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Article ; Online: Development-Associated Genes of the Epidermal Differentiation Complex (EDC).

Holthaus, Karin Brigit / Eckhart, Leopold

2024 Volume 12, Issue 1

Abstract: The epidermal differentiation complex (EDC) is a cluster of genes that encode protein components of the outermost layers of the epidermis in mammals, reptiles and birds. The development of the stratified epidermis from a single-layered ectoderm involves ... ...

Abstract	The epidermal differentiation complex (EDC) is a cluster of genes that encode protein components of the outermost layers of the epidermis in mammals, reptiles and birds. The development of the stratified epidermis from a single-layered ectoderm involves an embryo-specific superficial cell layer, the periderm. An additional layer, the subperiderm, develops in crocodilians and over scutate scales of birds. Here, we review the expression of EDC genes during embryonic development. Several EDC genes are expressed predominantly or exclusively in embryo-specific cell layers, whereas others are confined to the epidermal layers that are maintained in postnatal skin. The S100 fused-type proteins scaffoldin and trichohyalin are expressed in the avian and mammalian periderm, respectively. Scaffoldin forms the so-called periderm granules, which are histological markers of the periderm in birds. Epidermal differentiation cysteine-rich protein (EDCRP) and epidermal differentiation protein containing DPCC motifs (EDDM) are expressed in the avian subperiderm where they are supposed to undergo cross-linking via disulfide bonds. Furthermore, a histidine-rich epidermal differentiation protein and feather-type corneous beta-proteins, also known as beta-keratins, are expressed in the subperiderm. The accumulating evidence for roles of EDC genes in the development of the epidermis has implications on the evolutionary diversification of the skin in amniotes.
Language	English
Publishing date	2024-01-15
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2720870-9
ISSN	2221-3759 ; 2221-3759
ISSN (online)	2221-3759
ISSN	2221-3759
DOI	10.3390/jdb12010004
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Article ; Online: Editorial: Gasdermins in the defense against pathogens.

Eckhart, Leopold / Chen, Ruochan

Frontiers in immunology

2023 Volume 14, Page(s) 1238368

MeSH term(s)	Gasdermins ; Caspases/metabolism ; Inflammasomes/metabolism
Chemical Substances	Gasdermins ; Caspases (EC 3.4.22.-) ; Inflammasomes
Language	English
Publishing date	2023-06-20
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1238368
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Article: Differential Loss of OAS Genes Indicates Diversification of Antiviral Immunity in Mammals.

Eckhart, Leopold / Sipos, Wolfgang

Vaccines

2023 Volume 11, Issue 2

Abstract: One of the main mechanisms of inducing an antiviral response depends on 2'-5'-oligoadenylate synthetases (OAS), which sense double-stranded RNA in the cytoplasm and activate RNase L. Mutations leading to the loss of ... ...

Abstract	One of the main mechanisms of inducing an antiviral response depends on 2'-5'-oligoadenylate synthetases (OAS), which sense double-stranded RNA in the cytoplasm and activate RNase L. Mutations leading to the loss of functional
Language	English
Publishing date	2023-02-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines11020419
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Article ; Online: Evolutionary diversification of epidermal barrier genes in amphibians.

Sachslehner, Attila Placido / Eckhart, Leopold

Scientific reports

2022 Volume 12, Issue 1, Page(s) 13634

Abstract: The epidermal differentiation complex (EDC) is a cluster of genes encoding components of the skin barrier in terrestrial vertebrates. EDC genes can be categorized as S100 fused-type protein (SFTP) genes such as filaggrin, which contain two coding exons, ... ...

Abstract	The epidermal differentiation complex (EDC) is a cluster of genes encoding components of the skin barrier in terrestrial vertebrates. EDC genes can be categorized as S100 fused-type protein (SFTP) genes such as filaggrin, which contain two coding exons, and single-coding-exon EDC (SEDC) genes such as loricrin. SFTPs are known to be present in amniotes (mammals, reptiles and birds) and amphibians, whereas SEDCs have not yet been reported in amphibians. Here, we show that caecilians (Amphibia: Gymnophiona) have both SFTP and SEDC genes. Two to four SEDC genes were identified in the genomes of Rhinatrema bivittatum, Microcaecilia unicolor and Geotrypetes seraphini. Comparative analysis of tissue transcriptomes indicated predominant expression of SEDC genes in the skin of caecilians. The proteins encoded by caecilian SEDC genes resemble human SEDC proteins, such as involucrin and small proline-rich proteins, with regard to low sequence complexity and high contents of proline, glutamine and lysine. Our data reveal diversification of EDC genes in amphibians and suggest that SEDC-type skin barrier genes have originated either in a common ancestor of tetrapods followed by loss in Batrachia (frogs and salamanders) or, by convergent evolution, in caecilians and amniotes.
MeSH term(s)	Amphibians/genetics ; Animals ; Epidermis ; Humans ; Mammals ; Phylogeny ; Proline/genetics ; Reptiles/genetics ; S100 Proteins/genetics
Chemical Substances	S100 Proteins ; Proline (9DLQ4CIU6V)
Language	English
Publishing date	2022-08-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-18053-7
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Article ; Online: Comparative genomics of monotremes provides insights into the early evolution of mammalian epidermal differentiation genes.

