Title (eng)

Transglutaminase Activity is conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds

Author

Attila Placido Sachslehner   Medical University of Vienna

Leopold Eckhart   Medical University of Vienna

Reinhard Gruber   Medical University of Vienna

Ulrike Kuchler   Medical University of Vienna

Claudia Hess   University of Veterinary Medicine, Vienna

Karin Jäger   Medical University of Vienna

Miriam Geiselhofer   Medical University of Vienna

Bahar Golabi   Medical University of Vienna

Marta Surbek   Medical University of Vienna

Publishing

MDPI

Description (eng)

The cross-linking of structural proteins is critical for establishing the mechanical stability of the epithelial compartments of the skin and skin appendages. The introduction of isopeptide bonds between glutamine and lysine residues depends on catalysis by transglutaminases and represents the main protein cross-linking mechanism besides the formation of disulfide bonds. Here, we used a fluorescent labeling protocol to localize the activity of transglutaminases on thin sections of the integument and its appendages in mammals and birds. In human tissues, transglutaminase activity was detected in the granular layer of the epidermis, suprabasal layers of the gingival epithelium, the duct of sweat glands, hair follicles and the nail matrix. In the skin appendages of chickens, transglutaminase activity was present in the claw matrix, the feather follicle sheath, the feather sheath and in differentiating keratinocytes of feather barb ridges. During chicken embryogenesis, active transglutaminase was found in the cornifying epidermis, the periderm and the subperiderm. Transglutaminase activity was also detected in the filiform papillae on the tongue of mice and in conical papillae on the tongue of chickens. In summary, our study reveals that transglutaminase activities are widely distributed in integumentary structures and suggests that transglutamination contributes to the cornification of hard skin appendages such as nails and feathers.

Object languages

English

Date

2023

Rights

This work is licensed under a
CC BY 4.0 - Creative Commons Attribution 4.0 International License.

CC BY 4.0 International

http://creativecommons.org/licenses/by/4.0/

Classification

Evolutionary Origin; Cell-Death; In-Vitro; Proteins; Hair; Differentiation; Keratinocytes; Localization; Expression; Mutations

Member of the Collection(s) (1)