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Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines
Siderocalin (also lipocalin 2, NGAL or 24p3) binds iron as complexes with specific siderophores, which are low molecular weight, ferric ion-specific chelators. In innate immunity, siderocalin slows the growth of infecting bacteria by sequestering bacterial ferric siderophores. Siderocalin also binds...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3424236/ https://www.ncbi.nlm.nih.gov/pubmed/22928018 http://dx.doi.org/10.1371/journal.pone.0043696 |
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author | Correnti, Colin Richardson, Vera Sia, Allyson K. Bandaranayake, Ashok D. Ruiz, Mario Rahmanto, Yohan Suryo Kovačević, Žaklina Clifton, Matthew C. Holmes, Margaret A. Kaiser, Brett K. Barasch, Jonathan Raymond, Kenneth N. Richardson, Des R. Strong, Roland K. |
author_facet | Correnti, Colin Richardson, Vera Sia, Allyson K. Bandaranayake, Ashok D. Ruiz, Mario Rahmanto, Yohan Suryo Kovačević, Žaklina Clifton, Matthew C. Holmes, Margaret A. Kaiser, Brett K. Barasch, Jonathan Raymond, Kenneth N. Richardson, Des R. Strong, Roland K. |
author_sort | Correnti, Colin |
collection | PubMed |
description | Siderocalin (also lipocalin 2, NGAL or 24p3) binds iron as complexes with specific siderophores, which are low molecular weight, ferric ion-specific chelators. In innate immunity, siderocalin slows the growth of infecting bacteria by sequestering bacterial ferric siderophores. Siderocalin also binds simple catechols, which can serve as siderophores in the damaged urinary tract. Siderocalin has also been proposed to alter cellular iron trafficking, for instance, driving apoptosis through iron efflux via BOCT. An endogenous siderophore composed of gentisic acid (2,5-dihydroxybenzoic acid) substituents was proposed to mediate cellular efflux. However, binding studies reported herein contradict the proposal that gentisic acid forms high-affinity ternary complexes with siderocalin and iron, or that gentisic acid can serve as an endogenous siderophore at neutral pH. We also demonstrate that siderocalin does not induce cellular iron efflux or stimulate apoptosis, questioning the role siderocalin plays in modulating iron metabolism. |
format | Online Article Text |
id | pubmed-3424236 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34242362012-08-27 Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines Correnti, Colin Richardson, Vera Sia, Allyson K. Bandaranayake, Ashok D. Ruiz, Mario Rahmanto, Yohan Suryo Kovačević, Žaklina Clifton, Matthew C. Holmes, Margaret A. Kaiser, Brett K. Barasch, Jonathan Raymond, Kenneth N. Richardson, Des R. Strong, Roland K. PLoS One Research Article Siderocalin (also lipocalin 2, NGAL or 24p3) binds iron as complexes with specific siderophores, which are low molecular weight, ferric ion-specific chelators. In innate immunity, siderocalin slows the growth of infecting bacteria by sequestering bacterial ferric siderophores. Siderocalin also binds simple catechols, which can serve as siderophores in the damaged urinary tract. Siderocalin has also been proposed to alter cellular iron trafficking, for instance, driving apoptosis through iron efflux via BOCT. An endogenous siderophore composed of gentisic acid (2,5-dihydroxybenzoic acid) substituents was proposed to mediate cellular efflux. However, binding studies reported herein contradict the proposal that gentisic acid forms high-affinity ternary complexes with siderocalin and iron, or that gentisic acid can serve as an endogenous siderophore at neutral pH. We also demonstrate that siderocalin does not induce cellular iron efflux or stimulate apoptosis, questioning the role siderocalin plays in modulating iron metabolism. Public Library of Science 2012-08-21 /pmc/articles/PMC3424236/ /pubmed/22928018 http://dx.doi.org/10.1371/journal.pone.0043696 Text en © 2012 Correnti et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Correnti, Colin Richardson, Vera Sia, Allyson K. Bandaranayake, Ashok D. Ruiz, Mario Rahmanto, Yohan Suryo Kovačević, Žaklina Clifton, Matthew C. Holmes, Margaret A. Kaiser, Brett K. Barasch, Jonathan Raymond, Kenneth N. Richardson, Des R. Strong, Roland K. Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines |
title | Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines |
title_full | Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines |
title_fullStr | Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines |
title_full_unstemmed | Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines |
title_short | Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines |
title_sort | siderocalin/lcn2/ngal/24p3 does not drive apoptosis through gentisic acid mediated iron withdrawal in hematopoietic cell lines |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3424236/ https://www.ncbi.nlm.nih.gov/pubmed/22928018 http://dx.doi.org/10.1371/journal.pone.0043696 |
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