Evidence map›Paper›PMID 31233899›Full record

ReviewCellular and molecular gastroenterology and hepatology2019

Porphyrin-Induced Protein Oxidation and Aggregation as a Mechanism of Porphyria-Associated Cell Injury.

Dhiman Maitra, Juliana Bragazzi Cunha, Jared S Elenbaas, Herbert L Bonkovsky, Jordan A Shavit, M Bishr Omary

Open access · goldAbstract readReview
In one paragraph

Review in Cellular and molecular gastroenterology and hepatology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

45 citing papers in PubMed, 71 citations in OpenAlex.

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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

6 authors at 4 institutions in 2 countries.

Dhiman MaitraDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan. Electronic address: dm1401@cabm.rutgers.edu.
Juliana Bragazzi CunhaDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan.
Jared S ElenbaasMedical Scientist Training Program, Washington University in St. Louis, St. Louis, Missouri.
Herbert L BonkovskyGastroenterology & Hepatology, and Molecular Medicine & Translational Science, Wake Forest University School of Medicine/NC Baptist Hospital, Winston-Salem, North Carolina.
Jordan A ShavitDepartment of Pediatrics, Division of Pediatric Hematology and Oncology, University of Michigan Medical School, Ann Arbor, Michigan.
M Bishr OmaryDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan; Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan; Cell Biology, Faculty of Science and Technology, Åbo Akademi University, Turku, Finland.
University of Michigan · USÅbo Akademi University · FIAtrium Health Wake Forest Baptist · USWashington University in St. Louis · US

Funding

University of Michigan Center for Gastrointestinal ResearchP30DK034933 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1986 to 2021
$22.5M
Porphyrias Consortium: SupplementU54DK083909 · NIDDK · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI BALWANI, MANISHA, DESNICK, ROBERT J · 2009 to 2023
$18.5M
Mechanism of Proteotoxicity and Experimental Therapeutic Approaches in PorphyriaR01DK116548 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Bishr Omary · 2017 to 2026
$3.8M
Dissecting the Genetics of Human Hemostatic Disorders Using ZebrafishR01HL124232 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHAVIT, JORDAN A · 2015 to 2019
$1.9M
Identification of novel therapeutics for hemostatic disorders using zebrafishR01HL125774 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHAVIT, JORDAN A · 2018 to 2020
$899k
NHLBI NIH HHS R01 HL124232NHLBI NIH HHS R01 HL125774NIDDK NIH HHS P30 DK034933NIDDK NIH HHS R01 DK116548NIDDK NIH HHS U54 DK083909
6 · The paper itself

Abstract

Genetic porphyrias comprise eight diseases caused by defects in the heme biosynthetic pathway that lead to accumulation of heme precursors. Consequences of porphyria include photosensitivity, liver damage and increased risk of hepatocellular carcinoma, and neurovisceral involvement, including seizures. Fluorescent porphyrins that include protoporphyrin-IX, uroporphyrin and coproporphyrin, are photo-reactive; they absorb light energy and are excited to high-energy singlet and triplet states. Decay of the porphyrin excited to ground state releases energy and generates singlet oxygen. Porphyrin-induced oxidative stress is thought to be the major mechanism of porphyrin-mediated tissue damage. Although this explains the acute photosensitivity in most porphyrias, light-induced porphyrin-mediated oxidative stress does not account for the effect of porphyrins on internal organs. Recent findings demonstrate the unique role of fluorescent porphyrins in causing subcellular compartment-selective protein aggregation. Porphyrin-mediated protein aggregation associates with nuclear deformation, cytoplasmic vacuole formation and endoplasmic reticulum dilation. Porphyrin-triggered proteotoxicity is compounded by inhibition of the proteasome due to aggregation of some of its subunits. The ensuing disruption in proteostasis also manifests in cell cycle arrest coupled with aggregation of cell proliferation-related proteins, including PCNA, cdk4 and cyclin B1. Porphyrins bind to native proteins and, in presence of light and oxygen, oxidize several amino acids, particularly methionine. Noncovalent interaction of oxidized proteins with porphyrins leads to formation of protein aggregates. In internal organs, particularly the liver, light-independent porphyrin-mediated protein aggregation occurs after secondary triggers of oxidative stress. Thus, porphyrin-induced protein aggregation provides a novel mechanism for external and internal tissue damage in porphyrias that involve fluorescent porphyrin accumulation.

Indexed as

AnimalsCarcinoma, HepatocellularDermatitis, PhototoxicHemeHumansLiverLiver NeoplasmsMiceOxidation-ReductionOxidative StressPhotosensitivity DisordersPorphyriasPorphyrinsProtein AggregatesProtoporphyrinsUroporphyrinsHemePorphyrinsProtein Aggregatesprotoporphyrin IXProtoporphyrinsUroporphyrinsOxidative StressPhototoxicityPorphyriaProtein Aggregation

Identifiers

PMID31233899
PMCPMC6820234
OpenAlexW2952472386

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.