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GlossaryPeptidylarginine Deiminase

enzyme converting arginine in proteins to citrulline

Peptidylarginine Deiminase (PAD) is an enzyme that converts arginine residues in proteins into citrulline through a process called deimination or citrullination. This modification can affect protein function and is involved in various physiological processes, including the regulation of gene expression and the formation of hair. Dysregulation of PAD activity has been linked to autoimmune diseases and conditions like alopecia.

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

124 citations , November 2000 in “The journal of investigative dermatology/Journal of investigative dermatology”

PAD3 plays a key role in hair and skin protein structure and may be linked to skin diseases.

research Peptidylarginine Deiminase Isoforms Are Differentially Expressed in Anagen Hair Follicles and Other Human Skin Appendages

71 citations , June 2005 in “Journal of Investigative Dermatology”

PAD enzymes play a key role in hair growth and structure.

research Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases

57 citations , January 2020 in “International Journal of Molecular Sciences”

PADs are crucial for healthy skin and hair, and their imbalance can cause skin and hair disorders.

research Immunocytochemical Localization of Peptidylarginine Deiminase Type III, Trichohyalin, and Deiminated Trichohyalin in Infant Rat Dorsal Skin Hair Follicle

2 citations , January 2001 in “Biomedical Research”

Trichohyalin and peptidylarginine deiminase type III are found together in rat hair follicles, with trichohyalin being modified after expression.

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”

Two new enzymes, PAD-R11 and PAD-R4, were cloned and showed activity, with PAD-R11 resembling epidermal enzymes.

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