Abstract
High altitude hypoxia is a paraphysiological condition triggering redox status disturbances of cell organization leading, via oxidative stress, to proteins, lipids, and DNA damage. In man, skeletal muscle, after prolonged exposure to hypoxia, undergoes mass reduction and alterations at the cellular level featuring a reduction of mitochondrial volume density, accumulation of lipofuscin, a product of lipid peroxidation, and dysregulation of enzymes whose time course is unknown. The effects of 7-9 days exposure to 4559 m (Margherita Hut, Monte Rosa, Italy) on the muscle proteins pattern were investigated, pre- and post-exposure, in ten young subjects, by 2-D DIGE and MS. Ten milligram biopsies were obtained from the mid part of the vastus lateralis muscle at sea level (control) and at altitude, after 7-9 days hypoxia. Differential analysis indicates that proteins involved in iron transport, tricarboxylic acid (TCA) cycle, oxidative phosphorylation, and oxidative stress responses were significantly (p
| Original language | English |
|---|---|
| Pages (from-to) | 4668-4679 |
| Number of pages | 12 |
| Journal | Proteomics |
| Volume | 8 |
| Issue number | 22 |
| DOIs | |
| Publication status | Published - Nov 2008 |
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Keywords
- 2-D DIGE
- Hypoxia
- Mass spectrometry
- Muscle
ASJC Scopus subject areas
- Molecular Biology
- Biochemistry
Cite this
Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia. / Viganò, Agnese; Ripamonti, Marilena; De Palma, Sara; Capitanio, Daniele; Vasso, Michele; Wait, Robin; Lundby, Carsten; Cerretelli, Paolo; Gelfi, Cecilia.
In: Proteomics, Vol. 8, No. 22, 11.2008, p. 4668-4679.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia
AU - Viganò, Agnese
AU - Ripamonti, Marilena
AU - De Palma, Sara
AU - Capitanio, Daniele
AU - Vasso, Michele
AU - Wait, Robin
AU - Lundby, Carsten
AU - Cerretelli, Paolo
AU - Gelfi, Cecilia
PY - 2008/11
Y1 - 2008/11
N2 - High altitude hypoxia is a paraphysiological condition triggering redox status disturbances of cell organization leading, via oxidative stress, to proteins, lipids, and DNA damage. In man, skeletal muscle, after prolonged exposure to hypoxia, undergoes mass reduction and alterations at the cellular level featuring a reduction of mitochondrial volume density, accumulation of lipofuscin, a product of lipid peroxidation, and dysregulation of enzymes whose time course is unknown. The effects of 7-9 days exposure to 4559 m (Margherita Hut, Monte Rosa, Italy) on the muscle proteins pattern were investigated, pre- and post-exposure, in ten young subjects, by 2-D DIGE and MS. Ten milligram biopsies were obtained from the mid part of the vastus lateralis muscle at sea level (control) and at altitude, after 7-9 days hypoxia. Differential analysis indicates that proteins involved in iron transport, tricarboxylic acid (TCA) cycle, oxidative phosphorylation, and oxidative stress responses were significantly (p
AB - High altitude hypoxia is a paraphysiological condition triggering redox status disturbances of cell organization leading, via oxidative stress, to proteins, lipids, and DNA damage. In man, skeletal muscle, after prolonged exposure to hypoxia, undergoes mass reduction and alterations at the cellular level featuring a reduction of mitochondrial volume density, accumulation of lipofuscin, a product of lipid peroxidation, and dysregulation of enzymes whose time course is unknown. The effects of 7-9 days exposure to 4559 m (Margherita Hut, Monte Rosa, Italy) on the muscle proteins pattern were investigated, pre- and post-exposure, in ten young subjects, by 2-D DIGE and MS. Ten milligram biopsies were obtained from the mid part of the vastus lateralis muscle at sea level (control) and at altitude, after 7-9 days hypoxia. Differential analysis indicates that proteins involved in iron transport, tricarboxylic acid (TCA) cycle, oxidative phosphorylation, and oxidative stress responses were significantly (p
KW - 2-D DIGE
KW - Hypoxia
KW - Mass spectrometry
KW - Muscle
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UR - http://www.scopus.com/inward/citedby.url?scp=55849092859&partnerID=8YFLogxK
U2 - 10.1002/pmic.200800232
DO - 10.1002/pmic.200800232
M3 - Article
C2 - 18937252
AN - SCOPUS:55849092859
VL - 8
SP - 4668
EP - 4679
JO - Proteomics
JF - Proteomics
SN - 1615-9853
IS - 22
ER -