ArticleBiochemistry2006
Effects of biological oxidants on the catalytic activity and structure of group VIA phospholipase A2.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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.
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.
Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- The mechanism of allosteric regulation of calcium-independent phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular basis of unique specificity and regulation of group VIA calcium-independent phospholipase APharmacology & therapeutics · 2023Review
- Review
- Inhibition of TOR inCells · 2019Article
- Evidence of Highly Conserved β-Crystallin Disulfidome that Can be Mimicked by In Vitro Oxidation in Age-related Human Cataract and Glutathione Depleted Mouse Lens.Molecular & cellular proteomics : MCP · 2015Article
- Calcium-independent phospholipases A2 and their roles in biological processes and diseases.Journal of lipid research · 2015Review
- Group VIA phospholipase A2 mitigates palmitate-induced β-cell mitochondrial injury and apoptosis.The Journal of biological chemistry · 2014Article
- Article
- Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.Chemical reviews · 2011Review
- Effects of endoplasmic reticulum stress on group VIA phospholipase A2 in beta cells include tyrosine phosphorylation and increased association with calnexin.The Journal of biological chemistry · 2010Article
- Group VIA Ca2+-independent phospholipase A2 (iPLA2beta) and its role in beta-cell programmed cell death.Biochimie · 2010Review
- Phospholipases A2 and inflammatory responses in the central nervous system.Neuromolecular medicine · 2010Review
- Myeloperoxidase-dependent inactivation of surfactant protein D in vitro and in vivo.The Journal of biological chemistry · 2010Article
- Profiling the NIH Small Molecule Repository for compounds that generate H2O2 by redox cycling in reducing environments.Assay and drug development technologies · 2010Article
- H2O2-induced Ca2+ influx and its inhibition by N-(p-amylcinnamoyl) anthranilic acid in the beta-cells: involvement of TRPM2 channels.Journal of cellular and molecular medicine · 2009Article
- Calcium-independent phospholipases in the heart: mediators of cellular signaling, bioenergetics, and ischemia-induced electrophysiologic dysfunction.Journal of cardiovascular pharmacology · 2009Review
- Role of Ca2+-independent phospholipase A2 in cell growth and signaling.Biochemical pharmacology · 2008Review
- Discovering mechanisms of signaling-mediated cysteine oxidation.Current opinion in chemical biology · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Group VIA phospholipase A(2) (iPLA(2)beta) is expressed in phagocytes, vascular cells, pancreatic islet beta-cells, neurons, and other cells and plays roles in transcriptional regulation, cell proliferation, apoptosis, secretion, and other events. A bromoenol lactone (BEL) suicide substrate used to study iPLA(2)beta functions inactivates iPLA(2)beta by alkylating Cys thiols. Because thiol redox reactions are important in signaling and some cells that express iPLA(2)beta produce biological oxidants, iPLA(2)beta might be subject to redox regulation. We report that biological concentrations of H(2)O(2), NO, and HOCl inactivate iPLA(2)beta, and this can be partially reversed by dithiothreitol (DTT). Oxidant-treated iPLA(2)beta modifications were studied by LC-MS/MS analyses of tryptic digests and included DTT-reversible events, e.g., formation of disulfide bonds and sulfenic acids, and others not so reversed, e.g., formation of sulfonic acids, Trp oxides, and Met sulfoxides. W(460) oxidation could cause irreversible inactivation because it is near the lipase consensus sequence ((463)GTSTG(467)), and site-directed mutagenesis of W(460) yields active mutant enzymes that exhibit no DTT-irreversible oxidative inactivation. Cys651-sulfenic acid formation could be one DTT-reversible inactivation event because Cys651 modification correlates closely with activity loss and its mutagenesis reduces sensitivity to inhibition. Intermolecular disulfide bond formation might also cause reversible inactivation because oxidant-treated iPLA(2)beta contains DTT-reducible oligomers, and oligomerization occurs with time- and temperature-dependent iPLA(2)beta inactivation that is attenuated by DTT or ATP. Subjecting insulinoma cells to oxidative stress induces iPLA(2)beta oligomerization, loss of activity, and subcellular redistribution and reduces the rate of release of arachidonate from phospholipids. These findings raise the possibility that redox reactions affect iPLA(2)beta functions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.