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      Protective Effect of Bergapten against Human Erythrocyte Hemolysis and Protein Denaturation In Vitro

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          Abstract

          Bergapten, a furocoumarin found in many medicinal plants, is used for the management of various conditions. The present in vitro study evaluated the ability of bergapten to prevent human erythrocyte hemolysis and protein denaturation. Bergapten administered at 10, 30, and 100  μg/ml exhibited a significant concentration-dependent protection on the erythrocyte membrane exposed to hypotonicity and heat-induced hemolysis. The concentration at which bergapten inhibited 50% of the cells from hemolysis (IC 50) was determined on a dose-response curve, plotted as logarithmic (concentration) against percentage inhibition, keeping the hemolysis produced within the control group at 100%. Bergapten treatment produced an IC 50 value of 7.71 ± 0.27  μg/ml and 4.23 ± 0.42  μg/ml for hypotonicity and heat-induced hemolysis, respectively. Diclofenac sodium at similar concentrations produced an IC 50 value of 12.22 ± 0.30  μg/ml and 9.44 ± 0.23  μg/ml in the hypotonicity and heat-induced hemolysis, respectively. The ability of bergapten to inhibit protein denaturation was studied as part of an investigation on its mechanism of action. The results showed a significant concentration-dependent reduction in protein denaturation. When administered at 10, 30, and 100  μg/ml, bergapten produced a concentration-dependent reduction in albumin denaturation. Bergapten inhibited protein denaturation with IC 50 values of 5.34 ± 0.30  μg/ml and 12.18 ± 0.20  μg/ml in the heat-treated egg albumin and bovine serum albumin denaturation experiments, respectively. Diclofenac sodium (10, 30, and 100  μg/ml) exhibited a similar protection against heat-treated egg albumin and bovine serum albumin denaturation experiments with IC 50 values of 8.93 ± 0.17  μg/ml and 12.72 ± 0.11  μg/ml, respectively. Taken together, data from this study show that the pharmacological properties of bergapten may in part be related to its membrane-stabilizing and antidenaturation properties.

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          Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?

          Free radicals and other reactive species (RS) are thought to play an important role in many human diseases. Establishing their precise role requires the ability to measure them and the oxidative damage that they cause. This article first reviews what is meant by the terms free radical, RS, antioxidant, oxidative damage and oxidative stress. It then critically examines methods used to trap RS, including spin trapping and aromatic hydroxylation, with a particular emphasis on those methods applicable to human studies. Methods used to measure oxidative damage to DNA, lipids and proteins and methods used to detect RS in cell culture, especially the various fluorescent "probes" of RS, are also critically reviewed. The emphasis throughout is on the caution that is needed in applying these methods in view of possible errors and artifacts in interpreting the results.
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            Membrane stabilizing activity — a possible mechanism of action for the anti-inflammatory activity of Cedrus deodara wood oil

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              Disorders of red cell membrane.

              Studies during the last three decades have enabled the development of detailed molecular insights into the structural basis of altered function in various inherited red cell membrane disorders. This review highlights our current understanding of molecular and mechanistic insights into various inherited red cell membrane disorders involving either altered membrane structural organization (hereditary spherocytosis, hereditary elliptocytosis and hereditary ovalocytosis) or altered membrane transport function (hereditary stomatocytosis). The molecular basis for the vast majority of cases of hereditary spherocytosis, elliptocytosis and ovalocytosis have been fully defined while little progress has been made in defining the molecular basis for hereditary stomatocytosis. Mutations in a number of distinct genes account for hereditary spherocytosis and elliptocytosis, while a single genetic defect accounts for all cases of hereditary ovalocytosis. Based on these molecular insights, a comprehensive understanding of the structural basis for altered membrane function has been developed. Loss of vertical linkage between membrane skeleton and lipid bilayer leads to membrane loss in hereditary spherocytosis, while weakening of lateral linkages between skeletal proteins leads to membrane fragmentation and surface area loss in hereditary elliptocytosis. Importantly, the severity of anaemia in both these disorders is directly related to extent of membrane surface area loss. Splenectomy results in amelioration of anaemia.
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                Author and article information

                Contributors
                Journal
                Int J Inflam
                Int J Inflam
                iji
                International Journal of Inflammation
                Hindawi
                2090-8040
                2042-0099
                2021
                21 December 2021
                : 2021
                : 1279359
                Affiliations
                1Department of Pharmacology, Faculty of Pharmacy and Pharmaceutical Sciences, College of Health Sciences, Kwame Nkrumah University of Science & Technology, Kumasi, Ghana
                2Department of Biomedical Sciences, School of Allied Health Sciences, University of Cape Coast, Cape Coast, Ghana
                3Department of Pharmacotherapeutics and Pharmacy Practice, School of Pharmacy and Pharmaceutical Sciences, College of Health and Allied Sciences, University of Cape Coast, Cape Coast, Ghana
                4Department of Pharmacology, School of Medical Sciences, College of Health and Allied Sciences, University of Cape Coast, Cape Coast, Ghana
                Author notes

                Academic Editor: Sachchida Nand Rai

                Author information
                https://orcid.org/0000-0002-8361-9006
                https://orcid.org/0000-0003-1515-8938
                https://orcid.org/0000-0002-6830-0283
                https://orcid.org/0000-0002-4683-0988
                Article
                10.1155/2021/1279359
                8714387
                6a0d27c2-d238-47d1-b890-958f39abf925
                Copyright © 2021 Douglas Bosco Aidoo et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 4 October 2021
                : 7 December 2021
                : 10 December 2021
                Funding
                Funded by: Kwame Nkrumah University of Science and Technology
                Categories
                Research Article

                Immunology
                Immunology

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