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Асимметричный диметиларгинин и его роль в этиологии и патогенезе сердечно-сосудистых заболеваний

https://doi.org/10.18705/1607-419X-2008-14-4-306-314

Полный текст:

Аннотация

Асимметричный диметиларгинин (ADMA) представляет собой метилированное производное аминокислоты L-аргинина. Будучи структурным аналогом L-аргинина, ADMA обладает способностью ингибировать синтазу оксида азота (NO), что приводит к уменьшению образования NO в кровеносных сосудах и других тканях. В последние годы значительное внимание исследователей привлекает потенциальная роль ADMA в развитии сердечно-сосудистых заболеваний. Несмотря на то, что существование корреляции между повышением уровня ADMA в плазме крови и развитием эндотелиальной дисфункции, а также сосудистых осложнений было подтверждено во многих эпидемиологических и экспериментальных исследованиях, причинно-следственная связь повышения ADMA и развития сердечно-сосудистых заболеваний остается не доказанной. Для того, чтобы с точностью ответить на вопрос о том, является ли ADMA этиологическим фактором или всего лишь биологическим маркером сердечно-сосудистых заболеваний, требуются дополнительные исследования, посвященные биохимическим, генетическим и фармакологическим аспектам метаболических превращений ADMA.

Об авторах

Р. Н. Родионов
Университет Айовы, Айова Сити, США
Россия


И. О. Блохин
Университет Айовы, Айова Сити, США Федеральный центр сердца, крови и эндокринологии им. В.А. Алмазова, Санкт-Петербург, Россия Санкт-Петербургский государственный медицинский университет им. акад. И.П. Павлова, Санкт-Петербург, Россия
Россия


М. М. Галагудза
Федеральный центр сердца, крови и эндокринологии им. В.А. Алмазова, Санкт-Петербург, Россия Санкт-Петербургский государственный медицинский университет им. акад. И.П. Павлова, Санкт-Петербург, Россия
Россия


Е. В. Шляхто
Федеральный центр сердца, крови и эндокринологии им. В.А. Алмазова, Санкт-Петербург, Россия Санкт-Петербургский государственный медицинский университет им. акад. И.П. Павлова, Санкт-Петербург, Россия
Россия


С. Р. Лентц
Университет Айовы, Айова Сити, США
Россия


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157. Leiper J., and Vallance P. Biological significance of endogenous methylarginines that inhibit nitric oxide synthases. Cardiovasc Res 1999;43:542−548.

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168.

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170.

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172.

173. Rawal N., Rajpurohit R., Paik W.K., and Kim S. Purification and characterization of S-adenosylmethionine-protein-arginine N-methyltransferase from rat liver. Biochem J 1994;300:483−489.

174.

175. Tang J., Frankel A., Cook R.J., Kim S., Paik W.K., Williams K.R., Clarke S., and Herschman H.R. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J Biol Chem 2000;275:7723−7730.

176.

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178.

179. Ogawa T., Kimoto M., Watanabe H., and Sasaoka K. Metabolism of NG,NG-and NG,N'G-dimethylarginine in rats. Arch Biochem Biophys 1987;252:526−537.

180.

181. Ogawa T., Kimoto M., and Sasaoka K. Purification and properties of a new enzyme, NG,NG-dimethylarginine dimethylaminohydrolase, from rat kidney. J Biol Chem 1989;264:10205−10209.

182.

183. Ogawa T., Kimoto M., and Sasaoka K. Dimethylarginine:pyruvate aminotransferase in rats. Purification, properties, and identity with alanine:glyoxylate aminotransferase 2. J Biol Chem 1990;265:20938−20945.

184.

185. Sasaoka K., Ogawa T., and Kimoto M. N-Acetyl conjugates of basic amino acids newly identified in rat urine. Arch Biochem Biophys 1982;219:454−458.

186.

187. Leiper J.M., Santa M., Chubb A., MacAllister R.J., Charles I.G., Whitley G.S., and Vallance P. Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. Biochem J 1999;343 Pt 1:209−214.

188.

189. Tran C.T., Fox M.F., Vallance P., and Leiper J.M. Chromosomal localization, gene structure, and expression pattern of DDAH1: comparison with DDAH2 and implications for evolutionary origins. Genomics 2000;68:101−105.

190.

191. Wang D., Gill P.S., Chabrashvili T., Onozato M.L., Raggio J., Mendonca M., et al. Isoform-specific regulation by N(G),N(G)-dimethylarginine dimethylaminohydrolase of rat serum asymmetric dimethylarginine and vascular endothelium-derived relaxing factor/NO. Circ Res 2007;101:627−635.

192.

193. MacAllister R.J., Parry H., Kimoto M., Ogawa T., Russell R.J., Hodson H., et al. Regulation of nitric oxide synthesis by dimethylarginine dimethylaminohydrolase. Br J Pharmacol 1996;119:1533−1540.

194.

195. Kontani Y., Kaneko M., Kikugawa M., Fujimoto S., and Tamaki N. Identity of D-3-aminoisobutyrate-pyruvate aminotransferase with alanine-glyoxylate aminotransferase 2. Biochim Biophys Acta 1993;1156:161−166.

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Для цитирования:


Родионов Р.Н., Блохин И.О., Галагудза М.М., Шляхто Е.В., Лентц С.Р. Асимметричный диметиларгинин и его роль в этиологии и патогенезе сердечно-сосудистых заболеваний. Артериальная гипертензия. 2008;14(4):306-314. https://doi.org/10.18705/1607-419X-2008-14-4-306-314

For citation:


Rodionov R.N., Blokhin I.O., Galagudza M.M., Shlyakhto E.V., Lentz S.R. The emerging role of asymmetric dimethylarginine in cardiovascular disease. "Arterial’naya Gipertenziya" ("Arterial Hypertension"). 2008;14(4):306-314. (In Russ.) https://doi.org/10.18705/1607-419X-2008-14-4-306-314

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