Glycosaminoglycans (GAGs) from the integument of Lithobates catesbeianus were biochemically characterized and histochemically localized. Moreover, carbohydrate distribution was investigated using conventional and lectin histochemistry at light microscopy. Hyaluronan (HA), dermatan sulfate (DS) and a heparanoid were found in the integument. Sulfated and carboxylated GAGs were visualized in the Eberth-Katschenko (EK) layer, in the mucous glands, in the hypodermis as well as in the mast cells. Furthermore, glucose and galactose were identified in the integument through thin layer chromatography (TLC) assays. N-Acetyl-beta-glucosamine residues were identified in the mucous glandular cells, between the corneum and spinosum strata, in the subepidermal region, and in the EK layer. N-Acetyl-galactosamine residues were evident in the EK layer, corresponding to a residue of the dermatan sulfate chain, which may be related to the collagenous fiber arrangement. These glycoconjugates occurred as secretory glandular products and as dermal structural elements. Moreover, HA and DS are the predominant GAGs in the L. catesbeianus integument. Considering the importance of glycoconjugates, they play a significant role to the integrity of the skin, providing mechanical support for integument cells. In addition, they are important to the water regulation mechanisms, since L. catesbeianus is preferably aquatic.
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http://dx.doi.org/10.1016/j.micron.2010.03.001 | DOI Listing |
Comp Biochem Physiol B Biochem Mol Biol
January 2025
Departamento de Bioquímica, Centro de Biociências, Universidade Federal de Pernambuco, Recife, Pernambuco, Brazil. Electronic address:
This work investigated the peptide profile of skin secretion from Lithobates palmipes collected from the Brazilian Atlantic Forest. The secretion was submitted to reversed phase high-performance liquid chromatography (RP-HPLC) and the fractions were screened for antibacterial activity. RP-HPLC resulted in the separation of several peaks, among which 10 showed antibacterial activity and contained peptides of the ranatuerin, brevinin and temporin families.
View Article and Find Full Text PDFComp Biochem Physiol Part D Genomics Proteomics
December 2024
University of Connecticut, Department of Ecology and Evolutionary Biology, Storrs, CT, 06269, USA.
Among terrestrial ectotherms, hibernation is a common response to extreme cold temperatures and is associated with reduced physiological rates, including immunity. When winter wanes and temperatures increase, so too do vital rates of both ectothermic hosts and their parasites. Due to metabolic scaling, if parasite activity springs back faster than host immune functions then cold seasons and transitions between cold and warm seasons may represent periods of vulnerability for ectothermic hosts.
View Article and Find Full Text PDFDis Aquat Organ
May 2024
Sección Bioquímica, Departamento de Biología, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay.
The amphibian chytrid fungus Batrachochytrium dendrobatidis (Bd) causes chytridiomycosis, a disease among the main causes of amphibian declines worldwide. However, Bd studies on Neotropical amphibians from temperate areas are scarce. We present a comprehensive survey of Bd in Uruguay, in temperate central eastern South America, carried out between 2006 and 2014.
View Article and Find Full Text PDFComp Biochem Physiol Part D Genomics Proteomics
June 2024
Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8P 5C2, Canada. Electronic address:
As amphibians undergo thyroid hormone (TH)-dependent metamorphosis from an aquatic tadpole to the terrestrial frog, their innate immune system must adapt to the new environment. Skin is a primary line of defense, yet this organ undergoes extensive remodelling during metamorphosis and how it responds to TH is poorly understood. Temperature modulation, which regulates metamorphic timing, is a unique way to uncover early TH-induced transcriptomic events.
View Article and Find Full Text PDFBiology (Basel)
March 2024
Department of Chemical, Biological, Pharmaceutical, and Environmental Sciences, University of Messina, 98166 Messina, Italy.
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