| First Author | Anguera MC | Year | 2006 |
| Journal | Arch Biochem Biophys | Volume | 455 |
| Issue | 2 | Pages | 175-87 |
| PubMed ID | 17055997 | Mgi Jnum | J:116328 |
| Mgi Id | MGI:3694034 | Doi | 10.1016/j.abb.2006.09.008 |
| Citation | Anguera MC, et al. (2006) Methenyltetrahydrofolate synthetase is a high-affinity catecholamine-binding protein. Arch Biochem Biophys 455(2):175-87 |
| abstractText | Recombinant mouse 5,10-methenyltetrahydrofolate synthetase (MTHFS) was expressed in Escherichia coli and shown to co-purify with a chromophore that had a lambda(max) at 320nm. The chromophore remained bound to MTHFS during extensive dialysis, but dissociated from MTHFS when its substrate, 5-formyltetrahydrofolate, was bound. The chromophore was identified as an oxidized catecholamine by mass spectrometry and absorption spectroscopy. Purified recombinant mouse MTHFS and rabbit liver MTHFS proteins were shown to bind oxidized N-acetyldopamine (NADA) tightly. The addition of NADA to cell culture medium accelerated markedly folate turnover and decreased both folate accumulation and total cellular folate concentrations in MCF-7 cells. Expression of the MTHFS cDNA in MCF-7 cells increased the concentration of NADA required to deplete cellular folate. The results of this study are the first to identify a link between catecholamines and one-carbon metabolism and demonstrate that NADA accelerates folate turnover and impairs cellular folate accumulation in MCF-7 cells. |
