Increased Protein Arginine Methylation in Chronic Hypoxia

• DOI: 10.1165/rcmb.2006-0097oc
• Publication Date: 2006-05-12T08:02:11Z
• Authors: Ali O. Yildirim; Patrick Bulau; Dariusz Zakrzewicz; Kamila E. Kitowska; Norbert Weissmann; Friedrich Grimminger; Rory E. Morty; Oliver Eickelberg
• Keywords: Asymmetric dimethylarginine; Hypoxia

Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide synthesis. ADMA generated by catabolism proteins containing methylated arginine residues, and its levels are correlated with endothelial dysfunction in systemic cardiovascular diseases. Arginine methylation cellular catalyzed protein methyltransferases (PRMT). The expression localization PRMT the lung has not been addressed. Here, we sought to analyze isoforms determine whether altered during exposure chronic hypoxia (10% oxygen). Adult mice were exposed for up 3 wk, tissues harvested processed RT-PCR, Western blotting, immunohistochemistry, determination tissue levels. All investigated detected at mRNA level mouse lung, localized primarily bronchial alveolar epithelium. In lungs subjected hypoxia, PRMT2 up-regulated, whereas all other remained unchanged. This was mainly due increased type II cells, which did express detectable under normoxic conditions. Consistent these observations, ADMA/l-Arginine ratios hypoxic These results demonstrate that PRMTs expressed functional a potent regulator concentrations. data suggest structural changes caused may be linked metabolism.