Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6

Chavanas, Stéphane; Méchin, Marie-Claire; Takahara, Hidenari; Kawada, Akira; Nachat, Rachida; Serre, Guy; Simon, Michel

doi:10.1016/j.gene.2003.12.038

Cited by 181 publications

(185 citation statements)

References 23 publications

(34 reference statements)

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“…PAD Isozymes Modified S100A3 in Hair Follicle-In the mammalian cutaneous epithelium, protein-citrullination is reported to be catalyzed by PAD1, PAD2, and PAD3 (38) among the five known isozymes (39). In hair follicles, PAD3 is located in the cuticular cells expressing S100A3 (24 -26) as well as in the inner root sheaths and the medulla, where it co-localizes with trichohyalin (35,40).…”

Section: Citrullinated S100a3 Derived From Hair Follicles Andmentioning

confidence: 99%

Specific Citrullination Causes Assembly of a Globular S100A3 Homotetramer

Kizawa¹,

Takahara

Troxler

et al. 2008

Journal of Biological Chemistry

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S100A3 is a unique member of the Ca 2؉ -binding S100 protein family with the highest cysteine content and affinity for Zn 2؉ . This protein is highly expressed in the differentiating cuticular cells within the hair follicle and organized into mature hair cuticles. Previous studies suggest a close association of S100A3 with epithelial differentiation, leading to hair shaft formation, but its molecular function is still unknown. By two-dimensional PAGE-Western blot analyses using a modified citrulline antibody, we discovered that more than half of the arginine residues of native S100A3 are progressively converted to citrullines by Ca 2؉ -dependent peptidylarginine deiminases. Confocal immunofluorescent microscopy showed that the cytoplasmic S100A3 within the cuticular layer is mostly co-localized with the type III isoform of peptidylarginine deiminase (PAD3) but not with PAD1. Recombinant PAD1 and PAD2 are capable of converting all 4 arginines in recombinant S100A3, whereas PAD3 specifically converts only Arg-51 into citrulline. Gel filtration analyses showed that either enzymatic conversion of Arg-51 in S100A3 to citrulline or its mutational substitution with alanine (R51A) promotes a homotetramer assembly. Fluorescent titration of R51A suggested that its potential Ca 2؉ binding property increased during tetramerization. A prototype structural model of the globular Ca 2؉ -bound S100A3 tetramer with citrulline residues is presented. High concentrations of S100A3 homotetramer might provide the millimolar level of Ca 2؉ required for hair cuticular barrier formation.

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Section: Citrullinated S100a3 Derived From Hair Follicles Andmentioning

confidence: 99%

Specific Citrullination Causes Assembly of a Globular S100A3 Homotetramer

Kizawa¹,

Takahara

Troxler

et al. 2008

Journal of Biological Chemistry

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“…The most recently identifi ed PAD, PAD6, is found in male and female germ cells and is a crucial enzyme in fertility. The enzyme is essential for normal development of an embryo beyond the two-cell stage ( 54,61 ).…”

Section: Discussionmentioning

confidence: 99%

Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation

Proost¹,

Loos²,

Mortier³

et al. 2008

J Cell Biol

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“…The process requires high concentrations of Ca 2+ and is produced in inflammatory environments (Baeten et al, 2001;Chavanas et al, 2004;Vossenaar et al, 2003). Other mechanism that triggers arginine deimination is apoptosis (Baeten et al, 2001).…”

Section: Citrullinationmentioning

confidence: 99%

HLA and Citrullinated Peptides in Rheumatoid Arthritis

Álvarez¹

2011

Autoimmune Disorders - Pathogenetic Aspects

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Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6

Cited by 181 publications

References 23 publications

Specific Citrullination Causes Assembly of a Globular S100A3 Homotetramer

Specific Citrullination Causes Assembly of a Globular S100A3 Homotetramer

Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation

HLA and Citrullinated Peptides in Rheumatoid Arthritis

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