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Transglutaminase Activity Is Conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds
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...
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Published in: | International journal of molecular sciences 2023-01, Vol.24 (3), p.2193 |
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description | 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. |
doi_str_mv | 10.3390/ijms24032193 |
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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.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms24032193</identifier><identifier>PMID: 36768511</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Animals ; Appendages ; Catalysis ; Chickens ; cornification ; Crosslinking ; Disulfide bonds ; Embryogenesis ; Enzymes ; Epidermis ; Epithelium ; Esophagus ; Exocrine glands ; Feathers ; filiform papillae ; Fluorescence ; Follicles ; Glutamine ; Human tissues ; Humans ; Integument ; Investigations ; Keratinocytes ; Labeling ; Localization ; Lysine ; Mammals ; nail ; Papillae ; Poultry ; Proteins ; Sheaths ; Skin ; Structural proteins ; Sweat gland ; Tongue ; transglutaminase ; Transglutaminases</subject><ispartof>International journal of molecular sciences, 2023-01, Vol.24 (3), p.2193</ispartof><rights>2023 by the authors. 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/). 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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.</description><subject>Animals</subject><subject>Appendages</subject><subject>Catalysis</subject><subject>Chickens</subject><subject>cornification</subject><subject>Crosslinking</subject><subject>Disulfide bonds</subject><subject>Embryogenesis</subject><subject>Enzymes</subject><subject>Epidermis</subject><subject>Epithelium</subject><subject>Esophagus</subject><subject>Exocrine glands</subject><subject>Feathers</subject><subject>filiform papillae</subject><subject>Fluorescence</subject><subject>Follicles</subject><subject>Glutamine</subject><subject>Human tissues</subject><subject>Humans</subject><subject>Integument</subject><subject>Investigations</subject><subject>Keratinocytes</subject><subject>Labeling</subject><subject>Localization</subject><subject>Lysine</subject><subject>Mammals</subject><subject>nail</subject><subject>Papillae</subject><subject>Poultry</subject><subject>Proteins</subject><subject>Sheaths</subject><subject>Skin</subject><subject>Structural proteins</subject><subject>Sweat gland</subject><subject>Tongue</subject><subject>transglutaminase</subject><subject>Transglutaminases</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdkktv1DAURiMEoqWwY40isWHBgB_xa4M0jAqMVMSis7euHTv1kDjBTkbqv8ftlGrKyvb9jo7s61tVbzH6RKlCn8N-yKRBlGBFn1XnuCFkhRAXz0_2Z9WrnPcIEUqYelmdUS64ZBifV90uQcxdv8wwhAjZ1Ws7h0OYb-ttrjdjzC4dXFuHWF_PCebgQzldTmG-cX2AGmJbX_8u6XqaXGyhc7keff0ThgH6fB9_DanNr6sXvhTcm4f1otp9u9xtfqyufn3fbtZXK9sIOa-EsI4oA8wTB5JiYa0AoAQ1Rkjg2HuhhLTYGN4wxhXxyCjBTUksUoxeVNujth1hr6cUBki3eoSg7wtj6jSkOdjeaamgkQiIp4Y21ChjUBFKSkvXmKK-uL4cXdNiBtdaF0sD-ifSp0kMN7obD1opzGVDiuDDgyCNfxaXZz2EbF3fQ3TjkjURgnHMEJEFff8fuh-XFEun7qhGYcw4KtTHI2XTmHNy_vEyGOm7YdCnw1Dwd6cPeIT__T79CyITr80</recordid><startdate>20230122</startdate><enddate>20230122</enddate><creator>Sachslehner, Attila Placido</creator><creator>Surbek, Marta</creator><creator>Golabi, Bahar</creator><creator>Geiselhofer, Miriam</creator><creator>Jäger, Karin</creator><creator>Hess, Claudia</creator><creator>Kuchler, Ulrike</creator><creator>Gruber, Reinhard</creator><creator>Eckhart, Leopold</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-5645-2036</orcidid><orcidid>https://orcid.org/0000-0003-1447-9254</orcidid><orcidid>https://orcid.org/0000-0002-3535-5157</orcidid></search><sort><creationdate>20230122</creationdate><title>Transglutaminase Activity Is Conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds</title><author>Sachslehner, Attila Placido ; 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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.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>36768511</pmid><doi>10.3390/ijms24032193</doi><orcidid>https://orcid.org/0000-0002-5645-2036</orcidid><orcidid>https://orcid.org/0000-0003-1447-9254</orcidid><orcidid>https://orcid.org/0000-0002-3535-5157</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Animals Appendages Catalysis Chickens cornification Crosslinking Disulfide bonds Embryogenesis Enzymes Epidermis Epithelium Esophagus Exocrine glands Feathers filiform papillae Fluorescence Follicles Glutamine Human tissues Humans Integument Investigations Keratinocytes Labeling Localization Lysine Mammals nail Papillae Poultry Proteins Sheaths Skin Structural proteins Sweat gland Tongue transglutaminase Transglutaminases |
title | Transglutaminase Activity Is Conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds |
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