Effects of 2.4 GHz radiofrequency electromagnetic field (RF-EMF) on glioblastoma cells (U -118 MG).

INTRODUCTION AND OBJECTIVE: Mobile phones and Wi-Fi are the most commonly used forms of telecommunications. Initiated with the first generation, the mobile telephony is currently in its fifth generation without being screened extensively for any biological effects that it may have on humans or on animals. Some studies indicate that high frequency electromagnetic radiation emitted by mobile phone and Wi-Fi connection can have a negative effect upon human health, and can cause cancer, including brain tumour. OBJECTIVE: The aim of the study was to investigate the influence of 2.4 GHz radiofrequency electromagnetic field (RF-EMF) on the proliferation and morphology of normal (human embryonic kidney cell line Hek-293) and cancer cells (glioblastoma cell line U-118 MG). MATERIAL AND METHODS: The cell cultures were incubated in RF-EMF at the frequency of 2.4 GHz, with or without dielectric screen, for 24, 48 and 72h. In order to analyse the influence of the electromagnetic field on cell lines, Cytotoxicity test Cell Counting Kit-8 was performed. To protect cells against emission of the electromagnetic field, a dielectric screen was used. RESULTS: It was found that 2.4 GHz RF electromagnetic field exposure caused a significant decrease in viability of U-118 MG and Hek-293 cells. The impact of the electromagnetic field was strongest in the case of cancer cells, and the decrease in their survival was much greater compared to the healthy (normal) cells of the Hek-293 line. CONCLUSIONS: Results of the study indicate that using a radio frequency electromagnetic field (2.4 GHz) has a clearly negative effect on the metabolic activity of glioblastoma cells. RF-EMF has much less impact on reducing the viability of normal cells (Hek -293) than cancer cells.

No wonder, it is a hybrid. Natural hybridization between Jacobaea vulgaris and J. erucifolia revealed by molecular marker systems and its potential ecological impact.

Progressive changes in the environment are related to modifications of the habitat. Introducing exotic species, and interbreeding between species can lead to processes that in the case of rare species or small populations threatens their integrity. Given the declining trends of many populations due to increased hybridization, early recognition of hybrids becomes important in conservation management. Natural hybridization is prevalent in Jacobaea. There are many naturally occurring interspecific hybrids in this genus, including those between Jacobaea vulgaris and its relatives. Although Jacobaea erucifolia and J. vulgaris often co-occur and are considered closely related, apart from the few reports of German botanists on the existence of such hybrids, there is no information on research confirming hybridization between them. Morphologically intermediate individuals, found in the sympatric distributions of J. vulgaris and J. erucifolia, were hypothesized to be their hybrids. Two molecular marker systems (nuclear and chloroplast DNA markers) were employed to test this hypothesis and characterize putative hybrids. Nuclear and chloroplast DNA sequencing results and taxon-specific amplified fragment length polymorphism (AFLP) fragment distribution analysis confirmed the hybrid nature of all 25 putative hybrids. The AFLP patterns of most hybrids demonstrated a closer relationship to J. erucifolia, suggesting frequent backcrossing. Moreover, they showed that several individuals previously described as pure were probably also of hybrid origin, backcrosses to J. erucifolia and J. vulgaris. This study provides the first molecular confirmation that natural hybrids between J. vulgaris and J. erucifolia occur in Poland. Hybridization appeared to be bidirectional but asymmetrical with J. vulgaris as the usual maternal parent.

Alzheimer's disease against peptides products of enzymatic cleavage APP protein: Biological, pathobiological and physico-chemical properties of fibrillating peptides.

Various peptides products of enzymatic cleavage of key for Alzheimer's disease Amyloid Precursor Protein (APP) are well known, but still are matter of scientific debate. The Aß type products are especially challenging for experimental and medical research. This paper outlines several, still poorly known, biological and medical processes such as peptides biology, i.e., formation, biodistribution, translocation, transport and finally removal from brain compartments and body fluids like Intracellular Fluid (ICF), Cerebrospinal Fluid (CSF), Interstitial Fluid (ISF), blood serum or urine. In addition, the following studies concerning AD patients might prove challenging and simultaneously promising: peptides translocation through Blood-Brain - Barrier (BBB) and Blood-Cerebrospinal Fluid Barrier (BCSFB) and their removal from the brain according to a new concept of glymphatic system; - diagnostic difficulties that stem from physico-chemical properties and the nature of proteins or fibrillating peptides itself like low concentration, short half-live and from experimental-technical problems as well like high adsorption or low solubility of Aß, tau or amylin. The study of diagnostic parameters is very important, as it may better reflect early changes before the disease develops; one such parameter is the Aß42/Aß40 ratio, or the ratio with the total tau concentration combination and other new biomarkers like Aß1-38; other factors include oxidative stress and inflammation process proteins, complement factor H, alpha-2-macroglobulin, or clusterin. The study of various forms of pathological amyloid deposits that emerge in different but specific brain regions AD patients seems to be crucial as well. The composition of the first initial pathological, pre-fibrillating monomers of fibrillating peptides and their role in AD development and disease progression have been described as well. They are even more challenging for science and simultaneously might be more promising in early diagnosis for AD patients. As always in science, research leads to endless discoveries and further inquiry. Fundamental problems in this field most probably are still far from being definitively comprehended, and multiple crucial questions await better answers. What we really need is to study more and deeper into this matter.

