Abstract
We previously reported the identification of a novel gene, Bdm 1 (brain development-related molecule 1), that was up-regulated during postnatal brain development. We describe here the characterization of BDM1 protein in the brain. Antibody was raised against a synthetic peptide corresponding to the C-terminal part of the predicted BDM 1. Western blotting using this antibody revealed two forms of BDM1, 63 kDa and 64 kDa in size, very different to the 38 kDa size predicted from the open reading frame of a Bdm1 cDNA. The 64-kDa protein was detected during embryogenesis and the intensity of this band gradually decreased after birth. In contrast, the intensity of the 63-kDa band increased after birth. In vitro transcription and translation of Bdm 1 cDNA produced a 38-kDa protein. When brain extracts were treated by glycopeptidase A, Western blotting of these samples also revealed a 38-kDa band, suggesting that BDM 1 is modified by attachment of sugar chains. Cell fractionation of the embryonic brain demonstrated that BDM 1 was distributed mainly in the cytosolic fraction. Cytoplasmic distribution of EGFP-BDM 1 was also observed after transfection of an expression construct into PC12 cells. Thus, BDM 1 is expressed in the brain in a developmentally regulated manner.
