Planta Med 2011; 77(15): 1702-1706
DOI: 10.1055/s-0030-1271084
Biological and Pharmacological Activity
Original Papers
© Georg Thieme Verlag KG Stuttgart · New York

In Vitro Effect of Valepotriates Isolated from Valeriana glechomifolia on Rat P-Type ATPases

Gustavo M. Bettero1 [*] , Luisa Salles2 , 3 [*] , Renata M. Rosário Figueira1 , Gilsane von Poser2 , Stela M. K. Rates3 , François Noël1 , Luis E. M. Quintas1
  • 1Laboratório de Farmacologia Bioquímica e Molecular, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
  • 2Programa de Pós-Graduação em Ciências Farmacêuticas, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil
  • 3Laboratório de Psicofarmacologia Experimental, Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil
Further Information

Publication History

received Nov. 1, 2010 revised April 9, 2011

accepted April 14, 2011

Publication Date:
12 May 2011 (eFirst)

Abstract

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.

Supporting Information

References

1 These authors equally contributed to this work.

Prof. Dr. Luis Eduardo M. Quintas

Laboratório de Farmacologia Bioquímica e Molecular
Instituto de Ciências Biomédicas
Universidade Federal do Rio de Janeiro

Av. Carlos Chagas Filho 373

Bloco J, sala J-17, CCS

21941-902, Rio de Janeiro

Brazil

Phone: +55 21 25 62 67 32

Email: lquintas@farmaco.ufrj.br