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C Hipler

Publications and source records attributed to C Hipler.

43 records · Page 3Linked to original sources
PubMedDate not supplied

Lectin-binding sites in normal human testis.

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. Interstitial cells and lamina propria of seminiferous tubuli were stained by PNA, HPA, RCA II, SBA, ConA, and WGA indicating an abundance of the following glycoconjugates: N-GlcNAc, N-GalNAc, Gal, and Man. The germinative cells were stained cytoplasmatically by ConA (Alpha-D-Man/-Glc). Sertoli cells showed the same pattern with ConA. Early spermatids fixed PNA and RCA II in the acrosomal region. Elongated spermatids fixed WGA on their acrosomes and fainty on the flagellae too indicating abundance of N-GlcNAc residues. The findings argue for differentiation-related modifications of lectin-binding sites on germinative cells and the usefulness of Bouin-fixed samples for lectin histochemistry.

Acetates↗
PubMedDate not supplied

Testicular lectinhistochemistry in the Sertoli-cell-only-syndrome.

Glycoconjugate expression was studied in tissue specimens of the Sertoli-cell-only-syndrome by lectinhistochemistry. Both ConA and WGA marked the cell surface of Sertoli cells fainty. UEA I labelled their nucleoli. PNA and RCA failed to stain Sertoli cells. These staining patterns resembled those of normal human testis. The thickened tubular walls in the Sertoli-cell-only-syndrome were abundant in binding sites for WGA, PNA, UEA I, and RCA. ConA stained the outer part of the wall heavily, but failed to react with the adluminal part. It is suggested, that the Sertoli-cell-only-syndrome is accompanied by a selective loss of mannosyl residues in the adluminal part of thickened tubular walls.

Humans↗
PubMedDate not supplied

[Partial characterization of the epithelial lectin binding sites of human gingiva and skin].

Frozen sections of human gingiva and skin, fixed in acetone, were subjected to limited enzyme digestion (neuraminidase, proteinase K, trypsin) or, respectively, the application of solvents (chloroform/methanol, triton X-100) to allow a partial characterization of epithelial lectin binding sites. Gingiva differs from normal skin in that more conA-binding glycolipids are present in the lower cell layers. In the upper layers conA-fixing glycoproteins are prevailing. Psoriatic foci regularly exhibit an increased presence of conA-binding glycolipids. Gingiva and normal skin have some common features in the behavior of the lectin binding sites of HPA, WGA and UEA I. Analogies in the binding pattern of conA and UEA I in gingival tissue and in psoriatic foci are thus due to different lectin receptors.

Binding Sites, Antibody↗
PubMedDate not supplied

Lectin-binding sites in testis of men with acrosomeless round-headed spermatozoa.

We report herein about lectin histochemistry of seminiferous epithelia in two infertile men with exlusely acrosomeless round-headed spermatozoa. FITC-conjugated lectins (ConA, PNA, RCA II, WGA) have been employed on tissue sections of Bouin fixed testicular biopsies. RCA II gave a dot-like fluorescence of the acrosomal region and WGA gave a cap-like acrosomal fluorescence of spermatids. PNA-a marker of acrosomal differentiation-failed to stain spermatids. The binding of ConA to germ cells was not influenced by this syndrome. In conclusion, the syndrome of acrosomeless round-headed spermatozoa is associated with selective perturbations of testicular lectin-binding sites. They might contribute of the inability of sperm cells to adhere to and penetrate into ova.

Acrosome↗
PubMedDate not supplied

[Contact allergy to dicyclohexylcarbodiimide].

Allergic contact dermatitis occurring in a 25 years old female biochemist was found to be due to occupational handling of dicyclohexylcarbodiimide (DCC). This was confirmed by patch testing. Though DCC is widely used in peptide chemistry as completing reagent, only a few publications report occupational allergic contact dermatitis.

Adult↗