Alzheimer's disease against peptides products of enzymatic cleavage of APP protein. Forming and variety of fibrillating peptides - some aspects.

Various and different peptides products resulting from enzymatic protein cleavage of Amyloid Precursor Proteins (APP) are the main agents in the pathophysiology of Alzheimer's disease (AD). Although relatively well-known, they still arouse interest leading to further intense and wide-ranging research. Their biology and physico-chemical properties still are challenging for basic, experimental research and are matter of scientific debate. The APP itself and its functions are still somewhat enigmatic and therefore it is also called the All Purpose Protein. Apart from well known amyloidogenic and antiamyloidogenic (non-amyloidogenic) enzymatic cleavage pathways of APP protein this paper deals with issues connected with other, alternative pathways that seem to be interesting and important as well. They lead to other than Aß forms of peptide products such as: N-APP, N-terminally cleavage products of APP (N-terminally truncated ) Aß', γ- secretase-independent pathway products that involve concerted cleavages of APP by α- and ß-secretase or products that emerge after caspase activity. Presence of all these peptides in CSF, ISF, blood serum and urine of the AD patients is crucial for successful diagnosis, giving rise to hope of their better detection and potentially better treatment of AD. Therefore, newly discovered products of the AßT domain cleavage (Aß total i.e. full fibrillating domain of APP), Aß type products and other peptides because of their biology and physico-chemical properties are very intriguing and deserve further experimental research. On the other hand after better recognition and better understanding their biology they might be enormously useful in the future for diagnosis and therapy for example Alzheimer's disease.

[Amylin under examination. Fibrillation - cytotoxic pancreatic polypeptide aggregation]. / Amylina w badaniach eksperymentalnych.Fibrylacja ­ cytotoksyczna agregacja polipeptydutrzustki.

In patients or animals affected by type 2 diabetes mellitus (DM2, non-insulin dependent diabetes mellitus [NIDDM]), some pathological deposits, called amyloid, are observed among cells of islets of Langerhans. Among other constituents, the deposits consist of an insoluble, fibrillar form of polypeptide neurohormone called amylin, produced by pancreatic beta cells. It is thought that formation of fibrillar deposits of misfolded and aggregated polypeptide is highly toxic to beta cells and leads to cell dysfunction, cell loss, pancreas destruction and progress of the disease. Due to the extreme insolubility of this polypeptide and its instant fibrillation, amylin constitutes a methodological problem, and there is a need for a special methodology in experiments. Some mechanisms and factors that govern amylin fibrillization are rather poorly understood. This article presents amylin as a fibrillating molecule and some methods and methodological aspects and problems that emerge at successive steps during the fibrillation process, including hypothesized cytotoxicity mechanisms of this polypeptide.

[Amylin under examination. Fibrillogenic polypeptide of pancreatic amyloid]. / Amylina w badaniach eksperymentalnych. Fibrylotwórczy polipeptyd amyloidu trzustkowego

In patients or animals affected by 2 type diabetes mellitus (diabetes mellitus type 2, DM2, non-insulin-dependent diabetes mellitus, NIDDM) or pancreatic tumor disease e.g., insulinoma, some pathological deposits, called amyloid, are observed among cells of islets of Langerhans. Among other constituents, pancreatic deposits consist of an insoluble, fibrillar form of peptide neurohormone termed amylin, produced by pancreatic beta cells. It is thought that formation of fibrillar deposits of misfolded and aggregated peptide is highly toxic to beta cells and leads to cell dysfunction, cell loss, pancreas destruction and progress of the disease. This relatively small, 37-amino acid peptide constitutes a serious scientific, research and to some extent a medical problem. This article presents amylin as a fibrillating molecule which participates in formation of amyloid deposits in human and animal pancreas, Langerhans islets as a microenvironment of pancreatic amyloid formation, occurrence of amylin and amyloid in animals and humans, and physico-chemical requirements to meet to name amylin deposit as amyloid.

