Dynamic regulation of extracellular ATP in <i>Escherichia coli</i>

dc.creatorAlvarez, Cora Lilia
dc.creatorCorradi, Gerardo Raúl
dc.creatorLauri, Natalia
dc.creatorMarginedas Freixa, Irene
dc.creatorLeal Denis, Maria Florencia
dc.creatorEnrique, Nicolás Jorge
dc.creatorMaté, Sabina María
dc.creatorMilesi, Verónica
dc.creatorOstuni, Mariano Aníbal
dc.creatorHerlax, Vanesa Silvana
dc.creatorSchwarzbaum, Pablo Julio
dc.date2017-04
dc.date2020-05-21T15:45:41Z
dc.date.accessioned2023-07-14T19:51:18Z
dc.date.available2023-07-14T19:51:18Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/96491
dc.identifierhttps://ri.conicet.gov.ar/11336/49158
dc.identifierhttp://www.biochemj.org/content/474/8/1395.long
dc.identifierissn:0264-6021
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7436946
dc.descriptionWe studied the kinetics of extracellular ATP (ATPe) in Escherichia coli and their outer membrane vesicles (OMVs) stimulated with amphipatic peptides melittin (MEL) and mas-toparan 7 (MST7). Real-time luminometry was used to measure ATPe kinetics, ATP release, and ATPase activity. The latter was also determined by following [32P]Pi released from [γ-32P]ATP. E. coli was studied alone, co-incubated with Caco-2 cells, or in rat jejunum segments. In E. coli, the addition of [γ-32P]ATP led to the uptake and subsequent hydrolysis of ATPe. Exposure to peptides caused an acute 3-fold (MST7) and 7-fold (MEL) increase in [ATPe]. In OMVs, ATPase activity increased linearly with [ATPe] (0.1-1 mM). Exposure to MST7 and MEL enhanced ATP release by 3-7 fold, with similar kinetics to that of bacteria. In Caco-2 cells, the addition of ATP to the apical domain led to a steep [ATPe] increase to a maximum, with subsequent ATPase activity. The addition of bacterial suspensions led to a 6-7 fold increase in [ATPe], followed by an acute decrease. In perfused jejunum segments, exposure to E. coli increased luminal ATP 2 fold. ATPe regulation of E. coli depends on the balance between ATPase activity and ATP release. This balance can be altered by OMVs, which display their own capacity to regulate ATPe. E. coli can activate ATP release from Caco-2 cells and intestinal segments, a response which in vivo might lead to intestinal release of ATP from the gut lumen.
dc.descriptionInstituto de Estudios Inmunológicos y Fisiopatológicos
dc.descriptionInstituto de Investigaciones Bioquímicas de La Plata
dc.descriptionFacultad de Ciencias Médicas
dc.descriptionConsejo Nacional de Investigaciones Científicas y Técnicas
dc.formatapplication/pdf
dc.format1395-1416
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
dc.subjectCiencias Médicas
dc.subjectCaco-2 cells
dc.subjectEscherichia coli
dc.subjectExtracellular atp regulation
dc.subjectMastoparan 7
dc.subjectMelittin
dc.subjectOuter membrane vesicles
dc.titleDynamic regulation of extracellular ATP in <i>Escherichia coli</i>
dc.typeArticulo
dc.typeArticulo


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