PubMed Health⌕ Search

Biomedical subjects

W Tyran

Publications and source records attributed to W Tyran.

8 recordsLinked to original sources

The impairment of wound healing process is correlated with abnormalities of TNF-alpha production by peritoneal exudate cells in obstructive jaundiced rats.

The wound healing process and production of tumour necrosis factor alpha (TNF-alpha) by peritoneal cells of 7-day and 14-day obstructive jaundice (OJ) and sham-operated rats were investigated. In the study the skin wound breaking strength was measured. In addition such histological and biochemical parameters as fibroblast and endothelial cell proliferation, inflammatory cell infiltration and hydroxyproline content were evaluated in polyurethane sponge discs implanted subcutaneously into rats. TNF-alpha production by peritoneal exudate cells (PEC), both spontaneous and lipopolysaccharide (LPS)-induced was determined by a bioassay. In OJ rats the process of both early as well as late phase of healing was impaired. The breaking strength of skin wound was decreased, the fibroblast and endothelial cell proliferation and collagen deposition, as well as hydroxyproline content were diminished. In 7 day OJ the numbers of inflammatory cells in the implants were lowered with a subsequent slight increase on day 14 of OJ. The spontaneous and LPS induced TNF-alpha production by PEC were significantly higher in 7 day OJ as compared with sham-operated controls. On day 14 of OJ the LPS-induced TNF-alpha level was, in contrast, much lower and did not differ much from the spontaneous TNF-alpha production. We conclude that the impairment of wound healing in OJ results from disturbances in functioning of the immune system caused by systemic endotoxaemia.

Animals↗

Platinum complexes and pyruvate kinase activity.

The interaction of platinum complexes with bovine heart pyruvate kinase (PK) was studied by absorption, CD, fluorescence spectroscopy and enzymic activity test. Our results showed that activity of PK was reduced by cis-DDP and potassium tetrachloroplatinate in a time-and concentration dependent manner. Cis-DDP was less effective than K2PtCl4 in reducing PK activity. The native enzyme showed well defined negative Cotton effect at 222 and 208 nm indicating the presence of alpha-helical and beta structure. Platinum binding lowered the Cotton effect in this region by about 10-20% and 30-50% for the system with cis-DDP and K2PtCl4, respectively. Fluorescence study showed that platinum binding quenched tryptophan fluorescence suggesting that binding occurs at the tryptophan residue or its proximity. PK modifications induced by platinum binding would result in a greater resistance to denaturing agents.

Animals↗

[Activity of glucose-6-phosphate dehydrogenase in erythrocytes in patients with atopic asthma and allergic rhinitis].

A significant decrease of erythrocyte G-6-P dehydrogenase activity in patients with atopic asthma and allergic rhinitis was observed. In order to define the cause of this phenomenon the enzyme was isolated from the cells. The kinetic and molecular properties of the erythrocyte G-6-P dehydrogenase were studied. A change in the Michaelis constant for G-6-P dehydrogenase was seen in erythrocytes of both patient groups. The thermoresistance at 45 C was reduced significantly. These modified properties can imply a change in the dehydrogenase molecule, this is seen more significantly in the group with allergic rhinitis.

Adolescent↗

Haemolytic crises caused by Hoya carnosa in a patient with G6PD deficiency.

Haemolytic crises caused by contact with Hoya carnosa were observed in a 45-years old woman. The investigation of erythrocyte enzymes displayed both G6PD deficiency and its diminished affinity to G-6-P. Some properties of dehydrogenases isolated from erythrocytes of the patient's brother and son were also changed although clinical signs of haemolysis were absent.

Anemia, Hemolytic↗

Abnormalities of cobalt-activated acylase from human sarcoma, carcinoma and the adjacent tissue.

Cobalt-activated acylase form-2 from human uterine myosarcoma, lung adenocarcinoma and the adjacent tissue was isolated, purified and characterized. It was found, that the enzyme from the malignant neoplasms differed both from the normal tissue and benign tumor acylase-2 in its Km value, temperature optimum and effect of some ions. Some abnormal properties (pH dependence, activation by cobalt and thermostability) were common for benign and malignant tumors. In lung tissue adjacent to adenocarcinoma, some deviations of acylase properties were observed, similar to that found in tumor, indicating that biochemical changes may be present also in tissues unaffected by the neoplastic growth by the histopathological criteria.

Adenocarcinoma↗

Cobalt-activated acylase and aminoacylase I in human malignant tumors.

The activities and isoenzyme pattern of cobalt-activated acylase and of aminoacylase I were estimated in carcinomas of bronchi, lung, thorax, stomach, colon and uterus. In all cancer tissues the activity of cobalt-activated acylase was markedly increased as compared with the normal tissue. Alterations of the isoenzyme pattern of cobalt-activated acylase were found in the carcinoma of stomach and of uterus, with the increased expression of the form-1 of the enzyme. No regularity in the aminoacylase I changes in tumor tissues has been observed.

Amidohydrolases↗

Cobalt-activated acylase from human uterine myoma.

Cobalt-activated acylase was isolated from human uterine muscle and myoma. The enzyme was purified by ammonium sulphate precipitation, and subsequent chromatography on DEAE-cellulose, Sephadex G-150 and DEAE-Sephadex. The comparison of muscle acylase and acylase obtained from myoma has shown differences in the enzyme stability, the dependence of activity on pH and in the susceptibility to the effect of activators and inhibitors. Only one molecular form of cobalt-activated acylase has been found in both tissues.

Acyltransferases↗