[Amylin under examination. Fibrillogenic polypeptide hormone of the pancreas]. / Amylina w badaniach eksperymentalnych. Fibrylotwórczy polipeptydowy hormon trzustki.

In patients or animals affected by type 2 diabetes mellitus (DM2, non-insulin dependent diabetes mellitus [NIDDM]) some pathological deposits, called amyloid, are observed among cells of islets of Langerhans. Among other constituents, deposits consist of an insoluble, fibrillar form of peptide neurohormone called amylin, produced by pancreatic beta cells. It is thought that formation of fibrillar deposits of misfolded and aggregated peptide is highly toxic to beta cells and leads to cell dysfunction, cell loss, pancreas destruction and progress of the disease. This relatively small 37-amino acid peptide constitutes a serious scientific, research and to some extent a medical problem. This article presents amylin as a hormone, neurohormone and as a fibrillating molecule which participates in amyloid deposit formation in human and animal pancreas. The role of some amino acids important for fibril formation has been highlighted.

[Diabetes type 2 and Alzheimer disease - one or two diseases? Mechanisms of association]. / Cukrzyca typu 2 a choroba Alzheimera - jedna czy dwie choroby? Mechanizmy asocjacji.

Some epidemiological data and pathophysiological evidence suggest similarities and connection of two amyloidoses: diabetes mellitus type 2, (DM2) (non-insulin dependent diabetes mellitus, NIDDM) and Alzheimer's disease (AD). What they have in common is insulin resistance, neurodegeneration, development and progression of dementia, and the fact that in the course of both diseases fibrillar aggregates of specific proteins are accumulated in affected organs. What is more, experimental evidence also supports the hypothesis that small prefibrillar aggregates that emerge prior to the appearance of mature fibrils are responsible for a key step in development and cytotoxicity of both diseases. They also have similar pathogenic effects. Both peptides possess the common receptor AMY3. More and more evidence is accumulating that key cell regulation processes are similar for both diseases as well. The question is raised: can Alzheimer be a new form of diabetes disease?

[Plasma carbonyl group concentration in pregnant women with IUGR treated by L-arginine and acetylsalicylic acid]. / Ocena stezenia grup karbonylowych u kobiet ciezarnych z hipotrofia wewnatrzmaciczna plodu leczonych L-arginina i kwasem acetylosalicylowym.

OBJECTIVES: Carbonyl groups are the elements connecting protein structure, they influent into biological activity. High concentration of carbonyl groups means high risk of protein destruction. DESIGN: The aim of this study was the evaluation of carbonyl group concentration in blood serum in normal pregnancy and in women with IUGR treated by L-arginine and acetylsalicylic acid. MATERIAL AND METHODS: The study was done at the Department of High Risk Pregnancy, Department of Gynaecology and Obstetrics, Medical University of Lódz, in 1999-2002. The study group included 80 pregnant women hospitalised due to foetal growth restriction, between the 32-th and 38-th weeks of pregnancy. The treatment was conducted for twenty days and consisted of everyday low dose aspirin (Acard) and L-arginine (NO precursor). The ultrasound and laboratory examinations were done on the first day of hospitalisation in both groups, and at 20-th day of treatment in the group of IUGR. The carbonyl groups concentration was measured by Levine method and expressed in mmol/1 mg proteins. RESULTS: In controls mean value of carbonyl groups concentration was 1.848 +/- 0.291 mmol/1 mg proteins and after 20 days of observation 1.897 +/- 0.439. In the group with IUGR before treatment was 2.193 +/- 0.658. After 20 day of the therapy and the value decreased to 2.078 +/- 0.679. There is a significant difference between the value of carbonyl-groups concentration in normal pregnancy and IUGR. The carbonyl-groups concentration decreased after 20 days of treatment by L-arginine, and the value is still higher than in normal pregnancy. CONCLUSIONS: Oxidative protein damage in IUGR decreased in the process of treatment.

There is no evidence for the existence of complex formation between doxorubicin and glutathione.

Doxorubicin is co-transported with glutathione by several multidrug resistance proteins (MRPs). In order to check whether weak non-covalent aggregates between doxorubicin and glutathione can be formed, which might be substrates for the transporter, the effect of glutathione on the partition coefficient of doxorubicin was studied. No evidence of an effect of glutathione (at levels up to 20 microM) on the partition coefficient of doxorubicin was found in the pH range of 4.0-7.4. These results indicate that non-covalent doxorubicin-glutathione complexes do not form.