Steinbinder, Julia / Sachslehner, Attila Placido / Holthaus, Karin Brigit / Eckhart, Leopold

Scientific reports

2024 Volume 14, Issue 1, Page(s) 1437

Abstract: The function of the skin as a barrier against the environment depends on the differentiation of epidermal keratinocytes into highly resilient corneocytes that form the outermost skin layer. Many genes encoding structural components of corneocytes are ... ...

Abstract	The function of the skin as a barrier against the environment depends on the differentiation of epidermal keratinocytes into highly resilient corneocytes that form the outermost skin layer. Many genes encoding structural components of corneocytes are clustered in the epidermal differentiation complex (EDC), which has been described in placental and marsupial mammals as well as non-mammalian tetrapods. Here, we analyzed the genomes of the platypus (Ornithorhynchus anatinus) and the echidna (Tachyglossus aculeatus) to determine the gene composition of the EDC in the basal clade of mammals, the monotremes. We report that mammal-specific subfamilies of EDC genes encoding small proline-rich proteins (SPRRs) and late cornified envelope proteins as well as single-copy EDC genes such as involucrin are conserved in monotremes, suggesting that they have originated in stem mammals. Monotremes have at least one gene homologous to the group of filaggrin (FLG), FLG2 and hornerin (HRNR) in placental mammals, but no clear one-to-one pairwise ortholog of either FLG, FLG2 or HRNR. Caspase-14, a keratinocyte differentiation-associated protease implicated in the processing of filaggrin, is encoded by at least 3 gene copies in the echidna. Our results reveal evolutionarily conserved and clade-specific features of the genetic regulation of epidermal differentiation in monotremes.
MeSH term(s)	Pregnancy ; Animals ; Female ; Tachyglossidae/physiology ; Filaggrin Proteins ; Placenta ; Monotremata ; Platypus/genetics ; Mammals/genetics ; Genomics
Chemical Substances	Filaggrin Proteins
Language	English
Publishing date	2024-01-16
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-51926-7
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Article ; Online: Comparative genomics of sirenians reveals evolution of filaggrin and caspase-14 upon adaptation of the epidermis to aquatic life.

Steinbinder, Julia / Sachslehner, Attila Placido / Holthaus, Karin Brigit / Eckhart, Leopold

Scientific reports

2024 Volume 14, Issue 1, Page(s) 9278

Abstract: The mammalian epidermis has evolved to protect the body in a dry environment. Genes of the epidermal differentiation complex (EDC), such as FLG (filaggrin), are implicated in the barrier function of the epidermis. Here, we investigated the molecular ... ...

Abstract	The mammalian epidermis has evolved to protect the body in a dry environment. Genes of the epidermal differentiation complex (EDC), such as FLG (filaggrin), are implicated in the barrier function of the epidermis. Here, we investigated the molecular evolution of the EDC in sirenians (manatees and dugong), which have adapted to fully aquatic life, in comparison to the EDC of terrestrial mammals and aquatic mammals of the clade Cetacea (whales and dolphins). We show that the main subtypes of EDC genes are conserved or even duplicated, like late cornified envelope (LCE) genes of the dugong, whereas specific EDC genes have undergone inactivating mutations in sirenians. FLG contains premature stop codons in the dugong, and the ortholog of human CASP14 (caspase-14), which proteolytically processes filaggrin, is pseudogenized in the same species. As FLG and CASP14 have also been lost in whales, these mutations represent convergent evolution of skin barrier genes in different lineages of aquatic mammals. In contrast to the dugong, the manatee has retained functional FLG and CASP14 genes. FLG2 (filaggrin 2) is truncated in both species of sirenians investigated. We conclude that the land-to-water transition of sirenians was associated with modifications of the epidermal barrier at the molecular level.
MeSH term(s)	Filaggrin Proteins ; Intermediate Filament Proteins/genetics ; Intermediate Filament Proteins/metabolism ; Animals ; Epidermis/metabolism ; Evolution, Molecular ; Genomics/methods ; Caspase 14/genetics ; Caspase 14/metabolism ; Humans ; Phylogeny ; Adaptation, Physiological/genetics
Chemical Substances	Filaggrin Proteins ; Intermediate Filament Proteins ; FLG protein, human ; Caspase 14 (EC 3.4.22.-)
Language	English
Publishing date	2024-04-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comparative Study
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-60099-2
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Article ; Online: Comparative immunohistochemical analysis suggests a conserved role of EPS8L1 in epidermal and hair follicle barriers of mammals.

