Cited by 49Anesthesia and Neurotoxicity ResearchAnesthesia and Sedative AgentsAdvanced Proteomics Techniques and Applications

Halothane binding proteome in human brain cortex

Pan, Jonathan Z., Xi, Jin, Tobias, John W., Eckenhoff, Maryellen F., Eckenhoff, Roderic G.·2007·Journal of Proteome Research

Abstract

Inhaled anesthetics bind specifically to a wide variety of proteins in the brain. This set of proteins must include those that contribute to the physiological and behavioral phenotypes of anesthesia and the related side effects. To identify the anesthetic-binding targets and functional pathways associated with these targets in human brain, halothane photolabeling and two-dimensional (2D) gel electrophoresis were used. Both membrane and soluble proteins from human temporal cortex were prepared. More than 300 membrane and 400 soluble protein spots were detected on the stained blots, of which 23 membrane and 34 soluble proteins were labeled by halothane and identified by mass spectroscopy. Their functional classification reveals five groups, including carbohydrate metabolism, protein folding, oxidative phosphorylation, nucleoside triphosphatase, and dimer/kinase activity with different correlative stringency. When network analysis of the interaction between these protein molecules is used, the weighted interaction accentuates the cellular protein components important in cell growth and proliferation, cell cycle and cell death, and cell-cell signaling and interactions, although no pathway was specific. This study provides evidence for multiple anesthetic binding targets and suggests potential pathways involved in their actions.

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Crossref · 10.1021/pr060311u

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49 of 49 references verified0 citation errors · 0 not checkable

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  • Actual evidence (e.g. from genomics and proteomics) points to anesthetic action in microtubules.

    “Historically, views of anesthetic action have focused on neuronal membrane proteins, but actual evidence (e.g. from genomics and proteomics) [84,85] points to anesthetic action in microtubules.”

    From Consciousness in the universe (2014) · cites this paper as [85]

  • Anesthetics bind to tubulin and destabilize microtubules.

    “Anesthetics bind to tubulin, causing microtubules to destabilize [84, 85].”

    From The Biology of General Anesthesia from Paramecium to Primate (2019) · cites this paper as [84]

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Authors
Pan, J. Z., Xi, J., Tobias, J. W., Eckenhoff, M. F., & Eckenhoff, R. G.
Affiliations
  • University of Pennsylvania Health System (US)
  • Department of Anesthesiology and Critical Care and Department of Bioinformatics, University of Pennsylvania Health System, Philadelphia, Pennsylvania 19104
Corresponding author
Pan, Jonathan Z.
Venue
Journal of Proteome Research
Published
2006-12-19
Volume
6
Issue
2
Pages
582-592
ISSN
  • 1535-3893 (ISSN-L)
  • 1535-3907
OpenAlex
W1975765816
Cited by
49
References
49
Citations by year
2026: 4 · 2025: 5 · 2024: 1 · 2023: 2 · 2022: 6 · 2021: 2 · 2019: 4 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 4 · 2012: 2
FWCI
0.57
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Proteome Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (GM 51595, R01GM051595)
Topics
  • Life Sciences › Neuroscience › Developmental Neuroscience › Anesthesia and Neurotoxicity Research
  • Health Sciences › Medicine › Anesthesiology and Pain Medicine › Anesthesia and Sedative Agents
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords
halothane, cerebral cortex, temporal cortex, protein-protein interaction network, membrane proteins, soluble protein, carbohydrate metabolism, protein folding, oxidative phosphorylation, nucleoside triphosphatase, kinase activity, cell cycle, cell death, signal transduction, anesthetic side effects
MeSH terms
Cerebral Cortex, Enzymes, Halothane, Humans, Nerve Tissue Proteins, Protein Binding, Electrophoresis, Gel, Two-Dimensional, Proteome

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