Lectin‐Binding Sites in Normal Human Testis/Lektinbindungsstellen normaler humaner Hoden

@article{Wollina2009LectinBindingSI,
  title={Lectin‐Binding Sites in Normal Human Testis/Lektinbindungsstellen normaler humaner Hoden},
  author={Uwe Wollina and Gerhard Schreiber and Christine Zollmann and Christina Hipler and E. G{\"u}nther},
  journal={Andrologia},
  year={2009},
  volume={21}
}
Summary: Nine fluorescein isothiocyanate (FITC) — labelled lectins have been used to investigate the distribution of glycoconjugates in unfixed frozen and Bouin‐fixed sections of normal human testis. 
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A Lectin Histochemical Study on the Testis of the Babirusa, Babyroussa babyrussa (Suidae)
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The present findings showed that the distribution pattern of lectin binding in the testis of babirusa is somewhat different from that of pig or other mammals reported previously.
Distribution of Lectin‐Bindings in the Testis of the Lesser Mouse Deer, Tragulus javanicus
TLDR
The distribution of lectin bindings in the testis of the smallest ruminant, lesser mouse deer was studied using 12 biotinylated lectins specific for d‐galactose and oligosaccharide sugar residues to discuss in comparison with those of other animals and their possible functional implications.
Comparative Cellular Localization of Sugar Residues in Bull (Bos taurus) and Donkey (Equus asinus) Testes Using Lectin Histochemistry
TLDR
G glycoconjugate profiling through lectin histochemistry can characterize some cell-type selective markers that will be helpful in studying bull and donkey spermatogenesis.
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References

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TLDR
The increase in RCA I, PNA, SB A and HP A binding sites during germ cell differentiation is noticed, suggesting the appearance of certain galactose and N‐acetylgalactosamine containing glycoconjugates.
Factors affecting the binding of lectins to normal human skin
TLDR
The use of routine histological processing not only greatly reduced binding intensity overall but also altered the binding pattern.
Lectin binding sites in human seminiferous epithelium, in CIS cells and in seminomas.
TLDR
The results show that human germ cells are rich in carbohydrate-containing compounds with specific alterations in the expression of glucosyl moieties during germ cell development that supports the suggestion of the malignant nature of CIS germ cells.
Lectin-binding pattern of bull testis and epididymis.
TLDR
Findings suggest that the basal cells may beactive in the digestion of absorbed material and that they derive from the principal cells, which may be active in transporting absorbed material to them.
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TLDR
It was concluded that this reaction is at least partially due to the secretory products synthetized by principal, apical, narrow and light cells of the epididymal epithelium, indicating specialization of the cells for the production of distinct glycoproteins.
Lectin binding sites on the plasma membrane of epididymal and ejaculated chimpanzee sperm
TLDR
The general similarity in binding patterns of caput and cauda epididymal chimpanzee sperm exposed to Con A and DBA might reflect the fact that sperm morphology does not change during epididcyal transit in this species, thus implying a more stable membrane structure than is present in other primates so far studied.
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TLDR
The data thus illustrate some differences between classic and spermatocytic seminomas, but no diagnostic or pathognomonic pattern of lectin binding could be discerned, and the data do not support the earlier contentions that sper matabolic seminomas contain malignant equivalents of cells in advanced stages of sperMatogenesis.
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TLDR
It is presented that glycosphingolipids of circulating erythrocytes are membrane-packing substances providing for an energetically cheap carbohydrate protective coat at the cell surface providing protection for circulatory and membrane glycoproteins from proteolysis, denaturation and recognition of potentially antigenic sites of protein moieties by the immunosurveillance system of the body.
The fate of acrosomal staining during the acrosome reaction of human spermatozoa as revealed by a monoclonal antibody and PNA-lectin.
TLDR
The present results indicate that the corresponding antigen, evidently acrosin, and PNA-positive material are liberated during the acrosome reaction which suggests that they are not bound to the inner acrosomal membrane but are components of the Acrosomal matrix.
Effects of histological processing on lectin binding patterns in oral mucosa and skin
TLDR
Lipid extraction prior to lectin incubation resulted in complete elimination of detectable binding to epithelium suggesting that lectin-binding sites in the cell surface are associated with glycolipid or lipid.
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