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Publication : Gender-specific regulation of tyrosine hydroxylase in thymocyte differentiation antigen-1 knockout mice.

First Author  Carkaci-Salli N Year  2012
Journal  J Neurosci Res Volume  90
Issue  8 Pages  1583-8
PubMed ID  22430860 Mgi Jnum  J:284787
Mgi Id  MGI:6390235 Doi  10.1002/jnr.23046
Citation  Carkaci-Salli N, et al. (2012) Gender-specific regulation of tyrosine hydroxylase in thymocyte differentiation antigen-1 knockout mice. J Neurosci Res 90(8):1583-8
abstractText  Thymocyte differentiation antigen-1 (Thy-1) is a cell surface glycoprotein found on T cells and neurons and is involved in cell-to-cell interactions. In addition, Thy-1 knockouts (KO) are a potential mouse model of restless legs syndrome (RLS) based on clinical observations and the role of dopamine in the disease. In this study, we analyzed the activity and quantity of tyrosine hydroxylase (TH; the rate-limiting enzyme in dopamine production) and determined phosphorylation levels for the enzyme phosphoserine-40 (pSer-40). There was no significant difference in the total TH activity and pSer-40 TH levels between Thy-1 KO and control groups; however, TH specific activity was significantly lower (by 26%) in Thy-1 KO mice. This difference is due in part to increased TH protein levels in this group (increased by 29%). When analyzed by gender, Thy-1 KO female mouse striata contained less TH specific activity compared with control females (decreased by 41%) and male control or Thy-1 KO animals (decreased by 30%). TH specific activity and pSer-40 TH levels in male Thy-1 KO and control displayed no differences. However, pSer-40 TH was significantly higher in control females (38%) compared with control or Thy-1 KO males. The Thy-1 KO females exhibited significantly lower (28%) pSer-40 TH (normalized to GAPDH or TH) than control females. Indeed, the Thy-1 KO females had 50% of the pSer-40 TH found in controls. Our results suggest a gender effect on TH specific activity, TH protein levels, and serine-40 phosphorylation of TH in Thy-1 KO female mice.
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