In VitroEffect of Valepotriates Isolated fromValeriana glechomifoliaon Rat P-Type ATPases
| Autor: | Gustavo M, Bettero, Luisa, Salles, Renata M, Rosário Figueira, Gilsane von, Poser, Stela M K, Rates, François, Noël, Luis Eduardo M, Quintas, Luis E M, Quintas |
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| Rok vydání: | 2011 |
| Předmět: |
Male
Valerianaceae SERCA ATPase Pharmaceutical Science Pharmacology Kidney Epithelium Sarcoplasmic Reticulum Calcium-Transporting ATPases Analytical Chemistry H(+)-K(+)-Exchanging ATPase Inhibitory Concentration 50 Valerian In vivo P-type ATPases Drug Discovery Botany Animals Iridoids Rats Wistar Adenosine Triphosphatases biology Chemistry Endoplasmic reticulum Stomach Organic Chemistry Brain biology.organism_classification In vitro Rats Complementary and alternative medicine biology.protein Molecular Medicine Valeriana Sodium-Potassium-Exchanging ATPase |
| Zdroj: | Planta Medica. 77:1702-1706 |
| ISSN: | 1439-0221 0032-0943 |
| DOI: | 10.1055/s-0030-1271084 |
| Popis: | Valepotriates are iridoids found in variable amounts in Valerianaceae and might be among the bioactive compounds which confer anxiolytic properties to the Valeriana species. On the other hand, unspecific cytotoxicity has also been described. Presently, however, no particular molecular target has been defined for these compounds. Here we studied the effect of valtrate, acevaltrate, and 1- β-acevaltrate isolated from Valeriana glechomifolia on the enzymatic activity of rat P-type ATPases. Valepotriates did not affect rat skeletal muscle sarco/endoplasmic reticulum Ca²⁺-ATPase (SERCA) activity at the highest concentration used (100 µM). In contrast, the same concentration inhibited roughly half of the total H⁺/K⁺-ATPase activity from rat gastric epithelium (valtrate 54.6 ± 3.2 %, acevaltrate 60.7 ± 7.3 %, 1- β-acevaltrate 50.2 ± 3.1 %; mean ± SEM, n = 3-5). Finally, these substances showed the highest inhibitory potency toward Na⁺/K⁺-ATPase, and the inhibition curves obtained provided a similar IC₅₀ (in µM) for rat kidney α1 isoform (valtrate 21.2, acevaltrate 22.8, 1- β-acevaltrate 24.4) and brain hemispheres α2/ α3 isoforms (valtrate 19.4, acevaltrate 42.3, 1- β-acevaltrate 38.3). Our results suggest that P-type ATPases are differentially inhibited by valepotriates and that Na⁺/K⁺-ATPase might be one of their molecular targets in vivo. |
| Databáze: | OpenAIRE |
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