Evidence map›Paper›PMID 38848024›Full record

ArticleMetabolic brain disease2024

Protein vicinal thiols as intrinsic probes of brain redox states in health, aging, and ischemia.

Timothy D Foley, Wen C Huang, Emily A Petsche, Emily R Fleming, James C Hornickle

Abstract read
In one paragraph

Article in Metabolic brain disease, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

5 authors.

Timothy D FoleyBiochemistry Program, Department of Chemistry, University of Scranton, Scranton, PA, 18510, USA. foleyt2@scranton.edu.ORCID 0000-0002-2378-0703
Wen C HuangBiochemistry Program, Department of Chemistry, University of Scranton, Scranton, PA, 18510, USA.ORCID 0009-0000-3632-1998
Emily A PetscheBiochemistry Program, Department of Chemistry, University of Scranton, Scranton, PA, 18510, USA.ORCID 0009-0001-4091-817X
Emily R FlemingBiochemistry Program, Department of Chemistry, University of Scranton, Scranton, PA, 18510, USA.ORCID 0009-0001-9494-2722
James C HornickleBiochemistry Program, Department of Chemistry, University of Scranton, Scranton, PA, 18510, USA.ORCID 0009-0002-9080-2199

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nature of brain redox metabolism in health, aging, and disease remains to be fully established. Reversible oxidations, to disulfide bonds, of closely spaced (vicinal) protein thiols underlie the catalytic maintenance of redox homeostasis by redoxin enzymes, including thioredoxin peroxidases (peroxiredoxins), and have been implicated in redox buffering and regulation. We propose that non-peroxidase proteins containing vicinal thiols that are responsive to physiological redox perturbations may serve as intrinsic probes of brain redox metabolism. Using redox phenylarsine oxide (PAO)-affinity chromatography, we report that PAO-binding vicinal thiols on creatine kinase B and alpha-enolase from healthy rat brains were preferentially oxidized compared to other selected proteins, including neuron-specific (gamma) enolase, under conditions designed to trap in vivo protein thiol redox states. Moreover, measures of the extents of oxidations of vicinal thiols on total protein, and on creatine kinase B and alpha-enolase, showed that vicinal thiol-linked redox states were stable over the lifespan of rats and revealed a transient reductive shift in these redox couples following decapitation-induced global ischemia. Finally, formation of disulfide-linked complexes between peroxiredoxin-2 and brain proteins was demonstrated on redox blots, supporting a link between protein vicinal thiol redox states and the peroxidase activities of peroxiredoxins. The implications of these findings with respect to underappreciated aspects of brain redox metabolism in health, aging, and ischemia are discussed.

Indexed as

AgingBrainBrain IschemiaOxidation-ReductionSulfhydryl CompoundsAnimalsArsenicalsCreatine Kinase, BB FormMalePhosphopyruvate HydrataseRatsRats, Sprague-DawleyArsenicalsCreatine Kinase, BB FormoxophenylarsinePhosphopyruvate HydrataseSulfhydryl CompoundsAgingDisulfide bondsIschemiaPeroxiredoxinProtein thiolsRedox

Identifiers

PMID38848024
PMCPMC11233328

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.