A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress
<p>Abstract</p> <p>Background</p> <p>The nematode <it>Caenorhabditis elegans </it>is both sensitive and tolerant to hypoxic stress, particularly when the evolutionarily conserved hypoxia response pathway HIF-1/EGL-9/VHL is involved. Hypoxia-induced changes i...
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BMC
2010-09-01
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Series: | Proteome Science |
Online Access: | http://www.proteomesci.com/content/8/1/49 |
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author | Wu Yonghong Gao Yan Zhang Feilong Hang Xingyi Shi Jinping Ren Changhong Li Hualing Xu Langlai Chen Changsheng Zhang Chenggang |
author_facet | Wu Yonghong Gao Yan Zhang Feilong Hang Xingyi Shi Jinping Ren Changhong Li Hualing Xu Langlai Chen Changsheng Zhang Chenggang |
author_sort | Wu Yonghong |
collection | DOAJ |
description | <p>Abstract</p> <p>Background</p> <p>The nematode <it>Caenorhabditis elegans </it>is both sensitive and tolerant to hypoxic stress, particularly when the evolutionarily conserved hypoxia response pathway HIF-1/EGL-9/VHL is involved. Hypoxia-induced changes in the expression of a number of genes have been analyzed using whole genome microarrays in <it>C. elegans</it>, but the changes at the protein level in response to hypoxic stress still remain unclear.</p> <p>Results</p> <p>Here, we utilized a quantitative proteomic approach to evaluate changes in the expression patterns of proteins during the early response to hypoxia in <it>C. elegans</it>. Two-dimensional difference gel electrophoresis (2D-DIGE) was used to compare the proteomic maps of wild type <it>C. elegans </it>strain N2 under a 4-h hypoxia treatment (0.2% oxygen) and under normoxia (control). A subsequent analysis by MALDI-TOF-TOF-MS revealed nineteen protein spots that were differentially expressed. Nine of the protein spots were significantly upregulated, and ten were downregulated upon hypoxic stress. Three of the upregulated proteins were involved in cytoskeletal function (LEV-11, MLC-1, ACT-4), while another three upregulated (ATP-2, ATP-5, VHA-8) were ATP synthases functionally related to energy metabolism. Four ribosomal proteins (RPL-7, RPL-8, RPL-21, RPS-8) were downregulated, indicating a decrease in the level of protein translation upon hypoxic stress. The overexpression of tropomyosin (LEV-11) was further validated by Western blot. In addition, the mutant strain of <it>lev-11(x12</it>) also showed a hypoxia-sensitive phenotype in subsequent analyses, confirming the proteomic findings.</p> <p>Conclusions</p> <p>Taken together, our data suggest that altered protein expression, structural protein remodeling, and the reduction of translation might play important roles in the early response to oxygen deprivation in <it>C. elegans</it>, and this information will help broaden our knowledge on the mechanism of hypoxia response.</p> |
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spelling | doaj.art-3a239de5356b465093e29ad03ebe9e522022-12-22T03:24:56ZengBMCProteome Science1477-59562010-09-01814910.1186/1477-5956-8-49A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stressWu YonghongGao YanZhang FeilongHang XingyiShi JinpingRen ChanghongLi HualingXu LanglaiChen ChangshengZhang Chenggang<p>Abstract</p> <p>Background</p> <p>The nematode <it>Caenorhabditis elegans </it>is both sensitive and tolerant to hypoxic stress, particularly when the evolutionarily conserved hypoxia response pathway HIF-1/EGL-9/VHL is involved. Hypoxia-induced changes in the expression of a number of genes have been analyzed using whole genome microarrays in <it>C. elegans</it>, but the changes at the protein level in response to hypoxic stress still remain unclear.</p> <p>Results</p> <p>Here, we utilized a quantitative proteomic approach to evaluate changes in the expression patterns of proteins during the early response to hypoxia in <it>C. elegans</it>. Two-dimensional difference gel electrophoresis (2D-DIGE) was used to compare the proteomic maps of wild type <it>C. elegans </it>strain N2 under a 4-h hypoxia treatment (0.2% oxygen) and under normoxia (control). A subsequent analysis by MALDI-TOF-TOF-MS revealed nineteen protein spots that were differentially expressed. Nine of the protein spots were significantly upregulated, and ten were downregulated upon hypoxic stress. Three of the upregulated proteins were involved in cytoskeletal function (LEV-11, MLC-1, ACT-4), while another three upregulated (ATP-2, ATP-5, VHA-8) were ATP synthases functionally related to energy metabolism. Four ribosomal proteins (RPL-7, RPL-8, RPL-21, RPS-8) were downregulated, indicating a decrease in the level of protein translation upon hypoxic stress. The overexpression of tropomyosin (LEV-11) was further validated by Western blot. In addition, the mutant strain of <it>lev-11(x12</it>) also showed a hypoxia-sensitive phenotype in subsequent analyses, confirming the proteomic findings.</p> <p>Conclusions</p> <p>Taken together, our data suggest that altered protein expression, structural protein remodeling, and the reduction of translation might play important roles in the early response to oxygen deprivation in <it>C. elegans</it>, and this information will help broaden our knowledge on the mechanism of hypoxia response.</p>http://www.proteomesci.com/content/8/1/49 |
spellingShingle | Wu Yonghong Gao Yan Zhang Feilong Hang Xingyi Shi Jinping Ren Changhong Li Hualing Xu Langlai Chen Changsheng Zhang Chenggang A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress Proteome Science |
title | A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress |
title_full | A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress |
title_fullStr | A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress |
title_full_unstemmed | A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress |
title_short | A proteomic view of <it>Caenorhabditis elegans </it>caused by short-term hypoxic stress |
title_sort | proteomic view of it caenorhabditis elegans it caused by short term hypoxic stress |
url | http://www.proteomesci.com/content/8/1/49 |
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