Abstract
Citrulline residues are detected in keratins and filaggrin in the cornified layers
of mammalian epidermis. Such citrulline residues are formed by the enzymatic deimination
of arginine residues by peptidylarginine deiminases (EC 3.5.3.15). Major deiminated
keratins are derived from keratin K1. Two arginine residues identified as preferred
deimination sites in mouse K1 are located in its V subdomains. To develop an immunochemical
probe which recognizes the deiminated peptide sequence specifically, we enzymatically
deiminated an undecapeptide corresponding to the deiminated peptide sequence identified
in the V2 subdomain for immunizing rabbits. An IgG fraction obtained from the antiserum
was affinity-purified using an immobilized peptide column. The affinity-purified IgG
showed high specificity towards partially degraded keratin K1 obtained from the cornified
layer of 3-day-old mouse epidermis. It also yielded intense signals of unidentified
minor components localized in the cornified layers of late embryonic and early postnatal
mouse epidermis. Comparative studies using different types of the enzymes suggested
that peptidylarginine deiminase type I acted on the arginine residue in the V2 subdomain
of keratin K1 more readily than peptidylarginine deiminase type II. The data are discussed
in conjunction with possible factors influencing the specificity of the enzyme reaction.
Keywords
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Article info
Publication history
Accepted:
January 20,
1999
Received:
December 10,
1998
Identification
Copyright
© 1999 Elsevier Science Ireland Ltd. Published by Elsevier Inc. All rights reserved.
