dc.creator | Pertusa, José A. G. | es |
dc.creator | León Quinto, Trinidad | es |
dc.creator | Berná, Genoveva | es |
dc.creator | Tejedo Huamán, Juan Rigoberto | es |
dc.creator | Hmadcha, Abdelkrim | es |
dc.creator | Bedoya Bergua, Francisco Javier | es |
dc.creator | Martín, Franz | es |
dc.creator | Soria Escoms, Bernat | es |
dc.date.accessioned | 2018-12-20T09:41:02Z | |
dc.date.available | 2018-12-20T09:41:02Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Pertusa, J.A.G., León Quinto, T., Berná, G., Tejedo Huamán, J.R., Hmadcha, A., Bedoya Bergua, F.J.,...,Soria Escoms, B. (2017). Zn2+ chelation by serum albumin improves hexameric Zn2+ -insulin dissociation into monomers after exocytosis. PLoS ONE, 12, 1-16. | |
dc.identifier.issn | 1932-6203 | es |
dc.identifier.uri | https://hdl.handle.net/11441/81135 | |
dc.description.abstract | β-cells release hexameric Zn2+-insulin into the extracellular space, but monomeric Zn2+-free
insulin appears to be the only biologically active form. The mechanisms implicated in dissociation
of the hexamer remain unclear, but they seem to be Zn2+ concentration-dependent.
In this study, we investigate the influence of albumin binding to Zn2+ on Zn2+-insulin dissociation
into Zn2+-free insulin and its physiological, methodological and therapeutic relevance.
Glucose and K+-induced insulin release were analyzed in isolated mouse islets by static
incubation and perifusion experiments in the presence and absence of albumin and Zn2+
chelators. Insulin tolerance tests were performed in rats using different insulin solutions with
and without Zn2+ and/or albumin. Albumin-free buffer does not alter quantification by RIA of
Zn2+-free insulin but strongly affects RIA measurements of Zn2+-insulin. In contrast, accurate
determination of Zn2+-insulin was obtained only when bovine serum albumin or Zn2+
chelators were present in the assay buffer solution. Albumin and Zn2+ chelators do not modify
insulin release but do affect insulin determination. Preincubation with albumin or Zn2+
chelators promotes the conversion of ªslowº Zn2+-insulin into ªfastº insulin. Consequently,
insulin diffusion from large islets is ameliorated in the presence of Zn2+ chelators. These
observations support the notion that the Zn2+-binding properties of albumin improve the dissociation
of Zn2+-insulin into subunits after exocytosis, which may be useful in insulin determination,
insulin pharmacokinetic assays and islet transplantation. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Public Library of Science | es |
dc.relation.ispartof | PLoS ONE, 12, 1-16. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Zn2+ chelation by serum albumin improves hexameric Zn2+ -insulin dissociation into monomers after exocytosis | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.relation.publisherversion | https://doi.org/10.1371/journal.pone.0187547 | es |
dc.identifier.doi | 10.1371/journal.pone.0187547 | es |
idus.format.extent | 16 p. | es |
dc.journaltitle | PLoS ONE | es |
dc.publication.volumen | 12 | es |
dc.publication.initialPage | 1 | es |
dc.publication.endPage | 16 | es |