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pmid:28977037

Fast hyperbaric decompression after heliox saturation altered the brain proteome in rats.

Alvhild Alette Bjørkum · Eystein Oveland · Linda Stuhr · Marianne Bjordal Havnes · Frode Berven · Marit Grønning · Arvid Hope

PloS one · 2017 doi:10.1371/journal.pone.0185765

Paper

complete

Experiment

complete

Data

partial

Analysis

partial

Execution

absent

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Record details sci_version · id · kind · revision · content_hash · schema · created_at · updated_at · generator
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pmid:28977037
kind
science-record
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sha256:953096f2175d9f172e703f91fe071ba8d713a0762a27599b23415199e2619b8e
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https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json
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2026-11-01T15:40:28Z
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2026-11-01T21:21:05Z
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title
Fast hyperbaric decompression after heliox saturation altered the brain proteome in rats.
doi
10.1371/journal.pone.0185765
pmid
28977037
authors array · 7 items
[0]
Alvhild Alette Bjørkum
[1]
Eystein Oveland
[2]
Linda Stuhr
[3]
Marianne Bjordal Havnes
[4]
Frode Berven
[5]
Marit Grønning
[6]
Arvid Hope
journal
PloS one
year
2017
abstract
Better understanding of the physiological mechanisms and neurological symptoms involved in the development of decompression sickness could contribute to improvements of diving procedures. The main objective of the present study was to determine effects on the brain proteome of fast decompression (1 bar/20 s) compared to controls (1 bar/10 min) after heliox saturation diving, using rats in a model system. The protein S100B, considered a biomarker for brain injury, was not significantly different in serum samples from one week before, immediately after, and one week after the dive. Alterations in the rat brain proteome due to fast decompression were investigated using both iontrap and orbitrap LC-MS, and 967 and 1062 proteins were quantified, respectively. Based on the significantly regulated proteins in the iontrap (56) and orbitrap (128) datasets, the networks "synaptic vesicle fusion and recycling in nerve terminals" and "translation initiation" were significantly enriched in a system biological database analysis (Metacore). Ribosomal proteins (RLA2, RS10) and the proteins hippocalcin-like protein 4 and proteasome subunit beta type-7 were significantly upregulated in both datasets. The heat shock protein 105 kDa, Rho-associated protein kinase 2 and Dynamin-1 were significantly downregulated in both datasets. Another main effect of hyperbaric fast decompression in our experiment is inhibition of endocytosis and stimulation of exocytosis of vesicles in the presynaptic nerve terminal. In addition, fast decompression affected several proteins taking parts in these two main mechanisms of synaptic strength, especially alteration in CDK5/calcineurin are associated with a broad range of neurological disorders. In summary, fast decompression after heliox saturation affected the brain proteome in a rat model for diving, potentially disturbing protein homeostasis, e.g. in synaptic vesicles, and destabilizing cytoskeletal components. Data are available via ProteomeXchange with identifier PXD006349.
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The significantly regulated proteins due to fast decompression, according to two-sided t-tests, are denoted with an asterisk (*, p<0.05).
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sections[12] "The rat brain proteome after hyperbaric exposure with fast compared to slow decompression" paragraph 3
quote
The significantly regulated proteins due to fast decompression, according to two-sided t-tests, are denoted with an asterisk (*, p<0.05).
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sections[19] "Data Availability" paragraph 2
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Data are available via ProteomeXchange With identifier PXD006349.
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Headline result: Fast decompression after heliox saturation significantly altered the rat brain proteome, while serum S100B did not differ significantly. The statistical analysis used two-sided t-tests, and the raw LC-MS data and search/quantification results are available through ProteomeXchange under identifier PXD006349.
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sections[0] "Abstract" paragraph 1
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The protein S100B, considered a biomarker for brain injury, was not significantly different in serum samples from one week before, immediately after, and one week after the dive.
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sections[0] "Abstract" paragraph 1
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Alterations in the rat brain proteome due to fast decompression were investigated using both iontrap and orbitrap LC-MS, and 967 and 1062 proteins were quantified, respectively.
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sections[0] "Abstract" paragraph 1
quote
Based on the significantly regulated proteins in the iontrap (56) and orbitrap (128) datasets, the networks “synaptic vesicle fusion and recycling in nerve terminals” and “translation initiation” were significantly enriched in a system biological database analysis (Metacore).
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sections[0] "Abstract" paragraph 1
