English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
 Local TagsRelease HistoryDetailsSummary
  Epigallocatechin-3-gallate is an inhibitor of Na+,K+-ATPase by favoring the E1 conformation

Ochiai, H., Takeda, K., Soeda, S., Tahara, Y., Takenaka, H., Abe, K., et al. (2009). Epigallocatechin-3-gallate is an inhibitor of Na+,K+-ATPase by favoring the E1 conformation. Biochemical Pharmacology, 78(8), 1069-1074. doi:10.1016/j.bcp.2009.06.007.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D745-D Version Permalink: https://hdl.handle.net/21.11116/0000-000A-7110-4
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Ochiai, Hideo1, 2, Author
Takeda, Kazuo3, Author
Soeda, Shiori1, Author
Tahara, Yoshikazu3, Author
Takenaka, Hitoshi3, Author
Abe, Kazuhiro4, Author
Hayashi, Yutaro3, Author
Noguchi, Shunsuke1, Author
Inoue, Masumi2, Author
Schwarz, Silvia5, Author
Schwarz, Wolfgang5, 6, Author           
Kawamura, Masaru1, Author
Affiliations:
1Department of Cell Biology, University of Occupational and Environmental Health, Iseigaoka, Yahatanishiku, Kitakyushu 807-8555, Japan, ou_persistent22              
2Department of Cell and Systems Physiology, University of Occupational and Environmental Health, Kitakyushu 807-8555, Japan, ou_persistent22              
3Department of Biochemistry, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan, ou_persistent22              
4Department of Biophysics, Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan, ou_persistent22              
5Shanghai Research Center for Acupuncture and Medrians, Shanghai-Pudong 201203, China, ou_persistent22              
6Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

Content

show
hide
Free keywords: Epigallocatechin-3-gallate; Na+,K+-ATPase; Inhibition; P-type ATPase; Phospholipid
 Abstract: Four catechins, epigallocatechin-3-gallate, epigallocatechin, epicatechin-3-gallate, and epicatechin, inhibited activity of the Na+,K+-ATPase. The two galloyl-type catechins were more potent inhibitors, with IC50 values of about 1 μM, than were the other two catechins. Inhibition by epigallocatechin-3-gallate was noncompetitive with respect to ATP. Epigallocatechin-3-gallate reduced the affinity of vanadate, shifted the equilibrium of E1P and E2P toward E1P, and reduced the rate of the E1P to E2P transition. Epigallocatechin-3-gallate potently inhibited membrane-embedded P-type ATPases (gastric H+,K+-ATPase and sarcoplasmic reticulum Ca2+-ATPase) as well as the Na+,K+-ATPase, whereas soluble ATPases (bacterial F1-ATPase and myosin ATPase) were weakly inhibited. Solubilization of the Na+,K+-ATPase with a nonionic detergent reduced sensitivity to epigallocatechin-3-gallate with an elevation of IC50 to 10 μM. These results suggest that epigallocatechin-3-gallate exerts its inhibitory effect through interaction with plasma membrane phospholipid.

Details

show
hide
Language(s): eng - English
 Dates: 2019-04-162009-06-082009-06-172009-10-15
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bcp.2009.06.007
PMID: 19539611
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemical Pharmacology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam, Boston : Elsevier
Pages: - Volume / Issue: 78 (8) Sequence Number: - Start / End Page: 1069 - 1074 Identifier: ISSN: 0006-2952
CoNE: https://pure.mpg.de/cone/journals/resource/954925384102