The Fate of Trichohyalin

    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.
    Trichohyalin (THH) was identified as a major structural protein in hair follicle cells, undergoing postsynthetic modifications by Ca<sup>2+</sup>-dependent enzymes, transglutaminases (TGases), and peptidyl-arginine deiminase. The study explored the processing of a truncated, more soluble form of THH (THH-8) in vitro, finding that TGase 3 had the highest kinetic efficiency for cross-linking THH-8. The data suggested an in vivo model where THH is first denatured by peptidyl-arginine deiminase, making it more soluble and available for efficient cross-linking by TGase 3, forming rigid structures in hair follicle cells. This sequence was supported by the expression timing of THH and TGase 3 in hair follicle cells.
    Discuss this study in the Community →

    Cited in this study

    6 / 6 results