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Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative

Bienzyme conjugate was obtained by the covalent connection of superoxide dismutase with catalase through endothelial glycocalyx glycosaminoglycan – chondroitin sulfate (SOD-CHS-CAT). This SOD-CHS-CAT conjugate has vasoprotective activity in respect to platelet interactions, tonus of the ring arteria...

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Autores principales: Maksimenko, A.V., Vavaev, A.V., Bouryachkovskaya, L.I., Mokh, V.P., Uchitel, I.A., Lakomkin, V.L., Kapelko, V.I., Tischenko, E.G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347582/
https://www.ncbi.nlm.nih.gov/pubmed/22649668
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author Maksimenko, A.V.
Vavaev, A.V.
Bouryachkovskaya, L.I.
Mokh, V.P.
Uchitel, I.A.
Lakomkin, V.L.
Kapelko, V.I.
Tischenko, E.G.
author_facet Maksimenko, A.V.
Vavaev, A.V.
Bouryachkovskaya, L.I.
Mokh, V.P.
Uchitel, I.A.
Lakomkin, V.L.
Kapelko, V.I.
Tischenko, E.G.
author_sort Maksimenko, A.V.
collection PubMed
description Bienzyme conjugate was obtained by the covalent connection of superoxide dismutase with catalase through endothelial glycocalyx glycosaminoglycan – chondroitin sulfate (SOD-CHS-CAT). This SOD-CHS-CAT conjugate has vasoprotective activity in respect to platelet interactions, tonus of the ring arterial fragment of a rat blood vessel, as well as normalization of hemodynamic parameters in rats and rabbits in conditions of oxidative stress caused by the administration of hydrogen peroxide. The SOD-CHS-CAT conjugate had antiplatelet potential due to its antiaggregation action manifested through the combination of enzyme activities and an acquired supramolecular structure. The influence on arterial fragment tonus was equivalent for SOD and CAT in native and conjugated form. Blood pressure and heart rate were significant and effectively normalized with SOD-CHS-CAT conjugate in rats and rabbits (after hydrogen peroxide administration as a perturbance stimulus). We have discovered the possibility of using the antioxidant bienzyme conjugate in chronic prophylaxis. It is important for a real development of the oral form of the SOD-CHS-CAT conjugate. These results indicate that the development of enzyme conjugates can be medically significant, as a promising approach for the creation of new drugs.
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spelling pubmed-33475822012-05-30 Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative Maksimenko, A.V. Vavaev, A.V. Bouryachkovskaya, L.I. Mokh, V.P. Uchitel, I.A. Lakomkin, V.L. Kapelko, V.I. Tischenko, E.G. Acta Naturae Research Article Bienzyme conjugate was obtained by the covalent connection of superoxide dismutase with catalase through endothelial glycocalyx glycosaminoglycan – chondroitin sulfate (SOD-CHS-CAT). This SOD-CHS-CAT conjugate has vasoprotective activity in respect to platelet interactions, tonus of the ring arterial fragment of a rat blood vessel, as well as normalization of hemodynamic parameters in rats and rabbits in conditions of oxidative stress caused by the administration of hydrogen peroxide. The SOD-CHS-CAT conjugate had antiplatelet potential due to its antiaggregation action manifested through the combination of enzyme activities and an acquired supramolecular structure. The influence on arterial fragment tonus was equivalent for SOD and CAT in native and conjugated form. Blood pressure and heart rate were significant and effectively normalized with SOD-CHS-CAT conjugate in rats and rabbits (after hydrogen peroxide administration as a perturbance stimulus). We have discovered the possibility of using the antioxidant bienzyme conjugate in chronic prophylaxis. It is important for a real development of the oral form of the SOD-CHS-CAT conjugate. These results indicate that the development of enzyme conjugates can be medically significant, as a promising approach for the creation of new drugs. A.I. Gordeyev 2010 /pmc/articles/PMC3347582/ /pubmed/22649668 Text en Copyright © 2010 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Maksimenko, A.V.
Vavaev, A.V.
Bouryachkovskaya, L.I.
Mokh, V.P.
Uchitel, I.A.
Lakomkin, V.L.
Kapelko, V.I.
Tischenko, E.G.
Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative
title Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative
title_full Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative
title_fullStr Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative
title_full_unstemmed Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative
title_short Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative
title_sort biopharmacology of enzyme conjugates: vasoprotective activity of supramolecular superoxide dismutase-chondroitin sulfate-catalase derivative
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347582/
https://www.ncbi.nlm.nih.gov/pubmed/22649668
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