ABSTRACT
<p><b>AIM</b>To analyse the alterations of protein expression in the kidney of spontaneously hypertensive rat with losartan.</p><p><b>METHODS</b>The proteins of the kidney were isolated by two-dimensional gel electrophoresis. The protein spots with significant changes were selected for further identification by LC-MS/MS.</p><p><b>RESULTS</b>The number of average protein spots of two groups was 570 +/- 48 and 686 +/- 30 respectively. Compared with the SHR, 13 spots had changed significantly after treated with losartan. There were 5 protein spots detected only in SHR group, while 4 up-regulated and 4 down-regulated protein spots were detected in SHR-L group. These differentially expressed proteins were detected by mass spectrometry. 7 spots were identified. There were Heat shock protein (Hsp), Tubulin alpha-1 chain, Transthyretin precursor, Liver regeneration-related protein LRRG03, Ezrin-radixin-moesin binding phosphoprotein 50, Phosphoglycerate kinase 1 and Anionic trypsin I precursor.</p><p><b>CONCLUSION</b>The different protein spots expression may play important roles in Losartan's effective protection to hypertension rats renal tissue.</p>
Subject(s)
Animals , Male , Rats , Angiotensin II Type 1 Receptor Blockers , Pharmacology , Therapeutic Uses , Chromatography, Liquid , Electrophoresis, Gel, Two-Dimensional , Methods , Hypertension , Drug Therapy , Metabolism , Kidney , Metabolism , Losartan , Pharmacology , Therapeutic Uses , Proteome , Metabolism , Proteomics , Methods , Rats, Inbred SHR , Tandem Mass SpectrometryABSTRACT
Idiopathic pulmonary arterial hypertension (IPAH) is a rare disease of unknown etiology. The exact pathogenesis of pulmonary arterial hypertension is still not well known. In the past decades, many protein molecules have been found to be involved in the development of IPAH. With proteomic techniques, profiling of human plasma proteome becomes more feasible in searching for disease-related markers. In present study, we showed the protein expression profiles of the serum of IPAH and healthy controls after depleting a few high-abundant proteins in serum. Thirteen spots had changed significantly in IPAH compared with healthy controls and were identified by LC-MS/MS. Alpha-1-antitrypsin and vitronectin were down-regulated in IPAH and may be valuable candidates for further explorations of their roles in the development of IPAH.