About: The Identification of a Calmodulin-Binding Domain within the Cytoplasmic Tail of Angiotensin-Converting Enzyme-2

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About: The Identification of a Calmodulin-Binding Domain within the Cytoplasmic Tail of Angiotensin-Converting Enzyme-2 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The Identification of a Calmodulin-Binding Domain within the Cytoplasmic Tail of Angiotensin-Converting Enzyme-2
Creator	Lew, Rebecca Smith, A Andrews, Robert Lai, Zon Mu, Fi-Tjen Yarski, Michael
Source	Medline; PMC
abstract	Angiotensin-converting enzyme (ACE)-2 is a homolog of the well-characterized plasma membrane-bound angiotensin-converting enzyme. ACE2 is thought to play a critical role in regulating heart function, and in 2003, ACE2 was identified as a functional receptor for severe acute respiratory syndrome coronavirus. We have recently shown that like ACE, ACE2 undergoes ectodomain shedding and that this shedding event is up-regulated by phorbol esters. In the present study, we used gel shift assays to demonstrate that calmodulin, an intracellular calcium-binding protein implicated in the regulation of other ectodomain shedding events, binds a 16-amino acid synthetic peptide corresponding to residues 762–777 within the cytoplasmic domain of human ACE2, forming a calcium-dependent calmodulin-peptide complex. Furthermore, we have demonstrated that ACE2 expressed in Chinese hamster ovary cells specifically binds to glutathione-S-transferase-calmodulin, but not glutathione-S-transferase alone, in pull-down assays using cell lysates. Finally, to investigate whether calmodulin has any effect on ACE2 ectodomain shedding in cells that endogenously express the enzyme, cells from a human liver cell line (Huh-7) expressing ACE2 were incubated with calmodulin-specific inhibitors, trifluoperazine and calmidazolium. Both trifluoperazine (25 μmol/liter) and calmidazolium, (25 μmol/liter) significantly increased the release of ACE2 into the medium (44.1 ± 10.8%, P < 0.05, Student’s t test; unpaired, two-tailed, and 51.1 ± 7.4% P < 0.05, one-way ANOVA, respectively;), as analyzed by an ACE2-specific quenched fluorescence substrate assay. We also show that the calmodulin-specific inhibitor-stimulated shedding of ACE2 is independent from phorbol ester-induced shedding. In summary, we have demonstrated that calmodulin is able to bind ACE2 and suggest that the ACE2 ectodomain shedding and/or sheddase(s) activation regulated by calmodulin is independent from the phorbol ester-induced shedding.
has issue date	2009-05-01(xsd:dateTime)
bibo:doi	10.1210/en.2008-1274
bibo:pmid	19164471
has license	no-cc
sha1sum (hex)	1eabe78df060e1b57ffaf8477b939198de0d9409
schema:url	https://doi.org/10.1210/en.2008-1274
resource representing a document's title	The Identification of a Calmodulin-Binding Domain within the Cytoplasmic Tail of Angiotensin-Converting Enzyme-2
has PubMed Central identifier	PMC7108506
has PubMed identifier	19164471
schema:publication	Endocrinology
resource representing a document's body	covid:1eabe78df060e1b57ffaf8477b939198de0d9409#body_text
is schema:about of	named entity 'ACE2' named entity 'quenched' named entity 'Angiotensin-converting enzyme' named entity 'gel' named entity 'test' named entity 'functional' named entity 'ACE' named entity 'Tail' named entity 'CALMODULIN' named entity 'EXPRESSED' named entity 'CALMODULIN' named entity 'PLASMA MEMBRANE' named entity 'CRITICAL' named entity '51.1' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'CALCIUM-BINDING PROTEIN' named entity 'INDUCED' named entity 'TAILED' named entity 'LIKE' named entity 'SHEDDING' named entity 'GLUTATHIONE' named entity 'PLAY' named entity 'REGULATION' named entity 'SUMMARY' named entity 'FORMING' named entity 'SUBSTRATE' named entity 'USED' named entity 'HOMOLOG' named entity 'USING' named entity 'ASSAY' named entity 'ENZYME' named entity 'LIVER CELL LINE' named entity 'TRIFLUOPERAZINE' named entity 'INTRACELLULAR CALCIUM' named entity 'UNPAIRED' named entity '0.05' named entity 'BOUND' named entity 'CELLS' named entity 'INCUBATED' named entity 'EXPRESS' named entity 'THOUGHT' named entity 'UP-REGULATED' named entity 'OVARY' named entity 'AMINO ACID' named entity 'TRANSFERASE' named entity 'EVENTS' named entity 'ROLE' covid:arg/1eabe78df060e1b57ffaf8477b939198de0d9409 named entity 'STUDENT' named entity 'HAVE' named entity 'INHIBITOR' named entity 'BUT' named entity 'PRESENT' named entity 'CHINESE HAMSTER' named entity '28S' named entity '762' named entity '150' named entity '10.8' named entity 'INHIBITORS' named entity 'BIND' named entity '777' named entity 'FUNCTIONAL' named entity 'CHARACTERIZED' named entity 'RECENTLY' named entity 'PHORBOL ESTERS' named entity 'SYNTHETIC PEPTIDE' named entity 'BINDING' named entity 'IDENTIFICATION' named entity '7.4' named entity 'REGULATED' named entity 'EFFECT' named entity 'CYTOPLASMIC DOMAIN' named entity 'ANALYZED' named entity 'DOMAIN' named entity 'BINDS' named entity 'PULL'

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