Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych: neurotransmitter acetylcholine

Sortuj według:

Ogranicz wyniki do:

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

Time-dependent model to mimic acetylcholine induced vasodilatation in arterial smooth muscle cells

100%

Sahrawat T. R., Chatterjee D.

International Letters of Natural Sciences

2016

tom 52

Computational approaches for spatial modeling of dynamics of the intercellular distribution of molecules can parse, simplify, classify and organize the spatiotemporal richness of any biochemical pathway and demonstrate its impact on the cells function by simply coupling it with the downstream effecters. One such online system biology modeling package is Virtual cell that provides a unique open source software and it’s used for making mathematical models to simulate the cytoplasmic control of molecule that interact to produce certain cellular behavior. In our present study, a spatial model for time dependent acetylcholine induced relaxation of vascular endothelial cells lining the lumen of blood vessel that regulate the contractility of the arteries was generated. The time-dependent action of neurotransmitter acetylcholine for total time period for 1 second was studied on the endothelial cell at an interval of every 0.05 seconds. Such time simulated spatial models may be useful for testing and developing new hypotheses, interpretation of results and understand the dynamic behavior of cells.

Evaluation of HI-6 oxime: potential use in protection of human acetylcholinesterase inhibited by antineoplastic drug irinotecan and its cyto-genotoxicity in vitro

80%

Radic B., Vrdoljak A. L., Zeljezic D., Fuchs N., Berend S., Kopjar N.

Acta Biochimica Polonica

2007

tom 54

nr 3

The function of acetylcholinesterase (AChE) is the rapid hydrolysis of the neurotransmitter acetylcholine (ACh), which is involved in the numerous cholinergic pathways in both the central and the peripheral nervous system. Therefore, AChE measurement is of high value for therapy management, especially during the course of intoxication with different chemicals or drugs that inhibit the enzyme. Pyridinium or bispyridinium aldoximes (oximes) are able to recover the activity of the inhibited enzyme. Since their adverse effects are not well elucidated, in this study the efficiency of HI-6 oxime in protection and/or reactivation of human erythrocyte AChE inhibited by the antineoplastic drug irinotecan as well as its cyto/genotoxicity in vitro were investigated. HI-6 was effective in protection of AChE and increased its activity up to 30%; the residual activity after irinotecan inhibition was 7%. Also, it reactivated the enzyme previously inhibited by 50% irinotecan (4.6 µg/ml) applied at ¼ of the IC50 value. The tested concentrations of HI-6 exhibited acceptable genotoxicity towards white blood cells, as estimated by the alkaline comet assay, DNA diffusion assay and cytogenetic endpoints (structural chromosome aberrations and cytokinesis-block micronucleus assay). The results obtained warrant the further investigation of HI-6 in vivo, as well as its development for possible application in chemotherapy.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 International Letters of Natural Sciences

1 Berend S.

1 Chatterjee D.

1 Fuchs N.

1 Kopjar N.

1 Radic B.

1 Sahrawat T. R.

1 Vrdoljak A. L.

1 Zeljezic D.

1 2016

1 2007

Wyniki wyszukiwania

Time-dependent model to mimic acetylcholine induced vasodilatation in arterial smooth muscle cells

Evaluation of HI-6 oxime: potential use in protection of human acetylcholinesterase inhibited by antineoplastic drug irinotecan and its cyto-genotoxicity in vitro