Publication: Sertoli cell expression of galectin-l and -3 and accessible binding sites in normal human testis and Sertoli cell only-syndrome
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Date
1999
Authors
Wollina, U. ; Schreiber, G. ; Görnig, M. ; Feldrappe, S. ; Burchert, M. ; 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
Galectins are vertebrate lectins interacting
with B-galactosides and derivates thereof such as blood
group A, B and H determinants. The expression of
galectin-l and -3 and galectin-specific binding sites by
human Sertoli cells was analyzed in normal human testis
and Sertoli cell only-syndrome (SCOS). Staining
intensity was scored semiquantitatively on a 4-grade
scale. Sertoli cells in normal testes displayed a moderate
cytoplasmic and weak nuclear staining for galectin-lspecific
binding sites. Galectin-3-specific binding sites
were expressed in Sertoli cells less intensely than
accessible ligands for galectin-l (mean score 2.25 for
galectin-l and 1.50 for galectin-3). Germ cells were only
weakly reactive. Tubular walls were negative for both
classes of galectin-specific binding sites. In SCOS,
galectin-l binding was moderate to strong and more
pronounced than galectin-3 binding by Sertoli cells
(mean scores 4.00 and 2.25). Tubular walls were
negative for galectin-staining. The ratio for galectin-1-1
galectin-3-specific binding (staining score ratio) was
1.50 form normal testis and 1.78 for SCOS disclosing a
relative increase of galectin-3 binding sites in the latter.
Staining with galectin-l- and -3-specific antisera showed
a strong cytoplasmic galectin-l immunoreactivity in
Sertoli cells of normal and SCOS testis (score 4.00 for
both). Anti-galectin-3 did not stain Sertoli cells or germ
cells in normal testis. Only Leydig cells were labeled
(score 3.00). In SCOS a weak to moderate nuclear
staining of Sertoli cells was noted (score 2.00).
Galectin-3 expression and galectin-l-specific binding sites were found to be increased in Sertoli cells
of SCOS. This modulation of reactivity can have
implications for Sertoli cell interactions with galectinreactive
extracellular matrix components like laminin
and for anti-apoptotic effects.
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