- Alpha-keratin and corneous beta protein in the parakeratinized epithelium of the tongue in the domestic goose (Anser anser f. domestica). [Journal Article]
- JEJ Exp Zool B Mol Dev Evol 2019; 332(5):158-166
- The parakeratinized epithelium is a common epithelium in the oral cavity in birds and is characterized by the presence of cell nuclei in the cells of the cornified layer. This epithelium covers almos…
The parakeratinized epithelium is a common epithelium in the oral cavity in birds and is characterized by the presence of cell nuclei in the cells of the cornified layer. This epithelium covers almost the entire dorsal surface of the tongue in the domestic goose apart of the lingual nail and conical papillae. So far no study has identified the molecular proteins alpha-keratin (IF-keratin) and/or corneous beta protein (CBP), which are responsible for keratinization or cornification processes in the parakeratinized epithelium of domestic geese. The study was performed using immunohistochemical (IHC) methods to identify alpha-keratin. The innovative method of Raman microspectroscopy was used to determine the presence of CBP and specify their percentage in epithelial layers of the parakeratinized epithelium. The results revealed that alpha-keratin is present in the whole parakeratinized epithelium. A strong staining reaction was detected in the basal and intermediate layers and a less strong staining reaction in the cornified layer. Raman microspectroscopy analysis confirmed the presence of alpha-keratin and demonstrated that its percentage decreases from the basal layer to the cornified layer. The Raman microspectroscopy technique revealed the occurrence of CBP in the parakeratinized epithelium and demonstrated that the percentage of this protein increases from the basal layer to the cornified layer. Performed analysis determines that parakeratinized epithelium undergoes cornification. However, the lower percentage of CBP in the cornified layer of parakeratinized epithelium than in orthokeratinized epithelium points to the fact that parakeratinized epithelium has a weaker protective function.
- Morphology of setae in regenerating caudal adhesive pads of the gecko Lygodactylus capensis (Smith, 1849). [Journal Article]
- ZZoology (Jena) 2019; 133:1-9
- After tail loss in the African gecko Lygodactylus capensis (Smith, 1949) a new tail is regenerated, including caudal adhesive pads. The axial skeleton of the regenerating tail consists in an elastic …
After tail loss in the African gecko Lygodactylus capensis (Smith, 1949) a new tail is regenerated, including caudal adhesive pads. The axial skeleton of the regenerating tail consists in an elastic cartilaginous tube replacing the original vertebrae that allows interacting with the substrate like in the original tail. The formation of adhesive setae has been analyzed using transmission and scanning electron microscopy coupled to immunolabeling for Corneous Beta Proteins. During progressive stages of epidermal differentiation new setae are developed at stage 4 of the shedding cycle and contain Corneous Beta Proteins. These structural proteins are faintly localized in the Oberhäutchen but are abundant in the beta-layer, indicating that the two epidermal layers have a different protein composition. The setae originate from the growth of Oberhäutchen spinulae into the cytoplasm of clear cells and the latter produce a thick fibrous meshwork of keratin and other unknown proteins localized around the growing setae. This cytoskeleton likely allows molding tail setae like for digital setae. A graded development of setae is observed from the base to the tip of regenerated pads and from the periphery to more central areas. The terminal end of the setae is subdivided into numerous filamentous spatulae that increase the adhesion contact. Sensory boutons are frequently detected at the margin of tail scales and adhesive pads, likely improving compliance with the substrate. The present study indicates that tail regeneration is a convenient experimental model to analyze adhesive setae formation, microstructures that allow to these lizards climbing vertical and arboreal substrates.
