Evidence map›Paper›PMID 25525887›Full record

ArticleMetallomics : integrated biometal science2015

ApoHRP-based assay to measure intracellular regulatory heme.

Hani Atamna, Marmik Brahmbhatt, Wafa Atamna, Gregory A Shanower, Joseph M Dhahbi

Open access · bronzeAbstract read
In one paragraph

Article in Metallomics : integrated biometal science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
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

31 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Localized heme sensing through a ternary molecular glue.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Heme metabolism mediates RANKL-induced osteoclastogenesis via mitochondrial oxidative phosphorylation.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025
    Article
  7. Article
  8. Update on heme biosynthesis, tissue-specific regulation, heme transport, relation to iron metabolism and cellular energy.Liver international : official journal of the International Association for the Study of the Liver · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022
    Review
  14. Review
  15. Unravelling the mechanisms controlling heme supply and demand.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Mammalian cell and tissue imaging using Raman and coherent Raman microscopy.Wiley interdisciplinary reviews. Systems biology and medicine · 2020
    Review
  20. A new model forThe Journal of biological chemistry · 2020
    Article
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

5 authors at 3 institutions in 1 country.

Hani AtamnaDepartment of Basic Sciences, TCMC, Scranton, PA, USA.
Marmik Brahmbhatt
Wafa Atamna
Gregory A Shanower
Joseph M Dhahbi
Commonwealth Medical College · USUniversity of Scranton · USUniversity of California, Riverside · US

Funding

Understanding the mechanism of cell senescence delay by methylene blueR15AG041414 · NIA · GEISINGER COMMONWEALTH SCHOOL OF MEDICINE · PI ATAMNA, HANI · 2011 to 2011
$314k
NIA NIH HHS R15 AG041414NIA NIH HHS R15AG041414
6 · The paper itself

Abstract

The majority of the heme-binding proteins possess a "heme-pocket" that stably binds to heme. Usually known as housekeeping heme-proteins, they participate in a variety of metabolic reactions (e.g., catalase). Heme also binds with lower affinity to the "Heme-Regulatory Motifs" (HRM) in specific regulatory proteins. This type of heme binding is known as exchangeable or regulatory heme (RH). Heme binding to HRM proteins regulates their function (e.g., Bach1). Although there are well-established methods for assaying total cellular heme (e.g., heme-proteins plus RH), currently there is no method available for measuring RH independent of the total heme (TH). The current study describes and validates a new method to measure intracellular RH. This method is based on the reconstitution of apo-horseradish peroxidase (apoHRP) with heme to form holoHRP. The resulting holoHRP activity is then measured with a colorimetric substrate. The results show that apoHRP specifically binds RH but not with heme from housekeeping heme-proteins. The RH assay detects intracellular RH. Furthermore, using conditions that create positive (hemin) or negative (N-methyl protoporphyrin IX) controls for heme in normal human fibroblasts (IMR90), the RH assay shows that RH is dynamic and independent of TH. We also demonstrated that short-term exposure to subcytotoxic concentrations of lead (Pb), mercury (Hg), or amyloid-β (Aβ) significantly alters intracellular RH with little effect on TH. In conclusion the RH assay is an effective assay to investigate intracellular RH concentration and demonstrates that RH represents ∼6% of total heme in IMR90 cells.

Indexed as

Amyloid beta-PeptidesApoenzymesCell LineEnzyme AssaysHemeHorseradish PeroxidaseHumansIntracellular SpaceLeadMercuryReference StandardsSubstrate SpecificityTime FactorsAmyloid beta-PeptidesApoenzymesHemeHorseradish PeroxidaseLeadMercury

Identifiers

PMID25525887
PMCPMC4326600
OpenAlexW1996434091

What OpenQuestion holds

Textmetadata
LicenceTDM
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Registered trials

None linked

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.