title: Hampered expression of isoaspartyl protein carboxyl methyltransferase gene in the human cataractous lens.
abstract: Isoaspartyl protein carboxyl methyltransferase (PIMT) is implicated in the repair of age-damaged proteins by converting altered aspartic acid residues to normal L-aspartic acid residues. Northern blot and reverse transcription (RT)-PCR analyses have revealed that PIMT gene expression in the human lens is detected exclusively in epithelial cells, and that the mRNA levels in cataractous lens epithelia are significantly lower than those in normal age-matched lens tissue. These results suggest that PIMT may play a vital role in maintaining the clarity of the lens and preventing cataract formation.
mesh_terms: D001224:Aspartic Acid / Q000378:metabolism; D001483:Base Sequence; D015152:Blotting, Northern; D002386:Cataract / Q000201:enzymology* / Q000235:genetics; D004848:Epithelium / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D007908:Lens, Crystalline / Q000201:enzymology*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D011496:Protein Methyltransferases / Q000235:genetics*; D012333:RNA, Messenger / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase
chemical_list: D012333:RNA, Messenger; D001224:Aspartic Acid; D011496:Protein Methyltransferases; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D012194:RNA-Directed DNA Polymerase