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Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases

1
UDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Paul Sabatier, Université de Toulouse Midi-Pyrénées, U1056, 31059 Toulouse, France
2
University of Ibaraki, School of Agriculture, Ibaraki 300-0393, Japan
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(2), 566; https://doi.org/10.3390/ijms21020566
Received: 19 December 2019 / Revised: 10 January 2020 / Accepted: 12 January 2020 / Published: 15 January 2020
Deimination, also known as citrullination, corresponds to the conversion of the amino acid arginine, within a peptide sequence, into the non-standard amino acid citrulline. This post-translational modification is catalyzed by a family of calcium-dependent enzymes called peptidylarginine deiminases (PADs). Deimination is implicated in a growing number of physiological processes (innate and adaptive immunity, gene regulation, embryonic development, etc.) and concerns several human diseases (rheumatoid arthritis, neurodegenerative diseases, female infertility, cancer, etc.). Here, we update the involvement of PADs in both the homeostasis of skin and skin diseases. We particularly focus on keratinocyte differentiation and the epidermal barrier function, and on hair follicles. Indeed, alteration of PAD activity in the hair shaft is responsible for two hair disorders, the uncombable hair syndrome and a particular form of inflammatory scarring alopecia, mainly affecting women of African ancestry.
Keywords: epidermis; peptidylarginine deiminase; citrullination; hair; alopecia; posttranslational modification; keratinocyte; differentiation epidermis; peptidylarginine deiminase; citrullination; hair; alopecia; posttranslational modification; keratinocyte; differentiation
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Méchin, M.-C.; Takahara, H.; Simon, M. Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases. Int. J. Mol. Sci. 2020, 21, 566.

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