Evidence map›Paper›PMID 35038454›Full record

ArticleLife sciences2022

ACE2 internalization induced by a SARS-CoV-2 recombinant protein is modulated by angiotensin II type 1 and bradykinin 2 receptors.

Andrea Estefanía Portales, Emilio Román Mustafá, Clara Inés McCarthy, María Paula Cornejo, Paula Monserrat Couto, Mariela Mercedes Gironacci, Julio Javier Caramelo, Mario Perelló, Jesica Raingo

Open access · greenAbstract read
In one paragraph

Article in Life sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 19 citations in OpenAlex.

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  10. [Angiotensin-converting enzyme 2 particapates in ozone-induced lung inflammation and airway remodeling in mice].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Andrea Estefanía PortalesLaboratorio de Electrofisiología, Instituto Multidisciplinario de Biología Celular (IMBICE), Universidad Nacional de La Plata (UNLP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (CIC), Calle 526 1499-1579, B1906APM Tolosa, Buenos Aires, Argentina.
Emilio Román MustafáLaboratorio de Electrofisiología, Instituto Multidisciplinario de Biología Celular (IMBICE), Universidad Nacional de La Plata (UNLP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (CIC), Calle 526 1499-1579, B1906APM Tolosa, Buenos Aires, Argentina.
Clara Inés McCarthyLaboratorio de Electrofisiología, Instituto Multidisciplinario de Biología Celular (IMBICE), Universidad Nacional de La Plata (UNLP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (CIC), Calle 526 1499-1579, B1906APM Tolosa, Buenos Aires, Argentina.
María Paula CornejoLaboratorio de Neurofisiología, Instituto Multidisciplinario de Biología Celular (IMBICE), Universidad Nacional de La Plata (UNLP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (CIC), Calle 526 1499-1579, B1906APM Tolosa, Buenos Aires, Argentina.
Paula Monserrat CoutoFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina.
Mariela Mercedes GironacciUniversidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (IQUIFIB, UBA-CONICET), Argentina.
Julio Javier CarameloFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina.
Mario PerellóLaboratorio de Neurofisiología, Instituto Multidisciplinario de Biología Celular (IMBICE), Universidad Nacional de La Plata (UNLP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (CIC), Calle 526 1499-1579, B1906APM Tolosa, Buenos Aires, Argentina.
Jesica RaingoLaboratorio de Electrofisiología, Instituto Multidisciplinario de Biología Celular (IMBICE), Universidad Nacional de La Plata (UNLP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (CIC), Calle 526 1499-1579, B1906APM Tolosa, Buenos Aires, Argentina.. Electronic address: jraingo@imbice.gov.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of Buenos Aires · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aimsAngiotensin-converting enzyme 2 (ACE2) is a key regulator of the renin-angiotensin system (RAS) recently identified as the membrane receptor for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Here we aim to study whether two receptors from RAS, the angiotensin receptor type 1 (AT1R) and the bradykinin 2 receptor (B2R) modulate ACE2 internalization induced by a recombinant receptor binding domain (RBD) of SARS-CoV-2 spike protein. Also, we investigated the impact of ACE2 coexpression on AT1R and B2R functionality. MATERIALS AND

methodsTo study ACE2 internalization, we assessed the distribution of green fluorescent protein (GFP) signal in HEK293T cells coexpressing GFP-tagged ACE2 and AT1R, or B2R, or AT1R plus B2R in presence of RBD alone or in combination with AT1R or B2R ligands. To estimate ACE2 internalization, we classified GFP signal distribution as plasma membrane uniform GFP (PMU-GFP), plasma membrane clustered GFP (PMC-GFP) or internalized GFP and calculated its relative frequency. Additionally, we investigated the effect of ACE2 coexpression on AT1R and B2R inhibitory action on voltage-gated calcium channels (Ca KEY

findingsRBD induced ACE2-GFP internalization in a time-dependent manner. RBD-induced ACE2-GFP internalization was increased by angiotensin II and reduced by telmisartan in cells coexpressing AT1R. RBD-induced ACE2-GFP internalization was strongly inhibited by B2R co-expression. This effect was mildly modified by bradykinin and rescued by angiotensin II in presence of AT1R. ACE2 coexpression impacted on B2R- and AT1R-mediated inhibition of Ca SIGNIFICANCE: Our work contributes to understand the role of RAS modulators in the susceptibility to SARS-CoV-2 infection and severity of COVID-19.

Indexed as

Angiotensin-Converting Enzyme 2Angiotensin IIAngiotensin II Type 1 Receptor BlockersGreen Fluorescent ProteinsHEK293 CellsHumansReceptor, Angiotensin, Type 1Receptor, Bradykinin B2Recombinant ProteinsSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Angiotensin IIAngiotensin II Type 1 Receptor BlockersGreen Fluorescent ProteinsReceptor, Angiotensin, Type 1Receptor, Bradykinin B2Recombinant ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2Angiotensin IIAT1RB2RSARS-CoV-2Telmisartan

Identifiers

PMID35038454
PMCPMC8758573
OpenAlexW4206633440

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.