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Comparative protein interactomics of neuroglobin and myoglobin
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| Zeitschriftentitel: | Journal of Neurochemistry |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | Journal of Neurochemistry, 123, 2012, 1, S. 192-198 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Haines, Bryan A. Davis, Darcy A. Zykovich, Artem Peng, Botao Rao, Rammohan Mooney, Sean D. Jin, Kunlin Greenberg, David A. Haines, Bryan A. Davis, Darcy A. Zykovich, Artem Peng, Botao Rao, Rammohan Mooney, Sean D. Jin, Kunlin Greenberg, David A. |
|---|---|
| author |
Haines, Bryan A. Davis, Darcy A. Zykovich, Artem Peng, Botao Rao, Rammohan Mooney, Sean D. Jin, Kunlin Greenberg, David A. |
| spellingShingle |
Haines, Bryan A. Davis, Darcy A. Zykovich, Artem Peng, Botao Rao, Rammohan Mooney, Sean D. Jin, Kunlin Greenberg, David A. Journal of Neurochemistry Comparative protein interactomics of neuroglobin and myoglobin Cellular and Molecular Neuroscience Biochemistry |
| author_sort |
haines, bryan a. |
| spelling |
Haines, Bryan A. Davis, Darcy A. Zykovich, Artem Peng, Botao Rao, Rammohan Mooney, Sean D. Jin, Kunlin Greenberg, David A. 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1111/j.1471-4159.2012.07881.x <jats:title>Abstract</jats:title><jats:p>Neuroglobin is a hypoxia‐inducible O<jats:sub>2</jats:sub>‐binding protein with neuroprotective effects in cell and animal models of stroke and Alzheimer’s disease. The mechanism underlying neuroglobin’s cytoprotective action is unknown, although several possibilities have been proposed, including anti‐oxidative and anti‐apoptotic effects. We used affinity purification–mass spectrometry methods to identify neuroglobin‐interacting proteins in normoxic and hypoxic murine neuronal (HN33) cell lysates, and to compare these interactions with those of a structurally and functionally related protein, myoglobin. We report that the protein interactomes of neuroglobin and myoglobin overlap substantially and are modified by hypoxia. In addition, neuroglobin‐interacting proteins include partners consistent with both anti‐oxidative and anti‐apoptotic functions, as well as with a relationship to several neurodegenerative diseases.</jats:p> Comparative protein interactomics of neuroglobin and myoglobin Journal of Neurochemistry |
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| title |
Comparative protein interactomics of neuroglobin and myoglobin |
| title_unstemmed |
Comparative protein interactomics of neuroglobin and myoglobin |
| title_full |
Comparative protein interactomics of neuroglobin and myoglobin |
| title_fullStr |
Comparative protein interactomics of neuroglobin and myoglobin |
| title_full_unstemmed |
Comparative protein interactomics of neuroglobin and myoglobin |
| title_short |
Comparative protein interactomics of neuroglobin and myoglobin |
| title_sort |
comparative protein interactomics of neuroglobin and myoglobin |
| topic |
Cellular and Molecular Neuroscience Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1471-4159.2012.07881.x |
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2012 |
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192-198 |
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<jats:title>Abstract</jats:title><jats:p>Neuroglobin is a hypoxia‐inducible O<jats:sub>2</jats:sub>‐binding protein with neuroprotective effects in cell and animal models of stroke and Alzheimer’s disease. The mechanism underlying neuroglobin’s cytoprotective action is unknown, although several possibilities have been proposed, including anti‐oxidative and anti‐apoptotic effects. We used affinity purification–mass spectrometry methods to identify neuroglobin‐interacting proteins in normoxic and hypoxic murine neuronal (HN33) cell lysates, and to compare these interactions with those of a structurally and functionally related protein, myoglobin. We report that the protein interactomes of neuroglobin and myoglobin overlap substantially and are modified by hypoxia. In addition, neuroglobin‐interacting proteins include partners consistent with both anti‐oxidative and anti‐apoptotic functions, as well as with a relationship to several neurodegenerative diseases.</jats:p> |
