Transfection of Eukaryotic Cells with Bipolar Cationic Derivatives of Tetraether Lipid

Author(s):  
Larissa Balakireva ◽  
Maxim Balakirev
Biologija ◽  
2017 ◽  
Vol 63 (3) ◽  
Author(s):  
Andriy Lysytsya ◽  
Natalya Matvienko ◽  
Mihail Kozii ◽  
Alexander Aishpur

It is known that polymeric derivatives of guanidine are actively used in many countries of the world as disinfectants and antiseptics. Polyhexamethylene guanidine (PHMG) and polyhexamethylene biguanidine (PHMB) are typical representatives of this class of compounds. They show a bacteriostatic effect in concentrations from 1 mg/l (or 10–4%) or above, and a bactericidal effect from 10 mg/l (10–3%) and above. It is considered that PHMG and PHMB are not very toxic to higher organisms. This is explained by the different mechanism of drugs action on prokaryotic and eukaryotic cells. However, their safety for the fauna of freshwater hydrocenoses has not been sufficiently studied. The toxic effect of the salts of PHMG on the representatives of various types and classes of hydrobionts was studied in the experiments. It has been established that the safe concentration of PHMG in water with a one-time action on selected test objects is 0.1 mg/l (10–5%). The histological analysis of a one-year-old carp that lived in an aquarium with a constant concentration of PHMG at 0.5 mg/l for 12 days showed that concentrations of an order of magnitude smaller – 0.01 mg/l (10–6%) is absolutely safe to consider. Chronic intoxication of fish caused by sublethal doses of PHMG leads to the development of numerous disorders in the liver, kidneys, and spleen, and to the inflammation of the pancreatic islets. A comparative analysis of the toxicity of PHMG for microand macroorganisms does not allow us to state that the latter are less sensitive to this xenobiotic. So far, there are not enough convincing reasons to believe that the mechanisms of action of PHMG on pro and eukaryotic cells are fundamentally different. At the same time, the binding of PHMG molecules to suspended particles in water, organic and inorganic impurities, flocculation, and biodegradation by microorganisms leads to a rapid decrease of free active molecules of this biocide in aquatic ecosystems.


Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.


Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.


Author(s):  
U. Aebi ◽  
E.C. Glavaris ◽  
R. Eichner

Five different classes of intermediate-sized filaments (IFs) have been identified in differentiated eukaryotic cells: vimentin in mesenchymal cells, desmin in muscle cells, neurofilaments in nerve cells, glial filaments in glial cells and keratin filaments in epithelial cells. Despite their tissue specificity, all IFs share several common attributes, including immunological crossreactivity, similar morphology (e.g. about 10 nm diameter - hence ‘10-nm filaments’) and the ability to reassemble in vitro from denatured subunits into filaments virtually indistinguishable from those observed in vivo. Further more, despite their proteinchemical heterogeneity (their MWs range from 40 kDa to 200 kDa and their isoelectric points from about 5 to 8), protein and cDNA sequencing of several IF polypeptides (for refs, see 1,2) have provided the framework for a common structural model of all IF subunits.


1982 ◽  
Vol 85 (1) ◽  
pp. 257-263 ◽  
Author(s):  
A. Graja ◽  
M. Przybylski ◽  
B. Butka ◽  
R. Swietlik

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