The rdw rat has hereditary hypothyroidism caused by a missense mutation (G2320R) with thyroglobulin (Tg) gene account for the Tg misfolding. In this report we revealed proteomic changes in the rdw adrenal gland by using an agarose two-dimensional gel electrophoresis (2-DE) and a liquid chromatography-tandem mass spectrometry system (LC-MS/MS). We compared the proteome map of the rdw adrenal cortex and medulla with that of normal tissues, quantitative alteration of protein contents related to adrenal function were detected, and the abnormal proteins were identified. In the rdw adrenal cortex, at least 7 protein spot levels were decreased. One of those identified proteins was 11beta-hydroxysteroid dehydrogenase (11beta-HSD) known to be the enzyme converting 11-deoxycorticosterone to corticosterone. In the rdw adrenal medulla, at least 2 protein spot levels were significantly increased. These proteins were respectively identified as tyrosine 3-hydroxylase (TH), which catalyzes the rate-limiting step in catecholamine biosynthesis, and secretogranin II (SgII), known as a neuroendocrine secretory granule protein. All the above alterations of protein contents were recovered by administration of T4 to rdw rat from three days to 28 days of age, however, resulted in failure by normal thyroid transplantation at 28 days of age. These results suggest that neonatal thyroid status critically affects expression of those proteins related to adrenal function.
