Evidence map›Paper›PMID 32421930›Full record

ArticleAnatomical record (Hoboken, N.J. : 2007)2020

Expression of Laminin γ2 Proteolytic Fragments in Murine Skin Following Exposure to Sulfur Mustard.

Yoke-Chen Chang, James D Wang, Hui-Ying Chang, Peihong Zhou, Rita A Hahn, Marion K Gordon, Jeffrey D Laskin, Donald R Gerecke

Open access · greenAbstract read
In one paragraph

Article in Anatomical record (Hoboken, N.J. : 2007), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Skin Models Used to Define Mechanisms of Action of Sulfur Mustard.Disaster medicine and public health preparedness · 2023
    Review
  2. Review
  3. 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

8 authors at 1 institution in 1 country.

Yoke-Chen ChangDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.ORCID 0000-0001-9384-6387
James D WangDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.
Hui-Ying ChangDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.
Peihong ZhouDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.
Rita A HahnDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.
Marion K GordonDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.
Jeffrey D LaskinEnvironmental and Occupational Health, Rutgers University School of Public Health, Piscataway, New Jersey, USA.
Donald R GereckeDepartment of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, New Jersey, USA.
Rutgers, The State University of New Jersey · US

Funding

UMDNJ/Rutgers University CounterACT Research Center of ExcellenceU54AR055073 · NIAMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI LASKIN, JEFFREY D · 2006 to 2024
$71.4M
Translational Research Support CoreP30ES005022 · NIEHS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PANOS G. GEORGOPOULOS · 1988 to 2026
$47.4M
TRAINING IN EVIRONMENTAL TOXICOLOGYT32ES007148 · NIEHS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI Lauren M Aleksunes · 1987 to 2026
$11.4M
NIAMS NIH HHS U54 AR055073NIEHS NIH HHS P30 ES005022NIEHS NIH HHS T32 ES007148
6 · The paper itself

Abstract

Laminin-332 is a basement membrane protein composed of three genetically distinct polypeptide chains that actively promote both skin epidermal cell adhesion and migration. Proteolytic fragments of the laminin γ2 chain stimulate migration and scattering of keratinocytes and cancer cells. Sulfur mustard (SM) is a bifunctional alkylating agent that induces separation of basal keratinocytes from the dermal-epidermal junction and invokes a strong inflammatory response leading to delayed wound repair. In the present studies, the role of laminin γ2 in SM-induced skin injury and wound repair was investigated using the mouse ear vesicant model. We found that laminin γ2 chain mRNA was preferentially upregulated in mouse ear skin exposed to SM. In situ hybridization confirmed overexpression of laminin γ2 transcript. Western blot analysis showed increased protein expression of the full-length proform of laminin γ2 and smaller processed fragments of laminin γ2 in skin exposed to SM. Dual immunofluorescence labeling indicated that laminin γ2 fragments are prevalent in suprabasal keratinocytes behind the leading edge in areas of hyperplasia in injured skin. In addition, co-expression of laminin γ2 and the senescent marker, p16

Indexed as

AnimalsCell MovementDermatologic AgentsKeratinocytesLamininMiceMustard GasSkinUp-RegulationWound HealingDermatologic AgentsLamc2 protein, mouseLamininMustard Gasbasement membranecellular migrationlaminin-332skin wound healingvesicant sulfur mustard

Identifiers

PMID32421930
PMCPMC7394410
OpenAlexW3024412022

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.