in this study with focus on homodimeric
human galectin-2. We first detected presence of specific
mRNA in various tissue types by processing post
mortem and surgical specimens by RT-PCR protocols.
Overlap of gene expression was noted with proto-type
galectins-1 and -7 and also family members from the
other two subgroups. To monitor expression on the level
of protein a polyclonal anti-galectin-2 antibody was
raised. Immunopositivity was semi-quantitatively
assessed in sections of 209 human samples establishing
an array both of normal tissues and samples with
inflammation or benign/malignant growth. In general,
positivity was predominantly epithelial without
restriction of staining to certain tissue types, as fittingly
indicated by our RT-PCR analysis. Staining was not limited to the cytoplasm but also included nuclear sites.
To examine the suitability of the labeled lectin as a
histochemical probe we biotinylated galectin-2 under
activity-preserving conditions and introduced it to tissue
profiling. Specific cytoplasmic staining proved the
validity of the concept. Our results encourage systematic
histopathologic studies by immuno- and lectin
histochemistry, especially by adding galectin-2 as study
object to galectin fingerprinting which has already
yielded prognostic information on galectins-1, -3, -4 and
-8 and hereby contributed to define functional
overlap/divergence in this lectin family.
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