Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain

Daniel W. Lambert; Nicola E. Clarke; Nigel M. Hooper; Anthony J. Turner

doi:S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085

Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain

Daniel W. Lambert
, Nicola E. Clarke
, Nigel M. Hooper
, Anthony J. Turner

Research output: Contribution to journal › Article › peer-review

Abstract

Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin-angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-α converting enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors. © 2007 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	385-390
Number of pages	5
Journal	FEBS Letters
Volume	582
Issue number	2
DOIs	https://doi.org/S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085
Publication status	Published - 23 Jan 2008

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

ACE
ACE2
Calmodulin
Collectrin
Shedding

Research Highlights, Institutes and Platforms

Dementia@Manchester

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S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085

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title = "Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain",

abstract = "Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin-angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-α converting enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors. {\textcopyright} 2007 Federation of European Biochemical Societies.",

keywords = "ACE, ACE2, Calmodulin, Collectrin, Shedding",

author = "Lambert, \{Daniel W.\} and Clarke, \{Nicola E.\} and Hooper, \{Nigel M.\} and Turner, \{Anthony J.\}",

note = "Lambert, Daniel W Clarke, Nicola E Hooper, Nigel M Turner, Anthony J Research Support, Non-U.S. Gov't Netherlands FEBS letters FEBS Lett. 2008 Jan 23;582(2):385-90. Epub 2007 Dec 10.",

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doi = "S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085",

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T1 - Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain

AU - Lambert, Daniel W.

AU - Clarke, Nicola E.

AU - Hooper, Nigel M.

AU - Turner, Anthony J.

N1 - Lambert, Daniel W Clarke, Nicola E Hooper, Nigel M Turner, Anthony J Research Support, Non-U.S. Gov't Netherlands FEBS letters FEBS Lett. 2008 Jan 23;582(2):385-90. Epub 2007 Dec 10.

PY - 2008/1/23

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N2 - Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin-angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-α converting enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors. © 2007 Federation of European Biochemical Societies.

AB - Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin-angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-α converting enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors. © 2007 Federation of European Biochemical Societies.

KW - ACE

KW - ACE2

KW - Calmodulin

KW - Collectrin

KW - Shedding

U2 - S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085

DO - S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085

M3 - Article

VL - 582

SP - 385

EP - 390

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain

Abstract

UN SDGs

Keywords

Research Highlights, Institutes and Platforms

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