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Assessment of protein-incorporated arginine methylation in biological specimens by CZE UV-detection

Zinellu, Angelo and Sotgia, Salvatore and Scanu, Bastianina and Formato, Marilena and Deiana, Luca and Carru, Ciriaco (2007) Assessment of protein-incorporated arginine methylation in biological specimens by CZE UV-detection. Electrophoresis, Vol. 28 (3), p. 4452-4458. eISSN 1522-2683. Article.

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DOI: 10.1002/elps.200700153

Abstract

Protein arginine methyltransferases methylate post-translationally arginine residues in proteins to synthesize monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), or symmetric dimethylarginine. Protein arginine methylation is involved in the regulation of signal transduction, RNA export, and cell proliferation. Moreover, upon proteolysis, arginines are released into the cytosol in which they exert important biological effects. Both MMA and ADMA are inhibitors of nitric oxide synthase and especially elevated levels of ADMA are associated with endothelial dysfunction and cardiovascular disease. Quantification of these analytes is commonly performed by HPLC after sample cleanup and derivatization. We propose a CE method in which these steps have been avoided and the procedure for sample preparation has been simplified. After acidic hydrolysis of proteins, samples were dried, resuspended in water, and directly injected in CE. A baseline separation of analytes was reached in a 60 cm×75 m id uncoated silica capillary, by using a Tris-phosphate run buffer at pH 2.15. This method allows an accurate assessment of protein arginine methylation degree in different biological samples such as whole blood, plasma, red blood cells, cultured cells, and tissue. Moreover, its good sensitivity permits to evaluate the methylation of a single protein type after the opportune purification steps. A method applicability concerns both clinical laboratories, where the evaluation of blood protein from numerous samples could be rapidly performed, and research laboratories where the factors affecting the arginine protein methylation degree could be easily studied.

Item Type:Article
ID Code:1516
Status:Published
Refereed:Yes
Uncontrolled Keywords:Asymmetric dimethylarginine, CE, monomethylarginine, methylation, symmetric dimethylarginine
Subjects:Area 05 - Scienze biologiche > BIO/10 Biochimica
Area 05 - Scienze biologiche > BIO/12 Biochimica clinica e biologia molecolare clinica
Divisions:001 Università di Sassari > 01 Dipartimenti > Scienze fisiologiche, biochimiche e cellulari
001 Università di Sassari > 01 Dipartimenti > Scienze biomediche
002 Altri enti e centri di ricerca del Nord Sardegna > National laboratory of the national institute of biostructures and biosystems, Osilo
Publisher:Wiley
eISSN:1522-2683
Deposited On:18 Aug 2009 10:05

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