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  • Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue.

Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue.

Cells (2022-06-25)
Kinga Skieresz-Szewczyk, Hanna Jackowiak, Marek Skrzypski
ABSTRACT

The lingual mucosa in birds is covered with two specific types of multilayered epithelia, i.e., the para- and orthokeratinized epithelium, that differ structurally and functionally. Comprehensive information on proteins synthesized in keratinocyte during their cytodifferentiation in subsequent layers of multilayered epithelia in birds concerns only the epidermis and are missing the epithelia of the lingual mucosa. The aim of the present study was to perform an immunohistochemical (IHC) and molecular analysis (WB) of bird-specific alpha-keratin, keratin-associated proteins (KAPs), namely filaggrin and loricrin, as well as transglutaminase 1 in the para- and orthokeratinized epithelium covering the tongue in the domestic duck, goose, and turkey. The results reveal the presence of alpha-keratin and KAPs in both epithelia, which is a sign of the cornification process. In contrast to the epidermis, the main KAPs involved in the cornification process of the lingual epithelia in birds is loricrin. Stronger expression with KAPs and transglutaminase 1 in the orthokeratinized epithelium than in the parakeratinized epithelium may determine the formation of a more efficient protective mechanical barrier. The presence of alpha-keratin, KAPs, and transglutaminase 1 epitopes characteristic of epidermal cornification in both types of the lingual epithelia may prove that they are of ectodermal origin.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Cytokeratin AE1/AE3 Antibody, recognizes acidic & basic cytokeratins, clone AE1/AE3, clone AE1/AE3, Chemicon®, from mouse