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

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.