Differences in glycosylation of intracellular proteins between benign and malignant thyroid neoplasms.

Differences in glycosylation of nuclear and cytosolic proteins isolated from benign and malignant human thyroid neoplasms were analyzed by lectin blotting and enzyme linked lectino-solid-phase assay using Erythrina cristagalli and Ricinus communis agglutinins. The results reported in this study have not shown any significant differences in lectin binding by nuclear proteins of benign and malignant tumors, however, quantitative and qualitative differences were observed in the patterns of cytosolic glycoproteins. In the majority of carcinomas samples lectin binding to cytosolic proteins was definitely weaker in comparison with adenomas and non-neoplastic specimens, which suggested alterations in glycosylation of cytosolic proteins in malignant tumors.

Glycoproteins of chicken liver nuclei cross-linked to DNA by cis-diamminedichloroplatinum.

Glycoproteins which participate in DNA-protein cross-links induced by action of cis-diamminedichloroplatinum (cis-DDP) in intact nuclei of chicken liver were investigated. Digoxigenin-labelled lectins with different sugar specificity were used for detection and characterization of these glycoproteins. Our results showed the presence of glycoproteins bearing high mannose as well as complex type oligosaccharides in chicken liver nuclei. In most cases of complex oligosaccharides, sialic acid residues bound in alpha(2-6) but not in alpha(2-3) linkage were present.

Nuclear liver glycoproteins at different stages of chicken embryo development.

In order to examine whether the patterns of nuclear and chromatin glycoproteins change during development the glycoproteins of foetal and adult chicken liver were investigated. Nuclear and chromatin proteins from both sources were separated by SDS-PAGE, transferred onto Immobilon-P transfer membrane or nitrocellulose and tested for concanavalin A (Con A), Galanthus nivalis agglutinin (GNA) and Aleuria aurantia agglutinin (AAA) binding. Results revealed a similarity in the profiles of nuclear and chromatin glycoproteins recognized by Con A from 14-, 16-, 18-day foetal and adult chicken liver. Generally GNA and AAA reacted more weakly with glycoproteins from foetal liver compared with the same glycoproteins from adult liver.

Glycoproteins present in the fraction of chromatin proteins loosely bound to DNA from hamster, chicken and frog liver cells.

There are numerous glycoproteins recognized by Concanavalin A (ConA) and Galanthus nivalis agglutinin (GNA) in 0.35 mol/l NaCl soluble fraction of chromatin proteins loosely bound to DNA from hamster, chicken and frog liver cells. Results of our detailed comparative analysis show a marked similarity between liver chromatin glycoproteins from the examined animals. The presence of similar chromatin glycoproteins in different animal species may indicate that they play an important universal role in the liver cells.

[Exposure to radon-222 of inhabitants of buildings in Olsztyn]. / Narazenie ludnosci na radon-222 w budynkach mieszkalnych Olsztyna.

The concentrations of radon-222 in the air of some buildings in Olsztyn were measured. The main source of radon in buildings is in general the ground under building and the materials used for building structure. In this work the results of radon-222 concentration measurements in the air of some buildings constructed before the 1939 year, in the buildings constructed after 1945 year with the traditional use of the bricks and in the buildings constructed with the use of great prefabricated plates are presented. The relations between radon-222 concentrations in the basements and in the first floor flats situated above the basement were evaluated. Based on the mean radon concentrations in the air of the various types of buildings investigated the effective doses for the inhabitants of each type of buildings were estimated.

Effect of carbohydrate moieties on the stability of nuclear glycoproteins from hamster liver.

The effect of carbohydrate moieties on the stability of hamster liver nuclear glycoproteins in the course of endogenous proteolysis employing highly specific digoxigenin-labelled lectins, was studied. Whole hamster liver nuclei were autolysed in optimum conditions for the action of nuclear proteinases able to degrade histones as well as non-histone proteins. Incubated samples were electrophoresed on sodium dodecyl sulphate-polyacrylamide gel. Coomassie blue stained gels demonstrated degradation of some proteins in particular after 18 and 24 h incubation. Proteins with molecular weights of about 46, 54 and 76 kD appeared to be resistant to proteolysis. The same location and intensity of bands of glycoproteins on immunoblots from incubated and nonincubated samples of nuclei indicated that oligosaccharide chains protect proteins from degradation.

Age-related patterns of lectin-binding nuclear glycoproteins of hamster liver.

We studied the age-related patterns of lectin-binding liver nuclear glycoproteins from hamsters between 5 and 35 weeks of age. The examinations of the carbohydrate structures of liver nuclear glycoproteins in relation to the age of hamsters were carried out after electrophoresis and blotting by a very sensitive immunological detection system with highly specific digoxigenin-labelled lectins. The results reported in the present study do not show any significant changes in the patterns of nuclear glycoproteins with regards to the age of hamsters except the decrease in affinity of wheat germ agglutinin (WGA) to 63 kDa glycoprotein bearing single O-linked N-acetylglucosamine residues.

Lectin-binding glycoproteins in nuclear fractions from hamster liver and Kirkman-Robbins hepatoma.

As a further step toward characterizing the major nuclear glycoproteins from hamster liver and Kirkman-Robbins hepatoma (Lipinska A. and Gaczynski M. Int. J. Biochem. 4, 1385-1390, 1992) its intranuclear localization was studied. The glycoprotein patterns of examined nuclear fractions of hamster liver and hepatoma revealed some cell specificity observed especially in nuclear matrix preparations. Our results show the extensive presence of envelope glycoproteins in the nuclear matrix.