Effects of (-)-epigallocatechin-3-gallate, the main component of green tea, on the cloned rat brain Kv1.5 potassium channels

Bok Hee Choi, Jin Sung Choi, Do Sik Min, Shin Hee Yoon, Duck Joo Rhie, Yang Hyeok Jo, Myung Suk Kim, Sang June Hahn

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33 Citations (Scopus)


The interaction of (-)-epigallocatechin-3-gallate (EGCG), the main component of green tea (Camellia sinensis), with rat brain Kv1.5 channels (rKv1.5) stably expressed in Chinese hamster ovary (CHO) cells was investigated using the whole-cell patch-clamp technique. EGCG inhibited rKv1.5 currents at +50 mV in a concentration-dependent manner, with an IC50 of 101.2 ± 6.2 μM. Pretreatment with protein tyrosine kinase (PTK) inhibitors (10 μM genistein, 100 μM AG1296), a tyrosine phosphatase inhibitor (500 μM sodium orthovanadate), or a protein kinase C (PKC) inhibitor (10 μM chelerythrine) did not block the inhibitory effect of EGCG on rKv1.5. The inhibition of rKv1.5 by EGCG displayed voltage-independence over the full activation voltage range positive to +10 mV. EGCG had no effect on the midpoint potential or the slope factor for steady-state activation and inactivation. EGCG did not affect the ion selectivity of rKv1.5. The activation (at +50 mV) kinetics was significantly slowed by EGCG. During repolarization (at -40 mV), EGCG also slowed the deactivation of the tail currents, resulting in a crossover phenomenon. Reversal of inhibition was detected by the application of repetitive depolarizing pulses and of identical double pulses, especially during the early part of the activating pulse, in the presence of EGCG. EGCG-induced inhibition of rKv1.5 showed identical affinity between EGCG and the multiple closed states of rKv1.5. These results suggest that EGCG interacts directly with rKv1.5 channels. Furthermore, by analyzing the kinetics of the interaction between EGCG and rKv1.5, we conclude that the inhibition of rKv1.5 channels by EGCG includes at least two effects: EGCG preferentially binds to the channel in the closed state, and blocks the channel by pore occlusion while depolarization is maintained.

Original languageEnglish
Pages (from-to)527-535
Number of pages9
JournalBiochemical Pharmacology
Issue number5
Publication statusPublished - 2001 Sept 1

Bibliographical note

Funding Information:
We thank Dr. Leonard Kaczmarek (Yale University School of Medicine, USA) for the rKv1.5 cDNA and Won Kim for reading the manuscript. This work was supported by a Korea Research Foundation Grant (KRF-2000-015-FP0026).

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Pharmacology


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