Ultrastructural Visualization of Cross-Linked Protein Features in Epidermal Appendages
July 1994
in “
Journal of Cell Science
”
New to Keratin? There is a guide in the encyclopedia. Read the guide → Studysummary This study found that the extraction-resistant structures in hair, feathers, and hagfish teeth are due to ε-(γ-glutamyl)lysine cross-linked proteins, emphasizing their role in maintaining the integrity of these materials.
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The study investigated the structural integrity of mammalian hair, bird feathers, and hagfish horny teeth after extraction with ionic detergent under reducing conditions. Despite the removal of solubilizable components like disulfide-bonded keratins, the structures remained largely intact due to ε-(γ-glutamyl)lysine cross-linked proteins. In hair, cell envelopes and intracellular deposits were preserved, while feathers retained barb structures but not the rachis. Hagfish teeth maintained visible cellular organization. The study identified four types of cross-linked features, highlighting the role of transglutaminases and substrate proteins in maintaining the function of epidermal appendages. These findings suggested potential diagnostic applications for assessing structural perturbations in these tissues.
