Estrous cycle dependent regulation of peptidylarginine deiminase transcripts in female rat pituitary

Watanabe, Kazutada; Hikichi, Kiyoko; Nagata, Saburo; Senshu, Tatsuo

doi:10.1016/s0006-291x(05)80168-8

Cited by 13 publications

(8 citation statements)

References 21 publications

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“…5 B). Watanabe et al have also reported on the estrous cycle variations of rat uterine peptidylarginine deiminase mRNA [18], and they obtained similar results except for the maximal level being at diestrus. These findings indicate that the metabolism of uterine peptidylarginine-deiminase mRNA as well as the enzyme activity are significantly different between the mouse and the rat.…”

Section: Identification Of the N-terminal And C-terminal Sequences Amentioning

confidence: 66%

cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase

Tsuchida

Takahara

Minami

et al. 1993

European Journal of Biochemistry

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Peptidylarginine deiminase is a protein‐modulating enzyme which converts the arginine residues in proteins to citrulline residues. This study describes the complete primary structure of mouse peptidylarginine deiminase, which was deduced from nucleotide sequence analysis of cDNA clones plus proteochemical analysis of the purified enzyme. The composite cDNA sequence contained a 5′ untranslated region of 7 bases, an open reading frame of 2019 bases that encoded 673 amino acids, a 3′ untranslated region of 2662 bases, and part of a poly(A) tail. The N‐terminal and C‐terminal sequences of the enzyme matched the sequences deduced from nucleotide analysis. Furthermore, we determined that the N‐terminal sequence was Nα‐acetyl‐Met‐Gln‐, a sequence which has never previously been reported among Nα‐acetyl‐Met proteins. The Arg 352 of the enzyme was converted to a citrulline residue and the potential Asn‐linked glycosylation site (Asn542‐Glu543‐Ser544) had no carbohydrate moiety. Thus, mouse peptidylarginine deiminase consists of 673 amino acids with a molecular mass of 76 260. Mouse peptidylarginine deiminase mRNA has two AU‐rich structures in the 3′ untranslated region which exhibit a high degree of similarity to those in lymphokine, cytokine and proto‐oncogene mRNA species. Since the rat enzyme (previously reported) does not possess these characteristic structures, we compared the levels of enzyme activity and mRNA in the mouse and rat uterus at four defined phases of the estrous cycle. The degradation of peptidylarginine deiminase and its mRNA proceeded significantly faster in the mouse than in the rat. We speculate that the unusual structure of the mouse enzyme and its mRNA be involved in this species‐specific rapid degradation.

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Section: Identification Of the N-terminal And C-terminal Sequences Amentioning

confidence: 66%

cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase

Tsuchida

Takahara

Minami

et al. 1993

European Journal of Biochemistry

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Section: Pituitarymentioning

confidence: 99%

“…First, Senshu et al showed that ovariectomy of rats causes a severe drop in pituitary PAD activity; however, this activity could be restored by repeated injections of 17β-estradiol [58,60]. Interestingly, they also found that, in the pituitary, PAD mRNA levels did not directly correlate with enzymatic activity, leading the authors to speculate that PAD mRNA might be regulated at the translational and stability levels [60]. Second, investigators found that 17β-estradiol causes a dose-dependent increase in PAD biosynthesis and activity, reaching levels four-to fivefold higher than that of controls in the somato-lactotroph rat pituitary-derived MtT/S cells line [61].…”

Section: Pituitarymentioning

confidence: 99%

Role for Peptidylarginine Deiminase Enzymes in Disease and Female Reproduction

2012

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“…Several in vivo experiments in rodents have shown an oestrogen‐modulation of Pad2 activity in the pituitary gland and the uterus (during the oestrous cycle). This was also observed in the MtT/S rat cell line (derived from pituitary cells) cultured in vitro [53–59]. PAD activity is low in the uterus of ovariectomized rats and restored to a normal level in 4 days after injections of oestradiol, but not of testosterone or progesterone [53].…”

Section: Regulation Of Pads and Deimination: Multilock Control Pointsmentioning

confidence: 78%

Update on peptidylarginine deiminases and deimination in skin physiology and severe human diseases

Méchin

Sebbag

Arnaud

et al. 2007

Intern J of Cosmetic Sci

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SynopsisDeimination (or citrullination) is a recently described post-translational modification, but its consequences are not yet well understood. It is catalysed by peptidylarginine deiminases (PADs). These enzymes transform arginyl residues involved in a peptidyl link into citrullyl residues in a calciumdependent manner. Several PAD substrates have already been identified like filaggrin and keratins K1 and K10 in the epidermis, trichohyalin in hair follicles, but also ubiquitous proteins like histones. PADs act in a large panel of physiological functions as cellular differentiation or gene regulation. It has been suggested that deimination plays a role in many major diseases such as rheumatoid arthritis, multiple sclerosis, Alzheimer's disease and psoriasis. Five human genes (PADIs), encoding five highly conserved paralogous enzymes (PAD1-4 and 6), have been characterized. These genes are clustered in a single locus, at 1p35-36 in man. Only PAD1-3 are expressed in human epidermis. PADs seem to be controlled at transcriptional, translational and activity levels and they present particular substrate specificities. In this review, we shall discuss these main biochemical, genetic and functional aspects of PADs together with their pathophysiological implications. Ré suméLa désimination (ou citrullination) est une modification post-traductionnelle catalysée par les peptidylarginine désiminases (PADs), décrite depuis peu et dont les conséquences sont encore mal comprises. Ces enzymes transforment, de façon dépendante du calcium, les résidus arginyl engagés dans un lien peptidique en résidus citrullyl. Plusieurs substrats ont été identifiés: la filaggrine et les cytokératines K1 et K10 de l'épiderme, la trichohyaline dans le follicule pileux mais aussi des protéines ubiquistes comme les histones. Les PADs interviennent dans de nombreuses fonctions physiologiques telles que la différenciation cellulaire ou la régulation génique. La désimination pourrait jouer un rôle dans plusieurs maladies sévères et fréquentes comme la polyarthrite rhumatoïde, la sclérose en plaque, la maladie d'Alzheimer ou encore le psoriasis. Cinq gènes humains (PADIs) codant pour 5 enzymes paralogues conservées (PAD1-4 et 6) ont été caractérisés. Ils sont regroupés en un seul locus, en 1p35-36 chez l'homme. Seules les PAD1-3 sont exprimées dans l'épiderme humain. Les PADs semblent contrôlées aux niveaux transcriptionnel et Correspondence: Marie-Claire Méchin, UMR5165, Faculté de Médecine,

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Estrous cycle dependent regulation of peptidylarginine deiminase transcripts in female rat pituitary

Cited by 13 publications

References 21 publications

cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase

cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase

Role for Peptidylarginine Deiminase Enzymes in Disease and Female Reproduction

Update on peptidylarginine deiminases and deimination in skin physiology and severe human diseases

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