- Molecular structure of sauropsid β-keratins from tuatara (Sphenodon punctatus). [Journal Article]
- JSJ Struct Biol 2019 Jul 01; 207(1):21-28
- The birds and reptiles, collectively known as the sauropsids, can be subdivided phylogenetically into the archosaurs (birds, crocodiles), the testudines (turtles), the squamates (lizards, snakes) and…
The birds and reptiles, collectively known as the sauropsids, can be subdivided phylogenetically into the archosaurs (birds, crocodiles), the testudines (turtles), the squamates (lizards, snakes) and the rhynchocephalia (tuatara). The structural framework of the epidermal appendages from the sauropsids, which include feathers, claws and scales, has previously been characterised by electron microscopy, infrared spectroscopy and X-ray diffraction analyses, as well as by studies of the amino acid sequences of the constituent β-keratin proteins (also referred to as the corneous β-proteins). An important omission in this work, however, was the lack of sequence and structural data relating to the epidermal appendages of the rhynchocephalia (tuatara), one of the two branches of the lepidosaurs. Considerable effort has gone into sequencing the tuatara genome and while this is not yet complete, there are now sufficient sequence data for conclusions to be drawn on the similarity of the β-keratins from the tuatara to those of other members of the sauropsids. These results, together with a comparison of the X-ray diffraction pattern of tuatara claw with those from seagull feather and goanna claw, confirm that there is a common structural plan in the β-keratins of all of the sauropsids, and not just those that comprise the archosaurs (birds and crocodiles), the testudines (turtles) and the squamates (lizards and snakes).
- Duplications in corneous beta protein genes and the evolution of gecko adhesion. [Journal Article]
- ICIntegr Comp Biol 2019 Mar 21
- Corneous proteins are an important component of the tetrapod integument. Duplication and diversification of keratins and associated proteins are linked with the origin of most novel integumentary str…
Corneous proteins are an important component of the tetrapod integument. Duplication and diversification of keratins and associated proteins are linked with the origin of most novel integumentary structures like mammalian hair, avian feathers, and scutes covering turtle shells. Accordingly, the loss of integumentary structures often coincides with the loss of genes encoding keratin and associated proteins. For example, many hair keratins in dolphins and whales have become pseudogenes. The adhesive setae of geckos and anoles are composed of both intermediate filament keratins (IF-keratins, formerly known as alpha-keratins) and corneous beta-proteins (CBPs, formerly known as beta-keratins) and recent whole genome assemblies of two gecko species and an anole uncovered duplications in seta-specific CBPs in each of these lineages. While anoles evolved adhesive toepads just once, there are two competing hypotheses about the origin(s) of digital adhesion in geckos involving either a single origin or multiple origins. Using data from three published gecko genomes, I examine CBP gene evolution in geckos and find support for a hypothesis where CBP gene duplications are associated with the repeated evolution of digital adhesion. Although these results are preliminary, I discuss how additional gecko genome assemblies, combined with phylogenies of keratin and associated protein genes and gene duplication models, can provide rigorous tests of several hypotheses related to gecko CBP evolution. This includes a taxon sampling strategy for sequencing and assembly of gecko genomes that could help resolve competing hypotheses surrounding the origin(s) of digital adhesion.
- Structure and function of skin in the pelagic sea snake, Hydrophis platurus. [Journal Article]
- JMJ Morphol 2019; 280(4):544-554
- We describe and interpret the functional morphology of skin of the Yellow-bellied sea snake, Hydrophis platurus. This is the only pelagic sea snake, and its integument differs from what is known for …
We describe and interpret the functional morphology of skin of the Yellow-bellied sea snake, Hydrophis platurus. This is the only pelagic sea snake, and its integument differs from what is known for other species of snakes. In gross appearance, the scales of H. platurus consist of non-overlapping, polygonal knobs with flattened outer surfaces bearing presumptive filamentous sensillae. The deep recesses between scales ('hinge') entrap and wick water over the body surface, with mean retention of 5.1 g/cm of skin surface, similar to that determined previously for the roughened, spiny skin of marine file snakes, Acrochordus granulatus. This feature possibly serves to maintain the skin wet when the dorsal body protrudes above water while floating on calm oceanic slicks where they forage. In contrast with other snakes, including three species of amphibious, semi-marine sea kraits (Laticauda spp.), the outer corneous β-protein layer consists of a syncytium that is thinner than seen in most other species. The subjacent α-layer is also thin, and lipid droplets and lamellar bodies are seen among the immature, cornifying α-cells. A characteristic mesos layer, comprising the water permeability barrier, is either absent or very thin. These features are possibly related to (1) permeability requirements for cutaneous gas exchange, (2) reduced gradient for water efflux compared with terrestrial environments, (3) less need for physical protection in water compared with terrestrial ground environments, and (4) increased frequency of ecdysis thought to be an anti-fouling mechanism. The lipogenic features of the α-layer possibly compensate for the reduced or absent mesos layer, or produce layers of cells that comprise what functionally might be termed a mesos layer, but where the organization of barrier lipids nonetheless appears less robust than what is characteristically seen in squamates.
