dc.contributor.author | Oien, Derek B. | |
dc.contributor.author | Ortiz, Andrea Naomi | |
dc.contributor.author | Rittel, Alexander G. | |
dc.contributor.author | Dobrowsky, Rick T. | |
dc.contributor.author | Johnson, Michael A. | |
dc.contributor.author | Levant, Beth | |
dc.contributor.author | Fowler, Stephen C. | |
dc.contributor.author | Moskovitz, Jackob | |
dc.date.accessioned | 2017-05-16T16:24:55Z | |
dc.date.available | 2017-05-16T16:24:55Z | |
dc.date.issued | 2010-07 | |
dc.identifier.citation | Oien, D. B., Ortiz, A. N., Rittel, A. G., Dobrowsky, R. T., Johnson, M. A., Levant, B., … Moskovitz, J. (2010). Dopamine D2 receptor function is compromised in the brain of the methionine sulfoxide reductase A knockout mouse. Journal of Neurochemistry, 114(1), 51–61. http://doi.org/10.1111/j.1471-4159.2010.06721.x | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24222 | |
dc.description.abstract | Previous research suggests that brain oxidative stress and altered rodent locomotor behavior are linked. We observed bio-behavioral changes in methionine sulfoxide reductase A knockout mice associated with abnormal dopamine signaling. Compromised ability of these knockout mice to reduce methionine sulfoxide enhances accumulation of sulfoxides in proteins. We examined the dopamine D2-receptor function and expression, which has an atypical arrangement and quantity of methionine residues. Indeed, protein expression levels of dopamine D2-receptor were higher in knockout mice compared with wild-type. However, the binding of dopamine D2-receptor agonist was compromised in the same fractions of knockout mice. Coupling efficiency of dopamine D2-receptors to G-proteins was also significantly reduced in knockout mice, supporting the compromised agonist binding. Furthermore, pre-synaptic dopamine release in knockout striatal sections was less responsive than control sections to dopamine D2-receptor ligands. Behaviorally, the locomotor activity of knockout mice was less responsive to the inhibitory effect of quinpirole than wild-type mice. Involvement of specific methionine residue oxidation in the dopamine D2-receptor third intracellular loop is suggested by in vitro studies. We conclude that ablation of methionine sulfoxide reductase can affect dopamine signaling through altering dopamine D2-receptor physiology and may be related to symptoms associated with neurological disorders and diseases. | en_US |
dc.publisher | Wiley | en_US |
dc.rights | This is the peer reviewed version of the following article: Oien, D. B., Ortiz, A. N., Rittel, A. G., Dobrowsky, R. T., Johnson, M. A., Levant, B., Fowler, S. C. and Moskovitz, J. (2010), Dopamine D2 receptor function is compromised in the brain of the methionine sulfoxide reductase A knockout mouse. Journal of Neurochemistry, 114: 51–61. , which has been published in final form at http://doi.org/10.1111/j.1471-4159.2010.06721.x. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. | en_US |
dc.subject | Dopamine | en_US |
dc.subject | Dopamine receptor | en_US |
dc.subject | Locomotor activity | en_US |
dc.subject | Methionine oxidation | en_US |
dc.subject | Oxidative stress | en_US |
dc.subject | Post-translation modification | en_US |
dc.title | Dopamine D2 receptor function is compromised in the brain of the methionine sulfoxide reductase A knockout mouse | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Oien, Derek B. | |
kusw.kuauthor | Ortiz, Andrea N. | |
kusw.kuauthor | Rittel, Alexander G. | |
kusw.kuauthor | Dobrowsky, Rick T. | |
kusw.kuauthor | Johnson, Michael A. | |
kusw.kuauthor | Fowler, Stephen C. | |
kusw.kuauthor | Moskovitz, Jackob | |
kusw.kudepartment | Pharmacy | en_US |
kusw.kudepartment | Chemistry | en_US |
dc.identifier.doi | 10.1111/j.1471-4159.2010.06721.x | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC2933736 | en_US |
dc.rights.accessrights | openAccess | |