Alibardi, Lorenzo / Surbek, Marta / Eckhart, Leopold

Protoplasma

2023 Volume 261, Issue 2, Page(s) 333–349

Abstract: The mammalian skin and its appendages depend on tightly coordinated differentiation of epithelial cells. Epidermal growth factor receptor (EGFR) pathway substrate 8 (EPS8) like 1 (EPS8L1) is enriched in the epidermis among human tissues and has also been ...

Abstract	The mammalian skin and its appendages depend on tightly coordinated differentiation of epithelial cells. Epidermal growth factor receptor (EGFR) pathway substrate 8 (EPS8) like 1 (EPS8L1) is enriched in the epidermis among human tissues and has also been detected in the epidermis of lizards. Here, we show by the analysis of single-cell RNA-sequencing data that EPS8L1 mRNA is co-expressed with filaggrin and loricrin in terminally differentiated human epidermal keratinocytes. Comparative genomics indicated that EPS8L1 is conserved in all main clades of mammals, whereas the orthologous gene has been lost in birds. Using a polyclonal antibody against EPS8L1, we performed an immunohistochemical screening of skin from diverse mammalian species and immuno-electron microscopy of human skin. EPS8L1 was detected predominantly in the granular layer of the epidermis in monotremes, marsupial, and placental mammals. The labeling was partly associated with cell membranes, and it was evident along the perimeter of keratinocytes at the transition with the cornified layer of the epidermis, similar to involucrin distribution. Basal, spinous, and the fully mature cornified layers lacked immunolabeling of EPS8L1. In addition to the epidermis, the hair follicle inner root sheath (IRS) was immunolabeled. Both epidermal granular layer and IRS contribute to the barrier function of the skin, suggesting that EPS8L1 is involved in the regulation of these barriers.
MeSH term(s)	Pregnancy ; Animals ; Female ; Humans ; Hair Follicle/metabolism ; Placenta/metabolism ; Epidermis/metabolism ; Mammals/metabolism ; Keratinocytes/metabolism ; Cell Differentiation ; Adaptor Proteins, Signal Transducing/metabolism
Chemical Substances	EPS8 protein, human ; Adaptor Proteins, Signal Transducing
Language	English
Publishing date	2023-10-27
Publishing country	Austria
Document type	Journal Article
ZDB-ID	123809-7
ISSN	1615-6102 ; 0033-183X
ISSN (online)	1615-6102
ISSN	0033-183X
DOI	10.1007/s00709-023-01898-8
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Article: Iron Metabolism of the Skin: Recycling versus Release.

Surbek, Marta / Sukseree, Supawadee / Eckhart, Leopold

Metabolites

2023 Volume 13, Issue 9

Abstract: The skin protects the body against exogenous stressors. Its function is partially achieved by the permanent regeneration of the epidermis, which requires high metabolic activity and the shedding of superficial cells, leading to the loss of metabolites. ... ...

Abstract	The skin protects the body against exogenous stressors. Its function is partially achieved by the permanent regeneration of the epidermis, which requires high metabolic activity and the shedding of superficial cells, leading to the loss of metabolites. Iron is involved in a plethora of important epidermal processes, including cellular respiration and detoxification of xenobiotics. Likewise, microorganisms on the surface of the skin depend on iron, which is supplied by the turnover of epithelial cells. Here, we review the metabolism of iron in the skin with a particular focus on the fate of iron in epidermal keratinocytes. The iron metabolism of the epidermis is controlled by genes that are differentially expressed in the inner and outer layers of the epidermis, establishing a system that supports the recycling of iron and counteracts the release of iron from the skin surface. Heme oxygenase-1 (HMOX1), ferroportin (SLC40A1) and hephaestin-like 1 (HEPHL1) are constitutively expressed in terminally differentiated keratinocytes and allow the recycling of iron from heme prior to the cornification of keratinocytes. We discuss the evidence for changes in the epidermal iron metabolism in diseases and explore promising topics of future studies of iron-dependent processes in the skin.
Language	English
Publishing date	2023-09-12
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2662251-8
ISSN	2218-1989
ISSN	2218-1989
DOI	10.3390/metabo13091005
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Article ; Online: Immunolocalization of epidermal differentiation complex proteins reveals distinct molecular compositions of cells that control structure and mechanical properties of avian skin appendages.

