The protein components ofliving cells in the hair follicle are amenable to study by standard molecular biological techniques, but identifying those in the hair shaft has been problematic until recently. Most of the protein, primarily keratins and keratin associated proteins, can be extracted under denaturing conditions, but 15-20% is intractable due to transglutaminase-mediated cross-linking. Shotgun proteomics now permits identifying >300 constituents of the isopeptide cross-linked proteome and even certain post-translational modifications. The proteins originate from all the intracellular compartments, indicating that the cross-linking process makes effective use of available resources to produce structures with great mechanical stability. Knowing this proteome provides a foundation for correlating defects in hair shaft structure with protein deficiencies. Such investigations can be extended to mouse models of aberrant pelage hair. Thus, inbred mouse strains can be distinguished by their hair proteomes, raising the possibility of similar variation in the human population. The nail plate is also amenable to this shotgun proteomic approach. Providing discrete and noninvasive sampling of the human proteome, these epidermal appendages could have diagnostic utility for certain disease states.
|Original language||English (US)|
|Number of pages||8|
|Journal||Journal of Cosmetic Science|
|State||Published - Mar 2011|
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