Evidence map›Paper›PMID 32272499›Full record

ReviewJournal of leukocyte biology2020

The Charcot-Leyden crystal protein revisited-A lysopalmitoylphospholipase and more.

Peter F Weller, Haibin Wang, Rossana C N Melo

Open access · greenAbstract readReview
In one paragraph

Review in Journal of leukocyte biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Eosinophil extracellular traps in respiratory ailment: Pathogenic mechanisms and clinical translation.World journal of otorhinolaryngology - head and neck surgery · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. How to detect eosinophil ETosis (EETosis) and extracellular traps.Allergology international : official journal of the Japanese Society of Allergology · 2021
    Review
  12. 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.

Peter F WellerDepartment of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0001-9580-560X
Haibin WangDepartment of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA.
Rossana C N MeloDepartment of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0003-1736-0806
Beth Israel Deaconess Medical Center · USUniversidade Federal de Juiz de Fora · BR

Funding

CYTOPLASMIC LIPID BODIES OF INFLAMMATORY CELLSR01AI022571 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WELLER, PETER F · 1985 to 2013
$4.5M
Human Eosinophils: Mechanisms of FunctioningR37AI020241 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WELLER, PETER F · 2010 to 2019
$4.5M
Airways Eosinophils as Antigen-presenting Cells in AsthmaR01AI051645 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WELLER, PETER F · 2001 to 2011
$3.8M
HUMAN EOSINOPHILS: MECHANISMS OF FUNCTIONINGR01AI020241 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WELLER, PETER F · 1985 to 2009
$3.5M
NIAID NIH HHS R01 AI020241NIAID NIH HHS R01 AI022571NIAID NIH HHS R01 AI051645NIAID NIH HHS R37 AI020241NIH HHS R01AI022571NIH HHS R01AI051645NIH HHS R37AI02024
6 · The paper itself

Abstract

The Charcot-Leyden crystal protein (CLC-P), a constituent of human and not mouse eosinophils, is one of the most abundant proteins within human eosinophils. It has a propensity to form crystalline structures, Charcot-Leyden crystals, which are hallmarks in their distinctive extracellular crystalline forms as markers of eosinophilic inflammation. The functions of CLC-P within eosinophils have been uncertain. Although the action of CLC-P as a lysophospholipase has been questioned, assays of chromatographically purified CLC-P and crystal-derived CLC-P as well as studies of transfected recombinant CLC-P have consistently documented that CLC-P endogenously expresses lysophospholipase activity, releasing free palmitate from substrate lysopalmitoylphosphatidylcholine. Rather than acting solely as a hydrolytic enzyme to release palmitate from a lysolipid substrate, some other lysophospholipases function more dominantly as acyl-protein thioesterases (APTs), enzymes that catalyze the removal of thioester-linked, long chain fatty acids, such as palmitate, from cysteine residues of proteins. As such APTs participate in palmitoylation, a post-translational modification that can affect membrane localization, vesicular transport, and secretion. CLC-P has attributes of an APT. Thus, whereas CLC-P expresses inherent lysophospholipase activity, like some other lysophospholipase enzymes, it likely also functions in regulating the dynamic palmitoylation cycle, including, given its dominant subplasmalemmal location, at the human eosinophil's plasma membrane.

Indexed as

EosinophilsGlycoproteinsHumansLysophospholipasePalmitic AcidGlycoproteinslysolecithin acylhydrolaseLysophospholipasePalmitic Acidacyl-protein thioesteraseCharcot-Leyden crystalsdepalmitoylasegalectin-10lysophospholipase

Identifiers

PMID32272499
PMCPMC9269718
OpenAlexW3015784712

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.