Immunohistochemical Demonstration of Peptidylarginine Deiminase in Human Sweat Glands

Urano, Yoshio; Watanabe, Kazutada; Sakaki, Akihiko; Arase, Seiji; Watanabe, Yasumori; Shigemi, Fumio; Takeda, Katsuyuki; Akiyama, K.; Senshu, Tatsuo

doi:10.1097/00000372-199006000-00005

Cited by 28 publications

(18 citation statements)

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“…In agreement, only PAD1-3 activities were detected in newborn mouse skin (Terakawa et al, 1991). But PAD2 was not immunodetected by Urano et al (1990) in human epidermis, using a serum directed against rat-PAD2 (Urano et al, 1990). This is probably because of epitope masking caused by the acetone fixation step performed in this work.…”

Section: Discussionsupporting

confidence: 72%

Peptidylarginine Deiminase Isoforms 1–3 Are Expressed in the Epidermis and Involved in the Deimination of K1 and Filaggrin

Nachat

Méchin

Takahara

et al. 2005

Journal of Investigative Dermatology

136

130

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Post-translational conversion of arginine to citrulline residues is catalyzed by peptidylarginine deiminases (PAD). Although the existence of five isoforms of PAD has been reported in rodents and humans, their tissue distribution, substrate specificity, and physiological function have yet to be explored. In the epidermis, deimination of filaggrin and keratins is involved in maintaining hydration of the stratum corneum (SC), and hence the cutaneous barrier function. Here, RT-PCR, western blotting, and confocal microscopy analyses with anti-peptide antibodies highly specific for each of the PAD1-4 demonstrated that only PAD1-3 are expressed in mouse and human epidermis. PAD1 was detected in all layers, including the SC, and PAD2 in all the living layers, whereas PAD3 expression was shown to be restricted to the granular layer and lower SC. Moreover, PAD1 and 3 were observed to co-localize with (pro)filaggrin, and PAD2 to be located at the keratinocyte periphery in the stratum granulosum. We also detected PAD1 in extracts of superficial SC, where K1 is deiminated. Moreover, we showed that PAD1 and 3 are able to modify filaggrin in vitro. These data strongly suggest that each enzyme exerts a specific role in the course of epidermis differentiation.

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Section: Discussionsupporting

confidence: 72%

Peptidylarginine Deiminase Isoforms 1–3 Are Expressed in the Epidermis and Involved in the Deimination of K1 and Filaggrin

Nachat

Méchin

Takahara

et al. 2005

Journal of Investigative Dermatology

136

130

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“…Neoplastic cells from extramammary Paget's disease were found immunoreactive to antibodies against a PAD, which, on the basis of the absence of staining of normal epidermis, could be PAD4 or PAD6 [44]. A recent study revealed that PAD4 is significantly expressed and co-located with CD34 (a marker of haematopoietic progenitor cells) and deiminated cytokeratins in most adenocarcinoma and some non-adenocarcinoma tissue samples [45].…”

Section: Cancermentioning

confidence: 99%

Peptidylarginine deiminases and deimination in biology and pathology: Relevance to skin homeostasis

Chavanas

Méchin

Nachat

et al. 2006

Journal of Dermatological Science

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“…or dual differen tiation [1,6,7], We used antibodies against CEA, S-100 protein. SC, SP-1 and PAD, which are present in the secretory and/or ductal portion of eccrine sweat glands [13][14][15][16][17], to examine whether MAC exhibits sweat gland differentiation. Our findings indicate that the epithelial cords and nests, as well as the ductal structures possess sweat glands differentia tion.…”

Section: Discussionmentioning

confidence: 99%

Microcystic Adnexal Carcinoma

et al. 1993

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Immunohistochemical Demonstration of Peptidylarginine Deiminase in Human Sweat Glands

Cited by 28 publications

References 0 publications

Peptidylarginine Deiminase Isoforms 1–3 Are Expressed in the Epidermis and Involved in the Deimination of K1 and Filaggrin

Peptidylarginine Deiminase Isoforms 1–3 Are Expressed in the Epidermis and Involved in the Deimination of K1 and Filaggrin

Peptidylarginine deiminases and deimination in biology and pathology: Relevance to skin homeostasis

Microcystic Adnexal Carcinoma

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