Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life

Research output: Contribution to journalJournal articleResearchpeer-review

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Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life. / Dao, Trong Tuan; Sehgal, Pankaj; Thanh Tung, Truong; Møller, Jesper Vuust; Nielsen, John; Palmgren, Michael Broberg; Christensen, Søren Brøgger; Fuglsang, Anja Thoe.

In: P L o S One, Vol. 11, No. 9, e0163260, 2016.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Dao, TT, Sehgal, P, Thanh Tung, T, Møller, JV, Nielsen, J, Palmgren, MB, Christensen, SB & Fuglsang, AT 2016, 'Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life', P L o S One, vol. 11, no. 9, e0163260. https://doi.org/10.1371/journal.pone.0163260

APA

Dao, T. T., Sehgal, P., Thanh Tung, T., Møller, J. V., Nielsen, J., Palmgren, M. B., Christensen, S. B., & Fuglsang, A. T. (2016). Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life. P L o S One, 11(9), [e0163260]. https://doi.org/10.1371/journal.pone.0163260

Vancouver

Dao TT, Sehgal P, Thanh Tung T, Møller JV, Nielsen J, Palmgren MB et al. Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life. P L o S One. 2016;11(9). e0163260. https://doi.org/10.1371/journal.pone.0163260

Author

Dao, Trong Tuan ; Sehgal, Pankaj ; Thanh Tung, Truong ; Møller, Jesper Vuust ; Nielsen, John ; Palmgren, Michael Broberg ; Christensen, Søren Brøgger ; Fuglsang, Anja Thoe. / Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life. In: P L o S One. 2016 ; Vol. 11, No. 9.

Bibtex

@article{53e1e7e3ac204dbe879eb52a5ebb523a,
title = "Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life",
abstract = "P-type ATPases catalyze the active transport of cations and phospholipids across biological membranes. Members of this large family are involved in a range of fundamental cellular processes. To date, a substantial number of P-type ATPase inhibitors have been characterized, some of which are used as drugs. In this work a library of natural compounds was screened and we first identified curcuminoids as plasma membrane H+-ATPases inhibitors in plant and fungal cells. We also found that some of the commercial curcumins contain several curcuminoids. Three of these were purified and, among the curcuminoids, demethoxycurcumin was the most potent inhibitor of all tested P-type ATPases from fungal (Pma1p; H+-ATPase), plant (AHA2; H+-ATPase) and animal (SERCA; Ca2+-ATPase) cells. All three curcuminoids acted as non-competitive antagonist to ATP and hence may bind to a highly conserved allosteric site of these pumps. Future research on biological effects of commercial preparations of curcumin should consider the heterogeneity of the material.",
keywords = "Journal Article",
author = "Dao, {Trong Tuan} and Pankaj Sehgal and {Thanh Tung}, Truong and M{\o}ller, {Jesper Vuust} and John Nielsen and Palmgren, {Michael Broberg} and Christensen, {S{\o}ren Br{\o}gger} and Fuglsang, {Anja Thoe}",
year = "2016",
doi = "10.1371/journal.pone.0163260",
language = "English",
volume = "11",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "9",

}

RIS

TY - JOUR

T1 - Demethoxycurcumin is a potent inhibitor of P-type ATPases from diverse kingdoms of life

AU - Dao, Trong Tuan

AU - Sehgal, Pankaj

AU - Thanh Tung, Truong

AU - Møller, Jesper Vuust

AU - Nielsen, John

AU - Palmgren, Michael Broberg

AU - Christensen, Søren Brøgger

AU - Fuglsang, Anja Thoe

PY - 2016

Y1 - 2016

N2 - P-type ATPases catalyze the active transport of cations and phospholipids across biological membranes. Members of this large family are involved in a range of fundamental cellular processes. To date, a substantial number of P-type ATPase inhibitors have been characterized, some of which are used as drugs. In this work a library of natural compounds was screened and we first identified curcuminoids as plasma membrane H+-ATPases inhibitors in plant and fungal cells. We also found that some of the commercial curcumins contain several curcuminoids. Three of these were purified and, among the curcuminoids, demethoxycurcumin was the most potent inhibitor of all tested P-type ATPases from fungal (Pma1p; H+-ATPase), plant (AHA2; H+-ATPase) and animal (SERCA; Ca2+-ATPase) cells. All three curcuminoids acted as non-competitive antagonist to ATP and hence may bind to a highly conserved allosteric site of these pumps. Future research on biological effects of commercial preparations of curcumin should consider the heterogeneity of the material.

AB - P-type ATPases catalyze the active transport of cations and phospholipids across biological membranes. Members of this large family are involved in a range of fundamental cellular processes. To date, a substantial number of P-type ATPase inhibitors have been characterized, some of which are used as drugs. In this work a library of natural compounds was screened and we first identified curcuminoids as plasma membrane H+-ATPases inhibitors in plant and fungal cells. We also found that some of the commercial curcumins contain several curcuminoids. Three of these were purified and, among the curcuminoids, demethoxycurcumin was the most potent inhibitor of all tested P-type ATPases from fungal (Pma1p; H+-ATPase), plant (AHA2; H+-ATPase) and animal (SERCA; Ca2+-ATPase) cells. All three curcuminoids acted as non-competitive antagonist to ATP and hence may bind to a highly conserved allosteric site of these pumps. Future research on biological effects of commercial preparations of curcumin should consider the heterogeneity of the material.

KW - Journal Article

U2 - 10.1371/journal.pone.0163260

DO - 10.1371/journal.pone.0163260

M3 - Journal article

C2 - 27644036

VL - 11

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 9

M1 - e0163260

ER -

ID: 166196698