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

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 layer...

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Autores principales: Skieresz-Szewczyk, Kinga, Jackowiak, Hanna, Skrzypski, Marek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9221158/
https://www.ncbi.nlm.nih.gov/pubmed/35741029
http://dx.doi.org/10.3390/cells11121899
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author Skieresz-Szewczyk, Kinga
Jackowiak, Hanna
Skrzypski, Marek
author_facet Skieresz-Szewczyk, Kinga
Jackowiak, Hanna
Skrzypski, Marek
author_sort Skieresz-Szewczyk, Kinga
collection PubMed
description 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.
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spelling pubmed-92211582022-06-24 Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue Skieresz-Szewczyk, Kinga Jackowiak, Hanna Skrzypski, Marek Cells Article 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. MDPI 2022-06-11 /pmc/articles/PMC9221158/ /pubmed/35741029 http://dx.doi.org/10.3390/cells11121899 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Skieresz-Szewczyk, Kinga
Jackowiak, Hanna
Skrzypski, Marek
Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue
title Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue
title_full Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue
title_fullStr Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue
title_full_unstemmed Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue
title_short Alpha-Keratin, Keratin-Associated Proteins and Transglutaminase 1 Are Present in the Ortho- and Parakeratinized Epithelium of the Avian Tongue
title_sort alpha-keratin, keratin-associated proteins and transglutaminase 1 are present in the ortho- and parakeratinized epithelium of the avian tongue
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9221158/
https://www.ncbi.nlm.nih.gov/pubmed/35741029
http://dx.doi.org/10.3390/cells11121899
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