Human Peptidylarginine Deiminase Type III: Molecular Cloning and Nucleotide Sequence of the cDNA, Properties of the Recombinant Enzyme, and Immunohistochemical Localization in Human Skin

    November 2000 in “ ˜The œjournal of investigative dermatology/Journal of investigative dermatology ”
    Takeshi Kanno, Masakazu Shiraiwa, Hidenari Takahara, Akira Kawada, Tadashi Tezuka, Jun Yamanouchi, Chikako Yosida-Noro, Atsushi Yoshiki, Moriaki Kusakabe, Motomu Manabe
    TLDR PAD3 plays a key role in hair and skin protein structure and may be linked to skin diseases.
    The study successfully cloned and sequenced the cDNA of human Peptidylarginine Deiminase Type III (PAD3), produced the recombinant enzyme in E. coli, and localized it in human skin using immunohistochemistry. The recombinant PAD3 exhibited significant catalytic activity towards structural proteins in the epidermis and hair follicles, particularly filaggrin and trichohyalin. Immunohistochemical analysis revealed PAD3's predominant localization in the inner and outer root sheaths of hair follicles, suggesting its role in modulating hair structural proteins during hair formation. The enzyme's expression in the epidermis was minimal, indicating its primary function in hair follicles.
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