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...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5065185?pdf=render |
| _version_ | 1811327538577801216 |
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| author | Hideharu Domoto Keiichi Iwaya Fumitaka Ikomi Hirotaka Matsuo Yutaka Tadano Shigenori Fujii Kazuyoshi Tachi Yoshiyuki Itoh Michiya Sato Kimitoshi Inoue Nariyoshi Shinomiya |
| author_facet | Hideharu Domoto Keiichi Iwaya Fumitaka Ikomi Hirotaka Matsuo Yutaka Tadano Shigenori Fujii Kazuyoshi Tachi Yoshiyuki Itoh Michiya Sato Kimitoshi Inoue Nariyoshi Shinomiya |
| author_sort | Hideharu Domoto |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T15:08:35Z |
| format | Article |
| id | doaj.art-20faaa43211b4baa8afd8a05d723723f |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-13T15:08:35Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-20faaa43211b4baa8afd8a05d723723f2022-12-22T02:42:04ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-011110e016380410.1371/journal.pone.0163804Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia.Hideharu DomotoKeiichi IwayaFumitaka IkomiHirotaka MatsuoYutaka TadanoShigenori FujiiKazuyoshi TachiYoshiyuki ItohMichiya SatoKimitoshi InoueNariyoshi ShinomiyaSaturation 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.http://europepmc.org/articles/PMC5065185?pdf=render |
| spellingShingle | Hideharu Domoto Keiichi Iwaya Fumitaka Ikomi Hirotaka Matsuo Yutaka Tadano Shigenori Fujii Kazuyoshi Tachi Yoshiyuki Itoh Michiya Sato Kimitoshi Inoue Nariyoshi Shinomiya Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia. PLoS ONE |
| title | Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia. |
| title_full | Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia. |
| title_fullStr | Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia. |
| title_full_unstemmed | Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia. |
| title_short | Up-Regulation of Antioxidant Proteins in the Plasma Proteome during Saturation Diving: Unique Coincidence under Hypobaric Hypoxia. |
| title_sort | up regulation of antioxidant proteins in the plasma proteome during saturation diving unique coincidence under hypobaric hypoxia |
| url | http://europepmc.org/articles/PMC5065185?pdf=render |
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