Protein arginine methylation is more prone to inhibition by S-adenosylhomocysteine than DNA methylation in vascular endothelial cells

Methyltransferases use S-adenosylmethionine (AdoMet) as methyl group donor, forming S-adenosylhomocysteine (AdoHcy) and methylated substrates, including DNA and proteins. AdoHcy inhibits most methyltransferases. Accumulation of intracellular AdoHcy secondary to Hcy elevation elicits global DNA hypom...

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Veröffentlicht in:	PloS one 2013-02, Vol.8 (2), p.e55483-e55483
Hauptverfasser:	Esse, Ruben, Rocha, Monica S, Barroso, Madalena, Florindo, Cristina, Teerlink, Tom, Kok, Robert M, Smulders, Yvo M, Rivera, Isabel, Leandro, Paula, Koolwijk, Pieter, Castro, Rita, Blom, Henk J, de Almeida, Isabel Tavares
Format:	Artikel
Sprache:	eng
Schlagworte:	Accumulation Adenosine Adenosylmethionine Arginine Arginine - metabolism Bioaccumulation Biochemistry Biology Cells, Cultured Cytosine Deoxyribonucleic acid DNA DNA Methylation Endothelial cells Endothelium Endothelium, Vascular - cytology Endothelium, Vascular - metabolism Enzymes Gene expression High performance liquid chromatography Homocysteine Humans Hydrolase Hydrolases Hydrolysates Intracellular Liquid chromatography Medicine Metabolism Methylation Methyltransferases Pharmaceutical sciences Pharmacy Physiology Polymethyl methacrylate Protein folding Protein hydrolysates Proteins Pyrimidines Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction Risk factors S-Adenosylmethionine S-Adenosylmethionine - metabolism Signal transduction Studies Substrate inhibition Substrates Umbilical vein Western blotting
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