Abstract
Deimination or citrullination, is a post-translational modification with many facets. It is involved in several basic cellular processes, including gene regulation, embryonic development and terminal differentiation, and also in various pathophysiological mechanisms linked to severe human diseases such as multiple sclerosis and rheumatoid arthritis. Deimination, the calcium-dependent enzymatic conversion of peptidyl-arginine to peptidyl-citrulline, induces a decrease in the charge of the modified proteins with major consequences on their conformation, stability and/or interactions, and therefore on their functions. Five isotypes of peptidylarginine deiminases (1-4 and 6), exist in humans with a variable tissue expression. These highly conserved enzymes are closely regulated at transcriptional and post-transcriptional levels, probably including auto-deimination.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Arginine / metabolism*
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Autoimmune Diseases / enzymology
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Body Water / metabolism
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Calcium / physiology
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Chromatin / metabolism
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Citrulline / metabolism*
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Conserved Sequence
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Cornea / metabolism
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Epidermis / enzymology
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Evolution, Molecular
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Gene Expression Regulation / physiology
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Humans
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Hydrolases / deficiency
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Hydrolases / genetics
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Hydrolases / physiology*
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Isoenzymes / genetics
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Isoenzymes / physiology
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Mice
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Myelin Proteins / metabolism
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Neoplasms / enzymology
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Nervous System Diseases / enzymology
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Protein Processing, Post-Translational* / physiology
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Protein-Arginine Deiminase Type 6
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Protein-Arginine Deiminases
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Skin Diseases / enzymology
Substances
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Chromatin
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Isoenzymes
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Myelin Proteins
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Citrulline
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Arginine
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Hydrolases
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PAD6 protein, mouse
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Protein-Arginine Deiminase Type 6
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Protein-Arginine Deiminases
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Calcium