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 journal 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

Peptidylarginine Deiminase Type III PAD3 recombinant enzyme filaggrin trichohyalin hair follicles inner root sheath outer root sheath epidermis PAD3 hair structural proteins

Studysummary This study found that human peptidylarginine deiminase type III is the predominant isoform in hair follicles and may modulate structural proteins during hair and hair follicle formation.

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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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research Gene Expression of Mouse S100A3, a Cysteine-Rich Calcium-Binding Protein, in Developing Hair Follicle

40 citations , November 1998 in “The journal of investigative dermatology/Journal of investigative dermatology”

This study found that the S100A3 gene is exclusively expressed in hair follicle cells differentiating into hair shaft components in mice, suggesting its important role in hair formation.

research Molecular Cloning of Two Novel Types of Peptidylarginine Deiminase cDNAs from Retinoic Acid-Treated Culture of a Newborn Rat Keratinocyte Cell Line

39 citations , August 1998 in “FEBS Letters”

In this study, researchers identified two novel peptidylarginine deiminases from treated rat keratinocytes, both showing enzyme activity with PAD‐R11 reflecting a characteristic of epidermal enzymes.

research The Fate of Trichohyalin

135 citations , October 1997 in “Journal of biological chemistry/The Journal of biological chemistry”

This study suggests that trichohyalin is modified by peptidyl-arginine deiminase before being cross-linked by TGase 3, allowing the formation of rigid structures in hair follicle cells.

research Isolation and Molecular Cloning of Epidermal and Hair Follicle-Specific Peptidylarginine Deiminase Type III from Rat

42 citations , May 1997 in “The Journal of Biochemistry”

In this study, researchers purified and cloned rat peptidylarginine deiminase type III, demonstrating its activity and specific expression in the epidermis and hair follicles.

research Expression of Keratin K14 in the Epidermis and Hair Follicle: Insights Into Complex Programs of Differentiation

198 citations , November 1989 in “The Journal of Cell Biology”

This study reported that K14 expression patterns and keratin filament organization in human skin's hair follicles differ from those in the epidermis, indicating distinct differentiation programs.

research The Enzymic Derivation of Citrulline Residues from Arginine Residues In Situ During the Biosynthesis of Hair Proteins Cross-Linked by Isopeptide Bonds

45 citations , January 1977 in “Advances in experimental medicine and biology”

Hair follicles have an enzyme that converts arginine to citrulline in proteins.