The Fate of Trichohyalin

    October 1997 in “ Journal of biological chemistry/˜The œJournal of biological chemistry ”
    Edit Tarcsa, Lyuben N. Marekov, Jeanne M. Andreoli, William W. Idler, Eleonora Candi, Soo‐Il Chung, Peter M. Steinert
    TLDR Trichohyalin is modified by enzymes to form strong structures in hair cells.
    The study on "The Fate of Trichohyalin" investigated the post-translational modifications of trichohyalin (THH) in hair follicles, focusing on its cross-linking by transglutaminase 3 (TGase 3) and the effects of peptidyl-arginine deiminase (PAD) modification. Researchers found that PAD modification increased the solubility of THH, making it a better substrate for TGase 3, which then efficiently cross-linked THH to form rigid structures essential for the structural integrity of hair follicles. Immunofluorescence studies confirmed the co-expression of TGase 3 and THH in the inner root sheath and medulla, highlighting TGase 3's primary role in this process.
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