Importance of Citrullination on Hair Protein Molecular Assembly During Trichocytic Differentiation

摘要: In mammalian hair follicles, Ca2+-dependent peptidylarginine deiminases catalyze the conversion of arginines into citrullines in S100A3, a cysteine-rich member S100 protein family, and trichohyalin, fused-type family. These irreversible posttranslational modifications were first described inner root sheath medulla, later, cuticles. medullary cells, arginine residues repetitive peptide domains trichohyalin are converted to peptidylcitrullines. Consequently, α-helix rich structures unfolded due decreased intramolecular ionic interaction. Citrullinated which is susceptible further introduction isopeptide bonds, cross-linked keratin intermediate filaments, cornified envelope, or itself sheath. Interconnected predominantly deposited amorphous vacuoles mature medulla. cuticular hair-dominant-type deiminase specifically converts symmetric pair Arg51 on S100A3 dimer citrulline pair. The citrullinated assembles as homotetramer presence Ca2+ Zn2+. This trichocytic pathway likely be associated with homeostatic Zn2+ regulation during maturation. chapter summarizes previous reports pioneering research updated our current view deimination follicle.