Keratinization of the esophageal epithelium of domesticated mammals

Meyer, Wilfried; Schoennagel, Britta; Kacza, Johannes; Busche, Roger; Hornickel, Isabelle Nina; Hewicker‐Trautwein, M.; Schnapper, Anke

doi:10.1016/j.acthis.2013.07.008

Cited by 11 publications

(9 citation statements)

References 25 publications

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“…The human and primate esophagi 34 are not keratinized, and therefore it is plausible that esophagus-specific proteases, such as CAPN14, are a means of protecting the integrity of esophageal tissue (Fig 2). This hypothesis is supported by correlative evidence that CAPN14 mRNA expression in pigs, a species with keratinized esophagus, 32 is virtually undetectable 7 and by evolution of cationic antimicrobial peptides, 35 particularly defensins, 36 that provide antifungal resistance of human esophageal surface. 37 CAPN14’s role in regulation of esophageal tissue barrier function can account for the fact that an imbalance in proteolytic function in the human esophagus caused by genetic 9 or environmental 38 factors can result in predisposition to tissue damage, particularly loss of esophageal tissue integrity.…”

Section: Gene Structure and Conservationmentioning

confidence: 88%

“…Because esophageal epithelium is prone to damage because of food consumption, there are various defense mechanisms against esophageal damage. One of these mechanisms is keratinization of esophageal epithelium, which increases its mechanical stability 32 ; for example, animals consuming a diet rich in grains and plants have a highly keratinized esophagus. Another protective mechanism includes higher expression of protective molecules, such as the cationic antimicrobial peptides cathelicidin and β-defensins 2 and 3, 33 which are characteristic of carnivorous animals that have a less keratinized esophagus.…”

Section: Gene Structure and Conservationmentioning

confidence: 99%

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Calpain-14 and its association with eosinophilic esophagitis

Litosh

Rochman

Rymer

et al. 2017

Journal of Allergy and Clinical Immunology

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Calpains are a family of intracellular, calcium-dependent cysteine proteases involved in a variety of regulatory processes, including cytoskeletal dynamics, cell-cycle progression, signal transduction, gene expression, and apoptosis. These enzymes have been implicated in a number of disease processes, notably for this review involving eosinophilic tissue inflammation, such as eosinophilic esophagitis (EoE), a chronic inflammatory disorder triggered by allergic hypersensitivity to food and associated with genetic variants in calpain 14 (CAPN14). Herein we review the genetic, structural, and biochemical properties of CAPN14 and its gene product CAPN14, and its emerging role in patients with EoE. The CAPN14 gene is localized at chromosome 2p23.1-p21 and is most homologous to CAPN13 (36% sequence identity), which is located 365 kb downstream of CAPN14. Structurally, CAPN14 has classical calpain motifs, including a cysteine protease core. In comparison with other human calpains, CAPN14 has a unique expression pattern, with the highest levels in the upper gastrointestinal tract, particularly in the squamous epithelium of the esophagus. The CAPN14 gene is positioned in an epigenetic hotspot regulated by IL-13, a TH2 cytokine with increased levels in patients with EoE that has been shown to be a mediator of the disease. CAPN14 induces disruptive effects on the esophageal epithelium by impairing epithelial barrier function in association with loss of desmoglein-1 expression and has a regulatory role in repairing epithelial changes induced by IL-13. Thus CAPN14 is a unique protease with distinct tissue-specific expression and function in patients with EoE and is a potential therapeutic target for EoE and related eosinophilic and allergic diseases.

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Section: Gene Structure and Conservationmentioning

confidence: 88%

Section: Gene Structure and Conservationmentioning

confidence: 99%

Calpain-14 and its association with eosinophilic esophagitis

Litosh

Rochman

Rymer

et al. 2017

Journal of Allergy and Clinical Immunology

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“…The epithelium on the ventral surface of the lingual apex is characterized with thick corneous layer called lingual nail covering alphalayer and could be compared to the dorsal surface of the claws in birds and reptiles. The cytokeratins are characterized by different mechanical and nonmechanical functions (Paladini et al, 1996;Moll et al, 2008;Bragulla and Homberger, 2009;Meyer et al, 2014). Taking into account that cytokeratin clone AE1/3, detecting alpha-keratin in birds, identifies a wide spectrum of cytokeratins, including basic keratins CK 1-8 and acidic keratins CK 10, 13, 14, 15, 16, and 19, we can state that the presence of alphakeratin in the basal and intermediate layers of the epithelium on the ventral surface of the lingual apex is responsible for the formation of a stable cytoskeleton providing an adequate connection between neighboring cells and with the basal membrane.…”

