Zn2+ chelation by serum albumin improves hexameric Zn2+-insulin dissociation into monomers after exocytosis

PloS One
José A G PertusaBernat Soria

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 "slow" Zn2+-insulin into "...Continue Reading

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Citations

May 18, 2018·PloS One·Peter ProksFrances M Ashcroft
Feb 14, 2019·Inflammopharmacology·Tianjiao ZhaoWei Wei
Oct 3, 2018·Metallomics : Integrated Biometal Science·Michael J StevensonMarie C Heffern
Nov 3, 2021·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Swati AryaAlan J Stewart

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