Copper Sources for Sod1 Activation
Copper ions (i.e., copper) are a critical part of several cellular processes, but tight regulation of copper levels and trafficking are required to keep the cell protected from this highly reactive transition metal. Cu, Zn superoxide dismutase (Sod1) protects the cell from the accumulation of radica...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-06-01
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| Series: | Antioxidants |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2076-3921/9/6/500 |
| _version_ | 1797565887085019136 |
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| author | Stefanie D. Boyd Morgan S. Ullrich Amelie Skopp Duane D. Winkler |
| author_facet | Stefanie D. Boyd Morgan S. Ullrich Amelie Skopp Duane D. Winkler |
| author_sort | Stefanie D. Boyd |
| collection | DOAJ |
| description | Copper ions (i.e., copper) are a critical part of several cellular processes, but tight regulation of copper levels and trafficking are required to keep the cell protected from this highly reactive transition metal. Cu, Zn superoxide dismutase (Sod1) protects the cell from the accumulation of radical oxygen species by way of the redox cycling activity of copper in its catalytic center. Multiple posttranslational modification events, including copper incorporation, are reliant on the copper chaperone for Sod1 (Ccs). The high-affinity copper uptake protein (Ctr1) is the main entry point of copper into eukaryotic cells and can directly supply copper to Ccs along with other known intracellular chaperones and trafficking molecules. This review explores the routes of copper delivery that are utilized to activate Sod1 and the usefulness and necessity of each. |
| first_indexed | 2024-03-10T19:19:17Z |
| format | Article |
| id | doaj.art-ccf0a7c7df01441a8f122594510c4ade |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-10T19:19:17Z |
| publishDate | 2020-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-ccf0a7c7df01441a8f122594510c4ade2023-11-20T03:07:54ZengMDPI AGAntioxidants2076-39212020-06-019650010.3390/antiox9060500Copper Sources for Sod1 ActivationStefanie D. Boyd0Morgan S. Ullrich1Amelie Skopp2Duane D. Winkler3Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USADepartment of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USADepartment of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USADepartment of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USACopper ions (i.e., copper) are a critical part of several cellular processes, but tight regulation of copper levels and trafficking are required to keep the cell protected from this highly reactive transition metal. Cu, Zn superoxide dismutase (Sod1) protects the cell from the accumulation of radical oxygen species by way of the redox cycling activity of copper in its catalytic center. Multiple posttranslational modification events, including copper incorporation, are reliant on the copper chaperone for Sod1 (Ccs). The high-affinity copper uptake protein (Ctr1) is the main entry point of copper into eukaryotic cells and can directly supply copper to Ccs along with other known intracellular chaperones and trafficking molecules. This review explores the routes of copper delivery that are utilized to activate Sod1 and the usefulness and necessity of each.https://www.mdpi.com/2076-3921/9/6/500Sod1coppermetallo-chaperoneenzymemetallo-enzymemetallothionein |
| spellingShingle | Stefanie D. Boyd Morgan S. Ullrich Amelie Skopp Duane D. Winkler Copper Sources for Sod1 Activation Antioxidants Sod1 copper metallo-chaperone enzyme metallo-enzyme metallothionein |
| title | Copper Sources for Sod1 Activation |
| title_full | Copper Sources for Sod1 Activation |
| title_fullStr | Copper Sources for Sod1 Activation |
| title_full_unstemmed | Copper Sources for Sod1 Activation |
| title_short | Copper Sources for Sod1 Activation |
| title_sort | copper sources for sod1 activation |
| topic | Sod1 copper metallo-chaperone enzyme metallo-enzyme metallothionein |
| url | https://www.mdpi.com/2076-3921/9/6/500 |
| work_keys_str_mv | AT stefaniedboyd coppersourcesforsod1activation AT morgansullrich coppersourcesforsod1activation AT amelieskopp coppersourcesforsod1activation AT duanedwinkler coppersourcesforsod1activation |