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dc.contributor.author
Cerrato, Bruno Diego
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dc.contributor.author
Carretero, Oscar A.
dc.contributor.author
Janic, Brana
dc.contributor.author
Grecco, Hernan Edgardo
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dc.contributor.author
Gironacci, Mariela Mercedes
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dc.date.available
2018-06-04T20:46:28Z
dc.date.issued
2016-10
dc.identifier.citation
Cerrato, Bruno Diego; Carretero, Oscar A.; Janic, Brana; Grecco, Hernan Edgardo; Gironacci, Mariela Mercedes; Heteromerization Between the Bradykinin B 2 Receptor and the Angiotensin-(1-7) Mas Receptor Novelty and Significance; Lippincott Williams; Hypertension; 68; 4; 10-2016; 1039-1048
dc.identifier.issn
0194-911X
dc.identifier.uri
http://hdl.handle.net/11336/47238
dc.description.abstract
Bradykinin B2 receptor (B2R) and angiotensin-(1–7) Mas receptor (MasR)–mediated effects are physiologically interconnected. The molecular basis for such cross talk is unknown. It is hypothesized that the cross talk occurs at the receptor level. We investigated B2R–MasR heteromerization and the functional consequences of such interaction. B2R fused to the cyan fluorescent protein and MasR fused to the yellow fluorescent protein were transiently coexpressed in human embryonic kidney293T cells. Fluorescence resonance energy transfer analysis showed that B2R and MasR formed a constitutive heteromer, which was not modified by their agonists. B2R or MasR antagonists decreased fluorescence resonance energy transfer efficiency, suggesting that the antagonist promoted heteromer dissociation. B2R–MasR heteromerization induced an 8-fold increase in the MasR ligand-binding affinity. On agonist stimulation, the heteromer was internalized into early endosomes with a slower sequestration rate from the plasma membrane, compared with single receptors. B2R–MasR heteromerization induced a greater increase in arachidonic acid release and extracellular signal–regulated kinase phosphorylation after angiotensin-(1–7) stimulation, and this effect was blocked by the B2R antagonist. Concerning serine/threonine kinase Akt activity, a significant bradykinin-promoted activation was detected in B2R–MasR but not in B2R-expressing cells. Angiotensin-(1–7) and bradykinin elicited antiproliferative effects only in cells expressing B2R–MasR heteromers, but not in cells expressing each receptor alone. Proximity ligation assay confirmed B2R–MasR interaction in human glomerular endothelial cells supporting the interaction between both receptors in vivo. Our findings provide an explanation for the cross talk between bradykinin B2R and angiotensin-(1–7) MasR–mediated effects. B2R–MasR heteromerization induces functional changes in the receptor that may lead to long-lasting protective properties.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Lippincott Williams
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
B2 Receptor
dc.subject
Heteromerization
dc.subject
Internalization
dc.subject
Mas Receptor
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Heteromerization Between the Bradykinin B 2 Receptor and the Angiotensin-(1-7) Mas Receptor Novelty and Significance
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-04T17:30:54Z
dc.journal.volume
68
dc.journal.number
4
dc.journal.pagination
1039-1048
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Cerrato, Bruno Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
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Fil: Carretero, Oscar A.. Henry Ford Hospital; Estados Unidos
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Fil: Janic, Brana. Henry Ford Hospital; Estados Unidos
dc.description.fil
Fil: Grecco, Hernan Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina
dc.description.fil
Fil: Gironacci, Mariela Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.journal.title
Hypertension
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1161/HYPERTENSIONAHA.116.07874
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://hyper.ahajournals.org/content/68/4/1039
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5016258/
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