The Fate of Trichohyalin

October 1997 in “ Journal of biological chemistry/The Journal of biological chemistry ”

Edit Tarcsa, Lyuben N. Marekov, Jeanne M. Andreoli, William W. Idler, Eleonora Candi, Soo‐Il Chung, Peter M. Steinert

trichohyalin hair follicle cells Ca-dependent enzymes transglutaminases TGases peptidyl-arginine deiminase TGase 3 cross-linking denatured kinetic efficiency calcium-dependent enzymes TGase PAD cross-linking

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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