- Review: Evolution and diversification of corneous beta-proteins, the characteristic epidermal proteins of reptiles and birds. [Review]
- JEJ Exp Zool B Mol Dev Evol 2018; 330(8):438-453
- In all amniotes specialized intermediate filament keratins (IF-keratins), in addition to keratin-associated and corneous proteins form the outermost cornified layer of the epidermis. Only in reptiles…
In all amniotes specialized intermediate filament keratins (IF-keratins), in addition to keratin-associated and corneous proteins form the outermost cornified layer of the epidermis. Only in reptiles and birds (sauropsids) the epidermis of scales, claws, beaks, and feathers, largely comprises small proteins formerly indicated as "beta-keratins" but here identified as corneous beta-proteins (CBPs) to avoid confusion with true keratins. Genes coding for CBPs have evolved within the epidermal differentiation complex (EDC), a locus with no relationship with those of IF-keratins. CBP genes have the same exon-intron structure as EDC genes encoding other corneous proteins of sauropsids and mammals, but they are unique by encoding a peculiar internal amino acid sequence motif beta-sheet region that allows formation of CBP filaments in the epidermis and epidermal appendages of reptiles and birds. In contrast, skin appendages of mammals, like hairs, claws, horns and nails, contain keratin-associated proteins that, like IF-keratin genes, are encoded by genes in loci different from the EDC. Phylogenetic analysis shows that lepidosaurian (lizards and snakes) and nonlepidosaurian (crocodilians, birds, and turtles) CBPs form two separate clades that likely originated after the divergence of these groups of sauropsids in the Permian Period. Clade-specific CBPs evolved to make most of the corneous material of feathers in birds and of the shell in turtles. Based on the recent identification of the complete sets of CBPs in all major phylogenetic clades of sauropsids, this review provides a comprehensive overview of the molecular evolution of CBPs.
- Locking of the operculum in a water snail: Theoretical modeling and applications for mechanical sealing. [Journal Article]
- JTJ Theor Biol 2019 Mar 07; 464:104-111
- How can a water snail lock its door by an operculum? In this theoretical and experimental combined research, we revealed this by dissection, modeling and validation with a 3D printed technique. The o…
How can a water snail lock its door by an operculum? In this theoretical and experimental combined research, we revealed this by dissection, modeling and validation with a 3D printed technique. The operculum is a corneous or calcareous trapdoor-like sheet which attaches to the upper surface of the water snail's foot. It can plug the shell aperture by retracting the soft body when a predator or environmental threat is encountered. For a water snail (Pomacea canaliculata), the operculum can be locked in its shell rapidly. By optical microscope images, we found the operculum of P. canaliculata is a multilayered disk with a thicker center and thinner edge, which may be functionally influential for successful closing and opening the trapdoor. We filmed the locking in opercula of living snails, and designed an experiment to measure the deformation of opercula on the dead samples. We propose one mathematical model to describe the connections among geometry, sectionalized stiffness and the force for locking. By using 3D printing technique, we designed an operculum inspired locking mechanism to validate the theories we proposed. Under the same normal force, the water leakage rate of the bio-inspired structure can be reduced to 99% compared to the disk with uniform thickness. Our results reveal that the snail's operculum not only develops a light-weight trapdoor, but a locking mechanism which could serve as a valuable model for designing compliant locking mechanisms.
