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

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

In: PLOS ONE, Vol. 8, No. 2, 2013, p. e55483.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Esse, R, Rocha, MS, Barroso, M, Florindo, C, Teerlink, T, Kok, RM, Smulders, YM, Rivera, I, Leandro, P, Koolwijk, P, Castro, R, Blom, HJ & de Almeida, IT 2013, 'Protein arginine methylation is more prone to inhibition by S-adenosylhomocysteine than DNA methylation in vascular endothelial cells', PLOS ONE, vol. 8, no. 2, pp. e55483. https://doi.org/10.1371/journal.pone.0055483

APA

Esse, R., Rocha, M. S., Barroso, M., Florindo, C., Teerlink, T., Kok, R. M., Smulders, Y. M., Rivera, I., Leandro, P., Koolwijk, P., Castro, R., Blom, H. J., & de Almeida, I. T. (2013). Protein arginine methylation is more prone to inhibition by S-adenosylhomocysteine than DNA methylation in vascular endothelial cells. PLOS ONE, 8(2), e55483. https://doi.org/10.1371/journal.pone.0055483

Vancouver

Esse R, Rocha MS, Barroso M, Florindo C, Teerlink T, Kok RM et al. Protein arginine methylation is more prone to inhibition by S-adenosylhomocysteine than DNA methylation in vascular endothelial cells. PLOS ONE. 2013;8(2):e55483. https://doi.org/10.1371/journal.pone.0055483

Bibtex

@article{87479dc58594411b98c21aab3ea6d774,
title = "Protein arginine methylation is more prone to inhibition by S-adenosylhomocysteine than DNA methylation in vascular endothelial cells",
abstract = "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 hypomethylation. We aimed at determining the extent at which protein arginine methylation status is affected by accumulation of intracellular AdoHcy. AdoHcy accumulation in human umbilical vein endothelial cells was induced by inhibition of AdoHcy hydrolase by adenosine-2,3-dialdehyde (AdOx). As a measure of protein arginine methylation status, the levels of monomethylarginine (MMA) and asymmetric and symmetric dimethylated arginine residues (ADMA and SDMA, respectively) in cell protein hydrolysates were measured by HPLC. A 10% decrease was observed at a 2.5-fold increase of intracellular AdoHcy. Western blotting revealed that the translational levels of the main enzymes catalyzing protein arginine methylation, protein arginine methyl transferases (PRMTs) 1 and 5, were not affected by AdoHcy accumulation. Global DNA methylation status was evaluated by measuring 5-methylcytosine and total cytosine concentrations in DNA hydrolysates by LC-MS/MS. DNA methylation decreased by 10% only when intracellular AdoHcy concentration accumulated to 6-fold of its basal value. In conclusion, our results indicate that protein arginine methylation is more sensitive to AdoHcy accumulation than DNA methylation, pinpointing a possible new player in methylation-related pathology.",
keywords = "Arginine, Cells, Cultured, DNA Methylation, Endothelium, Vascular, Humans, Real-Time Polymerase Chain Reaction, Reverse Transcriptase Polymerase Chain Reaction, S-Adenosylmethionine, Journal Article, Research Support, Non-U.S. Gov't",
author = "Ruben Esse and Rocha, {Monica S} and Madalena Barroso and Cristina Florindo and Tom Teerlink and Kok, {Robert M} and Smulders, {Yvo M} and Isabel Rivera and Paula Leandro and Pieter Koolwijk and Rita Castro and Blom, {Henk J} and {de Almeida}, {Isabel Tavares}",
year = "2013",
doi = "10.1371/journal.pone.0055483",
language = "English",
volume = "8",
pages = "e55483",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "2",

}

RIS

TY - JOUR

T1 - Protein arginine methylation is more prone to inhibition by S-adenosylhomocysteine than DNA methylation in vascular endothelial cells

AU - Esse, Ruben

AU - Rocha, Monica S

AU - Barroso, Madalena

AU - Florindo, Cristina

AU - Teerlink, Tom

AU - Kok, Robert M

AU - Smulders, Yvo M

AU - Rivera, Isabel

AU - Leandro, Paula

AU - Koolwijk, Pieter

AU - Castro, Rita

AU - Blom, Henk J

AU - de Almeida, Isabel Tavares

PY - 2013

Y1 - 2013

N2 - 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 hypomethylation. We aimed at determining the extent at which protein arginine methylation status is affected by accumulation of intracellular AdoHcy. AdoHcy accumulation in human umbilical vein endothelial cells was induced by inhibition of AdoHcy hydrolase by adenosine-2,3-dialdehyde (AdOx). As a measure of protein arginine methylation status, the levels of monomethylarginine (MMA) and asymmetric and symmetric dimethylated arginine residues (ADMA and SDMA, respectively) in cell protein hydrolysates were measured by HPLC. A 10% decrease was observed at a 2.5-fold increase of intracellular AdoHcy. Western blotting revealed that the translational levels of the main enzymes catalyzing protein arginine methylation, protein arginine methyl transferases (PRMTs) 1 and 5, were not affected by AdoHcy accumulation. Global DNA methylation status was evaluated by measuring 5-methylcytosine and total cytosine concentrations in DNA hydrolysates by LC-MS/MS. DNA methylation decreased by 10% only when intracellular AdoHcy concentration accumulated to 6-fold of its basal value. In conclusion, our results indicate that protein arginine methylation is more sensitive to AdoHcy accumulation than DNA methylation, pinpointing a possible new player in methylation-related pathology.

AB - 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 hypomethylation. We aimed at determining the extent at which protein arginine methylation status is affected by accumulation of intracellular AdoHcy. AdoHcy accumulation in human umbilical vein endothelial cells was induced by inhibition of AdoHcy hydrolase by adenosine-2,3-dialdehyde (AdOx). As a measure of protein arginine methylation status, the levels of monomethylarginine (MMA) and asymmetric and symmetric dimethylated arginine residues (ADMA and SDMA, respectively) in cell protein hydrolysates were measured by HPLC. A 10% decrease was observed at a 2.5-fold increase of intracellular AdoHcy. Western blotting revealed that the translational levels of the main enzymes catalyzing protein arginine methylation, protein arginine methyl transferases (PRMTs) 1 and 5, were not affected by AdoHcy accumulation. Global DNA methylation status was evaluated by measuring 5-methylcytosine and total cytosine concentrations in DNA hydrolysates by LC-MS/MS. DNA methylation decreased by 10% only when intracellular AdoHcy concentration accumulated to 6-fold of its basal value. In conclusion, our results indicate that protein arginine methylation is more sensitive to AdoHcy accumulation than DNA methylation, pinpointing a possible new player in methylation-related pathology.

KW - Arginine

KW - Cells, Cultured

KW - DNA Methylation

KW - Endothelium, Vascular

KW - Humans

KW - Real-Time Polymerase Chain Reaction

KW - Reverse Transcriptase Polymerase Chain Reaction

KW - S-Adenosylmethionine

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1371/journal.pone.0055483

DO - 10.1371/journal.pone.0055483

M3 - SCORING: Journal article

C2 - 23408989

VL - 8

SP - e55483

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 2

ER -