Evidence map›Paper›PMID 32890564›Full record

ArticleInternational journal of biological macromolecules2020

Degradation of bacterial permeability family member A1 (BPIFA1) by house dust mite (HDM) cysteine protease Der p 1 abrogates immune modulator function.

Rui Zhang, Jessika Trower, Tongde Wu

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 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
0.2field-weighted citation impact, top 44% 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, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. A SPLUNC1 Peptidomimetic Inhibits Orai1 and Reduces Inflammation in a Murine Allergic Asthma Model.American journal of respiratory cell and molecular biology · 2022
    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

3 authors at 2 institutions in 2 countries.

Rui ZhangDepartment of Respiratory and Critical Care Medicine, General Hospital of Ningxia Medical University, Ningxia Medical University, Yinchuan, PR China.
Jessika TrowerDepartment of Pharmaceutical Sciences, 302 East Lawson Street, North Carolina Central University, Durham, NC 27707, USA.
Tongde WuDepartment of Pharmaceutical Sciences, 302 East Lawson Street, North Carolina Central University, Durham, NC 27707, USA; Biomanufacturing Research Institute & Technology Enterprise (BRITE), 302 East Lawson Street, North Carolina Central University, Durham, NC 27707, USA. Electronic address: twu@nccu.edu.
North Carolina Central University · USNingxia Medical University · CN

Funding

Support for QA/QC for Prior Approval ProcessUL1TR002553 · NCATS · DUKE UNIVERSITY · PI LI, JENNIFER S, MCNAMARA, JAMES O. · 2018 to 2023
$58.5M
Understanding Perceptions of HIV Risk, PrEP, and PrEP use among African American Women Attending an HBCUU54MD012392 · NIMHD · NORTH CAROLINA CENTRAL UNIVERSITY · PI Cherise Baldwin Harrington · 2017 to 2026
$38.1M
Translational Research Support CoreP30ES025128 · NIEHS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI Sue Fenton · 2015 to 2026
$18.3M
NCATS NIH HHS UL1 TR002553NIEHS NIH HHS P30 ES025128NIMHD NIH HHS U54 MD012392
6 · The paper itself

Abstract

Bacterial permeability family member A1 (BPIFA1) is one of the most abundant proteins present in normal airway surface liquid (ASL). It is known to be diminished in asthmatic patients' sputum, which causes airway hyperresponsiveness (AHR). What is currently unclear is how environmental factors, such as allergens' impact on BPIFA1's abundance and functions in the context of allergic asthma. House dust mite (HDM) is a predominant domestic source of aeroallergens. The group of proteases found in HDM is thought to cleave multiple cellular protective mechanisms, and therefore foster the development of allergic asthma. Here, we show that BPIFA1 is cleaved by HDM proteases in a time-, dose-, and temperature-dependent manner. We have also shown the main component in HDM that is responsible for BPIFA1's degradation is Der p1. Fragmented BPIFA1 failed to bind E. coli lipopolysaccharide (LPS), and hence elevated TNFα and IL-6 secretion in human whole blood. BPIFA1 degradation is also observed in vivo in bronchoalveolar fluid (BALF) of mice which are intranasally instilled with HDM. These data suggest that proteases associated with environmental allergens such as HDM cleave BPIFA1 and therefore impair its immune modulator function.

Indexed as

ImmunomodulationAllergensAnimalsAntigens, DermatophagoidesArthropod ProteinsCalciumCalcium SignalingCell LineCysteine EndopeptidasesCysteine Proteinase InhibitorsCytokinesGlycoproteinsHumansInflammation MediatorsMicePhosphoproteinsAllergensAntigens, DermatophagoidesArthropod ProteinsBPIFA1 protein, humanCalciumCysteine EndopeptidasesCysteine Proteinase InhibitorsCytokinesDermatophagoides pteronyssinus antigen p 1GlycoproteinsInflammation MediatorsPhosphoproteinsBPIFA1DegradationHDM

Identifiers

PMID32890564
PMCPMC7467078
OpenAlexW3081747070

What OpenQuestion holds

Textmetadata
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.