Literature DB >> 16973334

Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis.

Stéphane Chavanas1, Marie-Claire Méchin, Rachida Nachat, Véronique Adoue, Fanny Coudane, Guy Serre, Michel Simon.   

Abstract

Deimination corresponds to the transformation of arginine residues within a peptide sequence into citrulline residues. Catalyzed by peptidylarginine deiminases, it decreases the net positive charge of proteins, alters intra and intermolecular ionic interactions and probably the folding of target proteins. Deimination has recently been implicated in several physiological and pathological processes. Here, we describe the enzymes involved in this post-translational modification, focusing on their expression, location and roles in skin, as well as their known protein substrates in the epidermis and hair follicles. We discuss also the potential involvement of deimination in human diseases including cutaneous disorders.

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Year:  2006        PMID: 16973334     DOI: 10.1016/j.jdermsci.2006.07.004

Source DB:  PubMed          Journal:  J Dermatol Sci        ISSN: 0923-1811            Impact factor:   4.563


  29 in total

Review 1.  Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation.

Authors:  Erin E Witalison; Paul R Thompson; Lorne J Hofseth
Journal:  Curr Drug Targets       Date:  2015       Impact factor: 3.465

2.  Characterisation of skin barrier function using bioengineering and biophysical techniques.

Authors:  Quan Yang; Richard H Guy
Journal:  Pharm Res       Date:  2014-08-05       Impact factor: 4.200

3.  Kallikrein-related peptidase 5 functions in proteolytic processing of profilaggrin in cultured human keratinocytes.

Authors:  Jun-ichi Sakabe; Mami Yamamoto; Satoshi Hirakawa; Akira Motoyama; Isao Ohta; Kazuki Tatsuno; Taisuke Ito; Kenji Kabashima; Toshihiko Hibino; Yoshiki Tokura
Journal:  J Biol Chem       Date:  2013-04-29       Impact factor: 5.157

4.  Bleomycin hydrolase is regulated biphasically in a differentiation- and cytokine-dependent manner: relevance to atopic dermatitis.

Authors:  Yayoi Kamata; Mami Yamamoto; Fumitaka Kawakami; Ryoji Tsuboi; Atsushi Takeda; Kazuhiko Ishihara; Toshihiko Hibino
Journal:  J Biol Chem       Date:  2010-12-29       Impact factor: 5.157

5.  Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type I.

Authors:  Masaki Unno; Saya Kinjo; Kenji Kizawa; Hidenari Takahara
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-11-28

6.  Deimination of human filaggrin-2 promotes its proteolysis by calpain 1.

Authors:  Chiung-Yueh Hsu; Julie Henry; Anne-Aurélie Raymond; Marie-Claire Méchin; Valérie Pendaries; Dany Nassar; Britta Hansmann; Stéfana Balica; Odile Burlet-Schiltz; Anne-Marie Schmitt; Hidenari Takahara; Carle Paul; Guy Serre; Michel Simon
Journal:  J Biol Chem       Date:  2011-04-29       Impact factor: 5.157

7.  PADI4 and tumourigenesis.

Authors:  Xiaotian Chang; Kehua Fang
Journal:  Cancer Cell Int       Date:  2010-03-12       Impact factor: 5.722

8.  Neutral cysteine protease bleomycin hydrolase is essential for the breakdown of deiminated filaggrin into amino acids.

Authors:  Yayoi Kamata; Aya Taniguchi; Mami Yamamoto; Junko Nomura; Kazuhiko Ishihara; Hidenari Takahara; Toshihiko Hibino; Atsushi Takeda
Journal:  J Biol Chem       Date:  2009-03-13       Impact factor: 5.157

Review 9.  Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis.

Authors:  Shu Wang; Yanming Wang
Journal:  Biochim Biophys Acta       Date:  2013-07-13

10.  Neutral loss of isocyanic acid in peptide CID spectra: a novel diagnostic marker for mass spectrometric identification of protein citrullination.

Authors:  Gang Hao; Danchen Wang; Jane Gu; Qiuying Shen; Steven S Gross; Yanming Wang
Journal:  J Am Soc Mass Spectrom       Date:  2008-12-30       Impact factor: 3.109

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