Section: Alpha-and Beta-keratin In the Tongue Epitheliummentioning

confidence: 99%

Localization of Alpha‐Keratin and Beta‐Keratin (Corneous Beta Protein) in the Epithelium on the Ventral Surface of the Lingual Apex and Its Lingual Nail in the Domestic Goose (Anser Anser f. domestica) by Using Immunohistochemistry and Raman Microspectroscopy Analysis

Skieresz‐Szewczyk

Jackowiak

Buchwald

et al. 2017

The Anatomical Record

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The epithelium of the ventral surface of the apex of the tongue in most birds is specified by the presence of the special superficial layer called lingual nail. The aim of the present study is to determine the localization of the alpha-keratin and beta-keratin (corneous beta protein) in this special epithelium in the domestic goose by using immunohistochemistry staining and the Raman spectroscopy analysis. Due to lack of commercially available antibodies to detect beta-keratin (corneous beta protein), the Raman spectroscopy was used as a specific tool to detect and describe the secondary structure of proteins. The immunohistochemical (IHC) detections reveal the presence of alpha-keratin in all layers of the epithelium, but significant differences in the distribution of the alpha-keratin in the epithelial layers appear. The staining reaction is stronger from the basal layer to the upper zone of the intermediate layer. The unique result is weak staining for the alpha-keratin in the lingual nail. Applications of the Raman spectroscopy as a complementary method not only confirmed results of IHC staining for alpha-keratin, but showed that this technique could be used to demonstrate the presence of beta-keratin (corneous beta protein). Functionally, the localization of alpha-keratin in the epithelium of the ventral surface of the lingual apex provides a proper scaffold for epithelial cells and promotes structural integrity, whereas the presence of beta-keratin (corneous beta protein) in the lingual nail, described also as exoskeleton of the ventral surface of the apex, endures mechanical stress. Anat Rec, 300:1361-1368, 2017. © 2017 Wiley Periodicals, Inc.

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“…The pH within the esophagus is similar to that of the saliva pH 6-7 and is maintained by the bicarbonate secretion from the esophageal submucosal glands (SMGs). SMGs are present in the submucosa of human, pig and dog which have a non-keratinized stratified squamous epithelium and are absent in rodents (keratinized stratified squamous epithelium) [71,72]. The SMGs also secrete a mucin like substance which is primarily neutral in nature and hence loosely bound in comparison to acidic mucin which has a tendency to form an adherent layer as seen in the large intestine.…”

Section: Mucosa and Mucus Of The Mouth Esophagus Small And Large Inmentioning

confidence: 99%

A slippery slope: On the origin, role and physiology of mucus

Taherali

Varum

Basit

2018

Advanced Drug Delivery Reviews

143

127

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The mucosa of the gastrointestinal tract, eyes, nose, lungs, cervix and vagina is lined by epithelium interspersed with mucus-secreting goblet cells, all of which contribute to their unique functions. This mucus provides an integral defence to the epithelium against noxious agents and pathogens. However, it can equally act as a barrier to drugs and delivery systems targeting epithelial passive and active transport mechanisms. This review highlights the various mucins expressed at different mucosal surfaces on the human body, and their role in creating a mucoid architecture to protect epithelia with specialized functions. Various factors compromising the barrier properties of mucus have been discussed, with an emphasis on how disease states and microbiota can alter the physical properties of mucus. For instance, Akkermansia muciniphila, a bacterium found in higher levels in the gut of lean individuals induces the production of a thickened gut mucus layer. The aims of this article are to elucidate the different physiological, biochemical and physical properties of bodily mucus, a keen appreciation of which will help circumvent the slippery slope of challenges faced in achieving effective mucosal drug and gene delivery.

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Keratinization of the esophageal epithelium of domesticated mammals

Cited by 11 publications

References 25 publications

Calpain-14 and its association with eosinophilic esophagitis

Calpain-14 and its association with eosinophilic esophagitis

Localization of Alpha‐Keratin and Beta‐Keratin (Corneous Beta Protein) in the Epithelium on the Ventral Surface of the Lingual Apex and Its Lingual Nail in the Domestic Goose (Anser Anser f. domestica) by Using Immunohistochemistry and Raman Microspectroscopy Analysis

A slippery slope: On the origin, role and physiology of mucus

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