Alibardi, Lorenzo / Eckhart, Leopold

Journal of morphology

2021 Volume 282, Issue 6, Page(s) 917–933

Abstract: The epidermal differentiation complex (EDC) is a cluster of genes that encode structural proteins of skin derivatives with variable mechanical performances, from the scales of reptiles and birds to the hard claws and beaks, and to the flexible but ... ...

Abstract	The epidermal differentiation complex (EDC) is a cluster of genes that encode structural proteins of skin derivatives with variable mechanical performances, from the scales of reptiles and birds to the hard claws and beaks, and to the flexible but resistant corneous material of feathers. Corneous proteins with or without extended beta-regions are produced from avian genomes, and include the largely prevalent corneous beta proteins (CβPs, formerly indicated as beta-keratins), and minor contribution from histidine-rich proteins, trichohyalin-like proteins (scaffoldin), loricrin, and other proteins rich in cysteine or other types of amino acids. The light-microscopic and ultrastructural immunolocalization of major and minor EDC-proteins in avian skin (feather CβPs, EDKM, EDWM, EDMTFH, EDDM, and scaffoldin) suggests that each specific appendage consists of a particular mix of these proteins in addition to the main proteins containing a peculiar beta-region of 34 amino acids, indicated as feather/scale/claw/beak CβPs (fCβPs, sCβPs, cCβPs, bCβPs). This indicates that numerous proteins of the EDC are added to the variable meshwork of intermediate filament keratins to produce avian epidermis with different mechanical and functional properties. Although the specific roles for these proteins are not known they likely make an important contribution to the final material properties of the different skin appendages of birds. The highest number of sauropsid CβPs is found in birds, suggesting a relation to the evolution of feathers, and additional epidermal differentiation proteins have contributed to the evolutionary adaptations of avian skin.
MeSH term(s)	Animals ; Birds ; Cell Differentiation ; Epidermis ; Feathers ; Keratins ; Reptiles ; beta-Keratins
Chemical Substances	beta-Keratins ; Keratins (68238-35-7)
Language	English
Publishing date	2021-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3084-3
ISSN	1097-4687 ; 0022-2887 ; 0362-2525
ISSN (online)	1097-4687
ISSN	0022-2887 ; 0362-2525
DOI	10.1002/jmor.21357
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Article ; Online: Comparative genomics reveals evolutionary loss of epiplakin in cetaceans.

Fuchs, Peter / Drexler, Corinne / Ratajczyk, Sonia / Eckhart, Leopold

Scientific reports

2022 Volume 12, Issue 1, Page(s) 1112

Abstract: The adaptation of vertebrates to different environments was associated with changes in the molecular composition and regulation of epithelia. Whales and dolphins, together forming the clade cetaceans, have lost multiple epithelial keratins during or ... ...

Abstract	The adaptation of vertebrates to different environments was associated with changes in the molecular composition and regulation of epithelia. Whales and dolphins, together forming the clade cetaceans, have lost multiple epithelial keratins during or after their evolutionary transition from life on land to life in water. It is unknown whether the changes in keratins were accompanied by gain or loss of cytoskeletal adapter proteins of the plakin family. Here we investigated whether plakin proteins are conserved in cetaceans and other vertebrates. Comparative analysis of genome sequences showed conservation of dystonin, microtubule actin crosslinking factor 1 (MACF1), plectin, desmoplakin, periplakin and envoplakin in cetaceans. By contrast, EPPK1 (epiplakin) was disrupted by inactivating mutations in all cetaceans investigated. Orthologs of EPPK1 are present in bony and cartilaginous fishes and tetrapods, indicating an evolutionary origin of EPPK1 in a common ancestor of jawed vertebrates (Gnathostomes). In many vertebrates, EPPK1 is flanked by an as-yet uncharacterized gene that encodes protein domains homologous to the carboxy-terminal segment of MACF1. We conclude that epiplakin, unlike other plakins, was lost in cetaceans.
MeSH term(s)	Animals ; Autoantigens/genetics ; Cetacea/genetics ; Datasets as Topic ; Evolution, Molecular ; Genomics ; Loss of Function Mutation
Chemical Substances	Autoantigens ; epiplakin
Language	English
Publishing date	2022-01-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-05087-0
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