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A proteomic approach to investigate the changes within the rat hypothalamo‐neurohypophyseal system induced by dehydration

The neuropeptide hormone arginine vasopressin (VP) is produced in the magnocellular neurons of the hypothalamic supraoptic (SON) and paraventricular (PVN) nuclei and stored in the posterior pituitary (PP). Dehydration evokes an up‐regulation of the expression of the VP gene in magnocellular neurons and a massive release of the peptide from the PP in the circulation to promote water conservation at the level of the kidney. In parallel, a functional remodelling of the hypothalamo‐neurohypophyseal system (HNS) is observed but not totally understood. To investigate this activity dependent plasticity of the HNS in terms of coordinated action of cellular and protein networks, we have used proteomic (2D Fluorescence DIfference Gel Electrophoresis (DIGE)) combined with MALDI mass spectrometry approaches to identify proteins that change in abundance in the SON and the PP from rat as a consequence of 3 days of dehydration. Semi‐quantitative Western‐Blotting, Immunohistochemistry and/or Enzymo Immuno Assay were used to confirm and/or complement the data. Using these approaches, we have identified many proteins implicated in various cellular functions, among them, a truncated form of ProSAAS, a Granin‐Like Neuroendocrine Peptide Precursor known as a potent inhibitor of the Prohormone Convertase 1, has been found significantly down‐regulated in the PP and up‐regulated in the SON after dehydration.