TY - JOUR
T1 - Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis
AU - Wang, Shu
AU - Wang, Yanming
N1 - Funding Information:
We thank members of the Wang lab as well as the Center for Eukaryotic Gene Regulation for helpful discussions. Shu Wang was partially supported by the BMMB graduate program . Research is supported by NIH R01 CA136856 .
PY - 2013/10
Y1 - 2013/10
N2 - Peptidylarginine deiminases are a family of enzymes that mediate post-translational modifications of protein arginine residues by deimination or demethylimination to produce citrulline. In vitro, the activity of PADs is dependent on calcium and reductive reagents carrying a free sulfhydryl group. The discovery that PAD4 can target both arginine and methyl-arginine for citrullination about 10. years ago renewed our interest in studying this family of enzymes in gene regulation and their physiological functions. The deregulation of PADs is involved in the etiology of multiple human diseases, including cancers and autoimmune disorders. There is a growing effort to develop isoform specific PAD inhibitors for disease treatment. However, the regulation of the activity of PADs in vivo remains largely elusive, and we expect that much will be learned about the role of these enzymes in a normal life cycle and under pathology conditions.
AB - Peptidylarginine deiminases are a family of enzymes that mediate post-translational modifications of protein arginine residues by deimination or demethylimination to produce citrulline. In vitro, the activity of PADs is dependent on calcium and reductive reagents carrying a free sulfhydryl group. The discovery that PAD4 can target both arginine and methyl-arginine for citrullination about 10. years ago renewed our interest in studying this family of enzymes in gene regulation and their physiological functions. The deregulation of PADs is involved in the etiology of multiple human diseases, including cancers and autoimmune disorders. There is a growing effort to develop isoform specific PAD inhibitors for disease treatment. However, the regulation of the activity of PADs in vivo remains largely elusive, and we expect that much will be learned about the role of these enzymes in a normal life cycle and under pathology conditions.
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U2 - 10.1016/j.bbagrm.2013.07.003
DO - 10.1016/j.bbagrm.2013.07.003
M3 - Review article
C2 - 23860259
AN - SCOPUS:84883214212
SN - 1874-9399
VL - 1829
SP - 1126
EP - 1135
JO - Biochimica et Biophysica Acta - Gene Regulatory Mechanisms
JF - Biochimica et Biophysica Acta - Gene Regulatory Mechanisms
IS - 10
ER -