Evidence map›Paper›PMID 26694316›Full record

ArticleMetallomics : integrated biometal science2016

Newport Green, a fluorescent sensor of weakly bound cellular Zn(2+): competition with proteome for Zn(2).

Mohammad Rezaul Karim, David H Petering

Abstract read
In one paragraph

Article in Metallomics : integrated biometal science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Proteomic High Affinity ZnInternational journal of molecular sciences · 2017
    Review
  6. Techniques for measuring cellular zinc.Archives of biochemistry and biophysics · 2016
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Mohammad Rezaul KarimDepartment of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, Milwaukee, WI 53201, USA. petering@uwm.edu.
David H PeteringDepartment of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, Milwaukee, WI 53201, USA. petering@uwm.edu.

Funding

Fluorescent Cellular Zinc Sensors. What Are They Imaging?R01GM085114 · NIGMS · UNIVERSITY OF WISCONSIN MILWAUKEE · PI PETERING, DAVID HAROLD · 2008 to 2011
$1.1M
Effective Methods to Identify the Toxic Metal ProteomeR21ES024509 · NIEHS · UNIVERSITY OF WISCONSIN MILWAUKEE · PI PETERING, DAVID HAROLD · 2014 to 2015
$400k
NIEHS NIH HHS ES-024509NIEHS NIH HHS R21 ES024509NIGMS NIH HHS GM-85114NIGMS NIH HHS R01 GM085114
6 · The paper itself

Abstract

Newport Green (NPG) is a recognized sensor of cellular Zn(2+) that displays fluorescence enhancement upon binding to Zn(2+). Because of its modest affinity for Zn(2+), the extent of its capacity to bind cellular Zn(2+) is unclear. The present study investigated the range of reactivity of NPG(ESTER) with cells, isolated (Zn)-proteome, and model Zn-proteins. The sensor accumulated in pig kidney LLC-PK1 cells and was slowly (>40 min) hydrolyzed to the fluorescent, acid form, NPG(ACID). The powerful, cell permeant Zn(2+) chelator, N,N,N',N'-tetrakis(2-pyridylmethyl)-ethane-1,2-diamine (TPEN) failed to quench the growing fluorescence emission, indicating that Zn-NPG(ACID) had not formed and NPG-Zn-protein adduct species probably were not present. Furthermore, NPG(ACID) did not bind to Zn-carbonic anhydrase or Zn-alcohol dehydrogenase, two proteins that form adducts with some other sensors. Strikingly, most of the NPG(ACID) that had been converted from NPG(ESTER) was detected in the extracellular medium not the cells. As a result, after cells were incubated with NPG(ESTER) and then Zn-pyrithione to raise the internal concentration of mobile Zn(2+), Zn-NPG(ACID) was only observed in the external medium. Residual cellular NPG(ACID) was unable to bind extra intracellular Zn(2+) delivered by pyrithione. Proteome isolated from the sonicated cell supernatant was also unreactive with NPG(ACID). Titration of proteome or glutathione with Zn(2+) in the presence of NPG(ACID) revealed that NPG(ACID) only weakly competes for mobile Zn(2+) in the presence of these cellular components. In addition, when proteomic Zn(2+) was released by a nitric oxide donor or N-ethyl-maleimide, little Zn(2+) was detected by NPG(ACID). However, exposure to nitric oxide independently enhanced the fluorescence properties of NPG(ACID). Thus, the biochemical properties of NPG related to cellular Zn(2+) chelation deepen the question of how it functions as a Zn(2+) sensor.

Indexed as

AnimalsCell LineFluorescent DyesProteomeProteomicsSwineZincFluorescent DyesProteomeZinc

Identifiers

PMID26694316
PMCPMC4777312

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.