Identification and characterisation of arsenite (+3 Oxidation State) methyltransferase (AS3MT) in mouse neuroblastoma cell line N1E-115

• Published in: Amino acids Vol. 35; no. 2; pp. 355 - 358
• Main Authors: John, J. P. P, Oh, J.-E, Pollak, A, Lubec, G
• Format: Journal Article
• Language: English
• Published: Vienna Vienna : Springer-Verlag 01.08.2008; Springer-Verlag; Springer Nature B.V
• Subjects: Analytical Chemistry; Animals; Arsenite methyltransferase; Arsenites - chemistry; Biochemical Engineering; Biochemistry; Biomedical and Life Sciences; Chromatography, Liquid - methods; Electrophoresis, Gel, Two-Dimensional; Life Sciences; MALDI-TOF-TOF; Mass Spectrometry - methods; Methyltransferases - chemistry; Methyltransferases - isolation & purification; Mice; Nano-LC-ESI-MS/MS; Neurobiology; Neuroblastoma - enzymology; Neuroblastoma cells; Oxidation; Proteins; Proteomics; Tumor Cells, Cultured; Keywords: Arsenite methyltransferase – MALDI-TOF-TOF – Nano-LC-ESI-MS/MS – Neuroblastoma cells
• ISSN: 0939-4451; 1438-2199
• DOI: 10.1007/s00726-007-0613-1

Handling and detoxification of metals by enzymes is a major issue that is not in the focus of current biomedical research concepts. The finding of the presence of arsenic (+3 Oxidation State) methyltransferase (AS3MT) in neuroblastoma cells NE-115 as a high abundance protein made us investigate primary structure of AS3MT reflecting an example of metal-handling in eucaryotes. Proteins extracted from NE-115 cells were run on 2-DE followed by two different mass spectrometrical methods. High sequence coverage was obtained by multiple protease digestion and a sequence conflict was solved at arginine 335. These findings are important when future studies on this enzyme are designed at the protein level and in particular, when antibodies against this protein will be generated.