Evidence map›Paper›PMID 30696842›Full record

ArticleScientific reports2019

Caspase-4 disaggregates lipopolysaccharide micelles via LPS-CARD interaction.

Jinsu An, Seong Ho Kim, Dohyeon Hwang, Kyung Eun Lee, Min Jung Kim, Eun Gyeong Yang, So Yeon Kim, Hak Suk Chung

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

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  15. Review
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  17. Review
  18. Galectin-3 promotes noncanonical inflammasome activation through intracellular binding to lipopolysaccharide glycans.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Pulmonary Inflammation and KRAS Mutation in Lung Cancer.Advances in experimental medicine and biology · 2021
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  20. 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 3 institutions in 1 country.

Jinsu AnCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Seong Ho KimCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Dohyeon HwangCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.ORCID 0000-0003-2231-9947
Kyung Eun LeeAdvanced Analysis Center, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu, Seoul, 02792, Republic of Korea.
Min Jung KimDepartment of Biological Sciences, Sookmyung Women's University, Seoul, Korea.
Eun Gyeong YangCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
So Yeon KimCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Hak Suk ChungCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea. hschung@kist.re.kr.ORCID 0000-0003-1166-9909
Bio-Medical Science (South Korea) · KRKorea Institute of Science and Technology · KRSookmyung Women's University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipopolysaccharides (LPS) are a major component of the outer membrane of Gram-negative bacteria and are pathogen-associated molecular patterns recognized by the TLR4/MD2 complex that induces an inflammatory response. Recently, the cytosolic receptors caspase-4/-5/-11 that bind LPS inside the cell and trigger inflammasome activation or pyroptosis, have been identified. Despite the important roles of caspase-4 in human immune responses, few studies have investigated its biochemical characteristics and interactions with LPS. Since caspase-4 (C258A) purified from an Escherichia coli host forms aggregates, monomeric proteins including full-length caspase-4, caspase-4 (C258A), and the CARD domain of caspase-4 have been purified from the insect cell system. Here, we report the overexpression and purification of monomeric caspase-4 (C258A) and CARD domain from E. coli and demonstrate that purified caspase-4 (C258A) and CARD domain bind large LPS micelles and disaggregate them to small complexes. As the molar ratio of caspase-4 to LPS increases, the size of the caspase-4/LPS complex decreases. Our results present a new function of caspase-4 and set the stage for structural and biochemical studies, and drug discovery targeting LPS/caspase-4 interactions by establishing a facile purification method to obtain large quantities of purified caspase-4 (C258A) and the CARD domain.

Indexed as

Bacterial Outer MembraneCaspase Activation and Recruitment DomainCaspases, InitiatorCatalytic DomainCell LineEscherichia coliHEK293 CellsHumansLipopolysaccharidesMicellesProtein BindingCASP4 protein, humanCaspases, InitiatorLipopolysaccharidesMicelles

Identifiers

PMID30696842
PMCPMC6351570
OpenAlexW2914871102

What OpenQuestion holds

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LicenceCC BY
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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.