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Asbestos‐induced changes in protein arginine methylation in human epithelial cells
Author(s) -
Pande Priyadarshini,
Hardman Jared,
Aust Ann E,
Hevel Joan M
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.lb118-c
Subject(s) - methylation , arginine , protein arginine methyltransferase 5 , methyltransferase , protein methylation , cytosol , gene isoform , microbiology and biotechnology , a549 cell , apoptosis , biochemistry , chemistry , biology , enzyme , amino acid , gene
Protein Arginine Methyltransferases (PRMTs) catalyze the addition of one or two methyl groups to the guanidino nitrogens of arginine side chains. Although this chemical modification may appear subtle, recent evidence has demonstrated complex levels of regulation and farreaching effects caused by protein arginine methylation. The current study shows that the global pattern of protein arginine methylation in A549 human lung epithelial cells undergoes dramatic changes during asbestos‐induced apoptosis. Changes in mRNA expression and protein expression of the various PRMT isoforms are evident. Most notably, PRMT 1 shows a redistribution between cytosolic and nuclear compartments and PRMT6 is only detectable in these cells after asbestos treatment.