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Biomedical subjects

A Jendryczko

Publications and source records attributed to A Jendryczko.

At least 73 records · Page 4Linked to original sources
PubMed1989

Zinc, vitamins A and E, and retinol-binding protein in sera of patients with cancer of the larynx.

Serum vitamin A concentrations were measured in 22 patients with laryngeal cancer and found to be significantly lower than those of patients of similar age with either nonmalignant laryngeal or other than laryngeal diseases. The levels of vitamin A in the patients with laryngeal cancer, but not in the controls, significantly correlated with serum concentrations of retinol-binding protein (RBP) and zinc. It is suggested that low levels of zinc might reduce the synthesis of RBP and thus reduce the mobilization of vitamin A from the liver stores.

Aged↗
PubMed1989

Plasma retinol, beta-carotene and vitamin E levels in relation to the future risk of pre-eclampsia.

20 healthy primigravidas were studied from 28 weeks' gestation until 4 days after delivery. In 9 of these women pre-eclampsia developed, the remaining 11 subjects who were age-matched had normal pregnancies. Plasma retinol, beta-carotene and vitamin E concentrations were measured by high performance liquid chromatography. The concentrations of retinol and vitamin E were significantly lower in the pre-eclampsia group than in the normotensive group at 28 weeks' gestation--that is before the onset of symptoms and signs of pre-eclampsia. The concentrations of retinol and vitamin E remained significantly lower in the pre-eclampsia group until delivery. It is suggested that measurement of the retinol or vitamin E concentration in plasma may be useful as a predictor of the likely development of pre-eclampsia.

Carotenoids↗
PubMed1988

Cartilage degradation by neutral metalloproteases in experimental collagen-like syndrome.

In this study, we sought to determine the role of neutral proteases in cartilage matrix proteoglycan degradation, which occurs during the experimental hydralazine-induced collagen-like syndrome (c-l-s) in rats. The digestion of endogenous proteoglycans by neutral proteases in homogenates of cartilage from rats with c-l-s has been measured and compared with that of normal age-matched controls. Cartilage specimens from the tibial plateau were analysed for DNA and proteoglycan content, and neutral proteoglycan-degrading activity, No significant difference in cartilage DNA concentration was observed among the rats with c-l-s and the controls. Total neutral proteoglycan-degrading metallo-enzyme activity, determined by direct tissue assay, was significantly higher in c-l-s cartilage than that in control cartilage. Serine protease activity on proteoglycans was much lower than that of metalloprotease. The results of this study are consistent with the hypothesis that the neutral metalloproteases of cartilage are involved in the degradation of proteoglycans in c-l-s.

Animals↗
PubMed1988

Lipid peroxidation in the nuclear fraction of rat lungs induced by hydralazine.

Hydralazine (1-hydrazinophthalazine) was administered in drinking water as a 0.0312% solution to randomly bred female Wistar rats during 3 weeks. The average daily intake of this compound was 6.74 mg for a rat. The treatment resulted in lipid peroxidation in the nuclear fraction of the lungs. This lipid peroxidation was detected spectrophotometrically by the appearance of a peak at 233-235 nm in the spectrum of chloroform-methanol extract. The close proximity of DNA may make it a possible target for attack by free radicals.

Animals↗