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Ultrastructural visualization of cross-linked protein features in epidermal appendages
R H Rice1, V J Wong, K E Pinkerton
1Department of Environmental Toxicology, University of California, Davis 95616.
Journal of Cell Science
|July 1, 1994
Summary
This study reveals that epsilon-(gamma-glutamyl)lysine cross-linked proteins form the structural basis of mammalian hair, bird feathers, and hagfish teeth after detergent extraction. These findings highlight the role of transglutaminases in epidermal appendage structure.
Area of Science:
- Biochemistry
- Structural Biology
- Dermatology
Background:
- Mammalian hair, bird feathers, and hagfish teeth are complex epidermal appendages.
- Their structural integrity relies on specific protein cross-linking mechanisms.
Purpose of the Study:
- To investigate the residual protein structures in hair, feather, and hagfish teeth after rigorous extraction.
- To identify the types and locations of epsilon-(gamma-glutamyl)lysine cross-linked proteins.
Main Methods:
- Extraction of mammalian hair, bird feather, and hagfish teeth using ionic detergent under reducing conditions.
- Microscopic analysis of the remaining protein structures.
Main Results:
- Extraction removed solubilizable proteins, leaving a residue of epsilon-(gamma-glutamyl)lysine cross-linked protein.
- Residual structures included cell envelopes, intracellular deposits, and remnant nuclei, preserving macroscopic features.
- Four types of cross-linked features were identified based on their location (sub-membrane, intercellular, cytoplasmic, nuclear).
Conclusions:
- Epsilon-(gamma-glutamyl)lysine cross-linked proteins are crucial for the structural integrity of epidermal appendages.
- Transglutaminases and their substrates play a vital role in forming these structures.
- The findings may inform diagnostic tests for epidermal appendage disorders.