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| author | Haines, Bryan A., Davis, Darcy A., Zykovich, Artem, Peng, Botao, Rao, Rammohan, Mooney, Sean D., Jin, Kunlin, Greenberg, David A. |
| author_facet | Haines, Bryan A., Davis, Darcy A., Zykovich, Artem, Peng, Botao, Rao, Rammohan, Mooney, Sean D., Jin, Kunlin, Greenberg, David A., Haines, Bryan A., Davis, Darcy A., Zykovich, Artem, Peng, Botao, Rao, Rammohan, Mooney, Sean D., Jin, Kunlin, Greenberg, David A. |
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| description | <jats:title>Abstract</jats:title><jats:p>Neuroglobin is a hypoxia‐inducible O<jats:sub>2</jats:sub>‐binding protein with neuroprotective effects in cell and animal models of stroke and Alzheimer’s disease. The mechanism underlying neuroglobin’s cytoprotective action is unknown, although several possibilities have been proposed, including anti‐oxidative and anti‐apoptotic effects. We used affinity purification–mass spectrometry methods to identify neuroglobin‐interacting proteins in normoxic and hypoxic murine neuronal (HN33) cell lysates, and to compare these interactions with those of a structurally and functionally related protein, myoglobin. We report that the protein interactomes of neuroglobin and myoglobin overlap substantially and are modified by hypoxia. In addition, neuroglobin‐interacting proteins include partners consistent with both anti‐oxidative and anti‐apoptotic functions, as well as with a relationship to several neurodegenerative diseases.</jats:p> |
| doi_str_mv | 10.1111/j.1471-4159.2012.07881.x |
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| spelling | Haines, Bryan A. Davis, Darcy A. Zykovich, Artem Peng, Botao Rao, Rammohan Mooney, Sean D. Jin, Kunlin Greenberg, David A. 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1111/j.1471-4159.2012.07881.x <jats:title>Abstract</jats:title><jats:p>Neuroglobin is a hypoxia‐inducible O<jats:sub>2</jats:sub>‐binding protein with neuroprotective effects in cell and animal models of stroke and Alzheimer’s disease. The mechanism underlying neuroglobin’s cytoprotective action is unknown, although several possibilities have been proposed, including anti‐oxidative and anti‐apoptotic effects. We used affinity purification–mass spectrometry methods to identify neuroglobin‐interacting proteins in normoxic and hypoxic murine neuronal (HN33) cell lysates, and to compare these interactions with those of a structurally and functionally related protein, myoglobin. We report that the protein interactomes of neuroglobin and myoglobin overlap substantially and are modified by hypoxia. In addition, neuroglobin‐interacting proteins include partners consistent with both anti‐oxidative and anti‐apoptotic functions, as well as with a relationship to several neurodegenerative diseases.</jats:p> Comparative protein interactomics of neuroglobin and myoglobin Journal of Neurochemistry |
| spellingShingle | Haines, Bryan A., Davis, Darcy A., Zykovich, Artem, Peng, Botao, Rao, Rammohan, Mooney, Sean D., Jin, Kunlin, Greenberg, David A., Journal of Neurochemistry, Comparative protein interactomics of neuroglobin and myoglobin, Cellular and Molecular Neuroscience, Biochemistry |
| title | Comparative protein interactomics of neuroglobin and myoglobin |
| title_full | Comparative protein interactomics of neuroglobin and myoglobin |
| title_fullStr | Comparative protein interactomics of neuroglobin and myoglobin |
| title_full_unstemmed | Comparative protein interactomics of neuroglobin and myoglobin |
| title_short | Comparative protein interactomics of neuroglobin and myoglobin |
| title_sort | comparative protein interactomics of neuroglobin and myoglobin |
| title_unstemmed | Comparative protein interactomics of neuroglobin and myoglobin |
| topic | Cellular and Molecular Neuroscience, Biochemistry |
| url | http://dx.doi.org/10.1111/j.1471-4159.2012.07881.x |