| Autor: |
Lee YP; Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University, Chuncheon, Korea., Kim DW, Lee MJ, Jeong MS, Kim SY, Lee SH, Jang SH, Park J, Kang TC, Won MH, Cho SW, Kwon OS, Eum WS, Choi SY |
| Jazyk: |
angličtina |
| Zdroj: |
BMB reports [BMB Rep] 2008 May 31; Vol. 41 (5), pp. 408-13. |
| DOI: |
10.5483/bmbrep.2008.41.5.408 |
| Abstrakt: |
Pyridoxal-5'-phosphate phosphatase (PLPP) catalyzes the dephosphorylation of pyridoxal-5'-phosphate (PLP). A human brain PLPP gene was fused with a PEP-1 peptide and produced a genetic in-frame PEP-1-PLPP fusion protein. The purified PEP-1-PLPP fusion protein was efficiently transduced into PC12 cells in a time- and dose-dependent manner when added exogenously to culture media. Once inside the cells, the transduced PEP-1-PLPP fusion protein was stable for 36 h. The concentration of PLP was markedly decreased by the addition of exogenous PEP-1-PLPP to media pretreated with the vitamin B(6) precursors; pyridoxine, pyridoxal kinase and pyridoxine-5'-phosphate oxidase into cells. The results suggest that the transduction of the PEP-1-PLPP fusion protein can be one mode of PLP level regulation, and to replenish this enzyme in the various neurological disorders related to vitamin B(6). |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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