Promiscuous activity of arginine:glycine amidinotransferase is responsible for the synthesis of the novel cardiovascular risk factor homoarginine.
| Autor: | Davids M; Metabolic Laboratory, Department of Clinical Chemistry, VU University Medical Center, Amsterdam, The Netherlands., Ndika JD, Salomons GS, Blom HJ, Teerlink T |
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| Jazyk: | angličtina |
| Zdroj: | FEBS letters [FEBS Lett] 2012 Oct 19; Vol. 586 (20), pp. 3653-7. Date of Electronic Publication: 2012 Aug 29. |
| DOI: | 10.1016/j.febslet.2012.08.020 |
| Abstrakt: | Low plasma homoarginine has emerged as a risk marker for cardiovascular disease. We exploited cells of a patient with a rare inborn error of metabolism to explore potential pathways of homoarginine synthesis, using stable isotopes and mass spectrometry. Control lymphoblasts, as opposed to lymphoblasts from an arginine:glycine amidinotransferase (AGAT)-deficient patient, were able to synthesize homoarginine from arginine and lysine. In contrast, in a patient with a deficiency of the urea cycle enzyme argininosuccinate synthase, plasma homoarginine was not decreased. We conclude that promiscuous activity of AGAT, a key enzyme in creatine synthesis, plays a pivotal role in homoarginine synthesis. (Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.) |
| Databáze: | MEDLINE |
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