Re-partitioning of Cu and Zn isotopes by modified protein expression
<p>Abstract</p> <p>Cu and Zn have naturally occurring non radioactive isotopes, and their isotopic systematics in a biological context are poorly understood. In this study we used double focussing mass spectroscopy to determine the ratios for these isotopes for the first time in mo...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2008-10-01
|
| Series: | Geochemical Transactions |
| Online Access: | http://www.geochemicaltransactions.com/content/9/1/11 |
| _version_ | 1818526418979520512 |
|---|---|
| author | Ragnarsdottir K Vala Hawkesworth Chris J Büchl Anette Brown David R |
| author_facet | Ragnarsdottir K Vala Hawkesworth Chris J Büchl Anette Brown David R |
| author_sort | Ragnarsdottir K Vala |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Cu and Zn have naturally occurring non radioactive isotopes, and their isotopic systematics in a biological context are poorly understood. In this study we used double focussing mass spectroscopy to determine the ratios for these isotopes for the first time in mouse brain. The Cu and Zn isotope ratios for four strains of wild-type mice showed no significant difference (δ<sup>65</sup>Cu -0.12 to -0.78 permil; δ<sup>66</sup>Zn -0.23 to -0.48 permil). We also looked at how altering the expression of a single copper binding protein, the prion protein (PrP), alters the isotope ratios. Both knockout and overexpression of PrP had no significant effect on the ratio of Cu isotopes. Mice brains expressing mutant PrP lacking the known metal binding domain have δ<sup>65</sup>Cu isotope values of on average 0.57 permil higher than wild-type mouse brains. This implies that loss of the copper binding domain of PrP increases the level of <sup>65</sup>Cu in the brain. δ<sup>66</sup>Zn isotope values of the transgenic mouse brains are enriched for <sup>66</sup>Zn to the wild-type mouse brains. Here we show for the first time that the expression of a single protein can alter the partitioning of metal isotopes in mouse brains. The results imply that the expression of the prion protein can alter cellular Cu isotope content.</p> |
| first_indexed | 2024-12-11T06:22:42Z |
| format | Article |
| id | doaj.art-08fce30631bb4945ae2f845d2501b93d |
| institution | Directory Open Access Journal |
| issn | 1467-4866 |
| language | English |
| last_indexed | 2024-12-11T06:22:42Z |
| publishDate | 2008-10-01 |
| publisher | BMC |
| record_format | Article |
| series | Geochemical Transactions |
| spelling | doaj.art-08fce30631bb4945ae2f845d2501b93d2022-12-22T01:17:45ZengBMCGeochemical Transactions1467-48662008-10-01911110.1186/1467-4866-9-11Re-partitioning of Cu and Zn isotopes by modified protein expressionRagnarsdottir K ValaHawkesworth Chris JBüchl AnetteBrown David R<p>Abstract</p> <p>Cu and Zn have naturally occurring non radioactive isotopes, and their isotopic systematics in a biological context are poorly understood. In this study we used double focussing mass spectroscopy to determine the ratios for these isotopes for the first time in mouse brain. The Cu and Zn isotope ratios for four strains of wild-type mice showed no significant difference (δ<sup>65</sup>Cu -0.12 to -0.78 permil; δ<sup>66</sup>Zn -0.23 to -0.48 permil). We also looked at how altering the expression of a single copper binding protein, the prion protein (PrP), alters the isotope ratios. Both knockout and overexpression of PrP had no significant effect on the ratio of Cu isotopes. Mice brains expressing mutant PrP lacking the known metal binding domain have δ<sup>65</sup>Cu isotope values of on average 0.57 permil higher than wild-type mouse brains. This implies that loss of the copper binding domain of PrP increases the level of <sup>65</sup>Cu in the brain. δ<sup>66</sup>Zn isotope values of the transgenic mouse brains are enriched for <sup>66</sup>Zn to the wild-type mouse brains. Here we show for the first time that the expression of a single protein can alter the partitioning of metal isotopes in mouse brains. The results imply that the expression of the prion protein can alter cellular Cu isotope content.</p>http://www.geochemicaltransactions.com/content/9/1/11 |
| spellingShingle | Ragnarsdottir K Vala Hawkesworth Chris J Büchl Anette Brown David R Re-partitioning of Cu and Zn isotopes by modified protein expression Geochemical Transactions |
| title | Re-partitioning of Cu and Zn isotopes by modified protein expression |
| title_full | Re-partitioning of Cu and Zn isotopes by modified protein expression |
| title_fullStr | Re-partitioning of Cu and Zn isotopes by modified protein expression |
| title_full_unstemmed | Re-partitioning of Cu and Zn isotopes by modified protein expression |
| title_short | Re-partitioning of Cu and Zn isotopes by modified protein expression |
| title_sort | re partitioning of cu and zn isotopes by modified protein expression |
| url | http://www.geochemicaltransactions.com/content/9/1/11 |
| work_keys_str_mv | AT ragnarsdottirkvala repartitioningofcuandznisotopesbymodifiedproteinexpression AT hawkesworthchrisj repartitioningofcuandznisotopesbymodifiedproteinexpression AT buchlanette repartitioningofcuandznisotopesbymodifiedproteinexpression AT browndavidr repartitioningofcuandznisotopesbymodifiedproteinexpression |