Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia

Saturation diving (SD) is one of the safest techniques for tolerating hyperbaric conditions for long durations. However, the changes in the human plasma protein profile that occur during SD are unknown. To identify differential protein expression during or after SD, 65 blood samples from 15 healthy...

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Published in:PloS one Vol. 11; no. 10; p. e0163804
Main Authors: Domoto, Hideharu, Iwaya, Keiichi, Ikomi, Fumitaka, Matsuo, Hirotaka, Tadano, Yutaka, Fujii, Shigenori, Tachi, Kazuyoshi, Itoh, Yoshiyuki, Sato, Michiya, Inoue, Kimitoshi, Shinomiya, Nariyoshi
Format: Journal Article
Language:English
Published: United States Public Library of Science 14-10-2016
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Summary:Saturation diving (SD) is one of the safest techniques for tolerating hyperbaric conditions for long durations. However, the changes in the human plasma protein profile that occur during SD are unknown. To identify differential protein expression during or after SD, 65 blood samples from 15 healthy Japanese men trained in SD were analyzed by two-dimensional fluorescence difference gel electrophoresis. The expression of two proteins, one 32.4 kDa with an isoelectric point (pI) of 5.8 and the other 44.8 kDa with pI 4.0, were elevated during SD to 60, 100, and 200 meters sea water (msw). The expression of these proteins returned to pre-diving level when the SD training was completed. The two proteins were identified using in-gel digestion and mass spectrometric analysis; the 32.4 kDa protein was transthyretin and the 44.8 kDa protein was alpha-1-acid glycoprotein 1. Oxidation was detected at methionine 13 of transthyretin and at methionine 129 of alpha-1-acid glycoprotein 1 by tandem mass spectrometry. Moreover, haptoglobin was up-regulated during the decompression phase of 200 msw. These plasma proteins up-regulated during SD have a common function as anti-oxidants. This suggests that by coordinating their biological effects, these proteins activate a defense mechanism to counteract the effects of hyperbaric-hyperoxic conditions during SD.
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Current address: Department of Pathology, Keiyu Hospital, Yokohama, Kanagawa, Japan
Current address: Maritime staff office, Ministry of Defense, Shinjuku, Tokyo, Japan
Conceptualization: K.Iwaya HD HM FI NS. Data curation: FI HD. Formal analysis: K. Iwaya YI MS SF. Funding acquisition: K. Iwaya. Investigation: K. Iwaya YI MS SF. Methodology: K. Iwaya HM FI. Project administration: NS. Resources: MS K. Iwaya KT SF YT. Software: K. Iwaya SF. Supervision: K. Inoue YT. Validation: K. Inoue NS SF. Visualization: K. Iwaya KT NS. Writing – original draft: HD K. Iwaya FI HM NS. Writing – review & editing: HD K. Iwaya MS NS.
Competing Interests: The authors have declared that no competing interests except for the salaries for the author [YI] who is employed by a commercial company: JEOL. This does not alter our adherence to PLOS ONE policies on sharing data and materials.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0163804