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Data are available via ProteomeXchange with identifier PXD006349
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Headline result: Fast decompression after heliox saturation significantly altered the rat brain proteome, while serum S100B did not differ significantly. The statistical analysis used two-sided t-tests, and the raw LC-MS data and search/quantification results are available through ProteomeXchange under identifier PXD006349.
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Fast hyperbaric decompression after heliox saturation altered the brain proteome in rats
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Proteins regulated in the brain of diving rats in both orbitrap and Iontrap analyses.
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Potential protein biomarker candidates for hyperbaric exposure
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Proteins regulated in the brain of diving rats in both orbitrap and Iontrap analyses.
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[5]
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10
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82
[8]
2.30
[9]
0.015
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[0]
40S ribosomal protein S10
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RS10_P63326
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2
[3]
23
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1.10
[5]
0.008
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4
[7]
35
[8]
1.58
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0.009
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0.000
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1
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§
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§§
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1.43
[9]
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Heat shock protein 105 kDa
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17
[3]
232
[4]
0.95
[5]
0.012
[6]
19
[7]
187
[8]
0.69
[9]
0.010
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Rho-associated protein kinase 2
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ROCK2_Q62868
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3
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4
[4]
0.93
[5]
0.024
[6]
29
[7]
149
[8]
0.68
[9]
0.032
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[0]
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DYN1_P21575
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34
[3]
839
[4]
0.95
[5]
0.033
[6]
60
[7]
911
[8]
0.76
[9]
0.020
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Proteins only detected in either orbitrap or Iontrap and significantly regulated.
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Potential protein biomarker candidates for hyperbaric exposure
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Proteins only detected in either orbitrap or Iontrap and significantly regulated.
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heliox saturation altered the brain proteome in rats.
[1]
iox saturation altered the brain proteome in rats.
[2]
er, and one week after the dive. Alterations in the rat brain proteome due to fast decompression wer
[3]
0 min) after heliox saturation diving, using rats in a model system. The protein S100B, consid
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her protein analysis. Sample preparation for mass spectrometry analyses The protein level profile in brain
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up (n = 10) were compared using quantitative proteomics analyses. From each animal one of the cerebr
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Complete file
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The main objective of the present study was to determine effects on the brain proteome of fast decompression (1 bar/20 s) compared to controls (1 bar/10 min) after heliox saturation diving, using rats in a model system. The protein S100B, considered a biomarker for brain injury, was not significantly different in serum samples from one week before, immediately after, and one week after the dive. Alterations in the rat brain proteome due to fast decompression were investigated using both iontrap and orbitrap LC-MS, and 967 and 1062 proteins were quantified, respectively. Based on the significantly regulated proteins in the iontrap (56) and orbitrap (128) datasets, the networks \"synaptic vesicle fusion and recycling in nerve terminals\" and \"translation initiation\" were significantly enriched in a system biological database analysis (Metacore). Ribosomal proteins (RLA2, RS10) and the proteins hippocalcin-like protein 4 and proteasome subunit beta type-7 were significantly upregulated in both datasets. The heat shock protein 105 kDa, Rho-associated protein kinase 2 and Dynamin-1 were significantly downregulated in both datasets. Another main effect of hyperbaric fast decompression in our experiment is inhibition of endocytosis and stimulation of exocytosis of vesicles in the presynaptic nerve terminal. In addition, fast decompression affected several proteins taking parts in these two main mechanisms of synaptic strength, especially alteration in CDK5/calcineurin are associated with a broad range of neurological disorders. In summary, fast decompression after heliox saturation affected the brain proteome in a rat model for diving, potentially disturbing protein homeostasis, e.g. in synaptic vesicles, and destabilizing cytoskeletal components. 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