- Immunolocalization of serpins in the regenerating tail of lizard suggests a role for epidermal and neural barrier formation. [Journal Article]
- ZZoology (Jena) 2018; 131:1-9
- Tail regeneration in lizard is stimulated from the apical epidermis and spinal cord, the principal sources of growth factors and signaling proteins that sustain regeneration. Immunolabeling shows tha…
Tail regeneration in lizard is stimulated from the apical epidermis and spinal cord, the principal sources of growth factors and signaling proteins that sustain regeneration. Immunolabeling shows that serpins (serine protease inhibitors), which genes are among those most up-regulated during tail regeneration, are prevalently immunolocalized in the regenerating epidermis and ependyma. Western blot detects main protein bands extracted from regenerating tail at 25-27 and 48-52 kDa. The former band may correspond to p27 serpin, a degraded immunogenic fragment of serpin detected in psoriasis and cancer. This suggests that also in lizard the degradation of these proteins occurs but is uncertain whether it is physiological with some function or the fragments derive from the extractive process. In the regenerating epidermis serpins are mainly accumulated in pre-corneous and corneous layers (alpha-layers), and also in the forming oberhautchen and hard beta-layer. In the tail tip serpin-immunolabeling is mainly seen in the ependymal tube and with lower intensity in blastema (mesenchymal) cells. Aside the control on endogenous proteases for the formation of a protective corneous barrier, serpins may also form a protective anti-microbial barrier for the ependyma. The protection of the epidermis and ependyma allows these tissue to continue the stimulation for tail regeneration.
- Rediagnosis of the squat lobster genus Gastroptychus Caullery, 1896, with a new genus Sternostylus and a new family Sternostylidae (Crustacea: Decapoda: Anomura: Chirostyloidea). [Journal Article]
- ZZootaxa 2018 Nov 20; 4524(1):77-86
- The chirostyloidean squat lobster genus Gastroptychus Caullery, 1896 is revised and is split into two genera: Gastroptychus sensu stricto (type species, Ptychogaster spinifer A. Milne-Edwards, 1880) …
The chirostyloidean squat lobster genus Gastroptychus Caullery, 1896 is revised and is split into two genera: Gastroptychus sensu stricto (type species, Ptychogaster spinifer A. Milne-Edwards, 1880) and Sternostylus new genus (type species, Ptychogaster formosus Filhol, 1884). Gastroptychus sensu stricto, is restricted to nine species with a sternal plastron, at sternite 3, abruptly demarcated from the preceding sternites (excavated sternum) by a distinct step forming a well-defined transverse or concave anterior margin at the articulation with maxillipeds 3, the maxillipeds 3 widely separated, with the distal parts accommodated in the excavated sternum between the left and right maxillipeds 3 when folded, and the P2-4 dactyli with the terminal spine demarcated by a suture. Sternostylus new genus, represented by 12 species, has the sternite 3 anteriorly bluntly produced medially and steeply sloping anterodorsally to the anterior sternite, with a pair of spines directly behind the anterior margin, the left and right maxillipeds 3 adjacent, and the P2-4 dactyli ending in an indistinctly demarcated corneous spine. The above-mentioned characters of Gastroptychus are consistent with Chirostylidae sensu stricto. Published molecular phylogenies indicate, however, that Sternostylus is the sister group to all the other Chirostylidae, and is designated the type genus of a new family, Sternostylidae.
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- Epicutaneous immunotherapy in rhino-conjunctivitis and food allergies: a review of the literature. [Review]
- JTJ Transl Med 2018 11 27; 16(1):329
- CONCLUSIONS: Overall, the EPIT study results, even if they were affected by great heterogeneity among the methodologies applied, have shown not only the high safety and adherence with this kind of immunotherapy but also suggested the possibility for obtaining definitive evidence of the efficacy of EPIT, especially for food allergies.