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

  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},
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. 

Sialic acid in human testis and changes with aging.

Findings indicate that changes in the metabolism of sialoderivatives in the testis could be related to morphofunctional changes in various testicular components typical of this organ during aging.

Lectin‐binding pattern of glycoconjugates during spontaneous testicular recrudescence in Syrian hamster (Mesocricetus auratus) after exposure to short photoperiod

The normal lectin pattern is recovered during testis recrudescence and germ cell apoptotic activity is low, as is observed by specific lectins for germ cells in apoptosis.

Identification of fucosylated glycoconjugates in Xenopus laevis testis by lectin histochemistry

A histochemical study of the fucose (Fuc)-containing glycoconjugates of Xenopus testis by means of lectins, combined with deglycosylation pretreatments, suggesting that fucosylated glycans are of both N- and O-linked types.

The Distribution Profile of Glycoconjugates in the Testis of Brown-Banded Bamboo Shark (Chiloscyllium punctatum) by Using Lectin Histochemistry

The increased intensity of most lectins in the interstitial cells indicates the association of glycoconjugates in their androgen-secreting activity in the bamboo shark testis, and peanut agglutinin (PNA) is used as an acrosomal marker in combination with other marker proteins for studying shark spermatogenesis.

Distribution of Lectin‐Bindings in the Testis of the Lesser Mouse Deer, Tragulus javanicus

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

G glycoconjugate profiling through lectin histochemistry can characterize some cell-type selective markers that will be helpful in studying bull and donkey spermatogenesis.

The acrosomal protein SP‐10 (Acrv1) is an ideal marker for staging of the cycle of seminiferous epithelium in the mouse

Evidence is presented that SP‐10 is a useful marker for staging the cycle of the seminiferous epithelium, and the anti‐SP‐10 antibody works well in different fixatives, on paraffin‐embedded as well as cryosections, and has been shown to be useful for characterizing spermatogenic defects in mutant mice.

Identification, Culture, and Characterization of Germline Stem Cell-Like Cells in Chicken Testes1

It is concluded that germline stem cell-like cells are present in chicken testicular cells retrieved from both juvenile and adult testes, which can be identified with the specific markers for primordial germ cells or embryonic germ cells.

N-Glycans in Xenopus laevis testis characterised by lectin histochemistry.

The β-elimination procedure, which removes O-linked glycans, revealed new labelling patterns with GNA, LCA and PHA-L, suggesting that some N-glycans were masked by O- glycans, and thus they became accessible to these lectins only after removal of the O- linked oligosaccharides.



Distribution of Glycoconjugates in Human Testis A Histochemical Study Using Fluorescein‐ and Rhodamine‐conjugated Lectins

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

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.

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.

Distribution of Lectin Binding in Rat Testis and Epididymis

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

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.

Lectin histochemistry of classic and spermatocytic seminoma.

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.

A hypothesis on the biological role of ABH, lewis and P blood group determinant structures in glycosphingolipids and glycoproteins

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.

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

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.