Protein composition of extracellular vesicles from skin secretions of the amphibian Bombina maxima
Proteomic analysis using liquid chromatographytandem mass spectrometry identified 131 proteins in the skin secretion-derived EVs, which were enriched in biological processes and molecular functions such as immune stress, metabolism, oxidoreduction, and transport. By targeting gangliosides and sulfat...
Gespeichert in:
Veröffentlicht in: | Dōngwùxué yánjiū 2022-07, Vol.43 (4), p.687-690 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | Proteomic analysis using liquid chromatographytandem mass spectrometry identified 131 proteins in the skin secretion-derived EVs, which were enriched in biological processes and molecular functions such as immune stress, metabolism, oxidoreduction, and transport. By targeting gangliosides and sulfatides in cell membrane lipid rafts (Guo et al., 2019), ßYCAT acts on both endocytic and exocytic pathways to form channels on endolysosomes and drive the import and export of cellular material (such as nutrients, water, ions, and antigens) via the endolysosomal pathways (Zhang et al., 2021). [...]ßY-CAT and its regulatory network define a secretory endolysosomal channel (SELC) pathway, thus representing a novel PFP-driven cell vesicular delivery system (Zhang et al., 2021). The ßY-CAT pathway plays multiple roles in toad adaptation to environment change, dependent on the cellular and surrounding environment, including in immune defense and tissue repair (Zhang et al., 2021), water maintenance under osmotic stress (Zhao et al., 2021), and nutrient acquisition or delivery under starvation (Shi et al., 2022). Amphibian skin is exposed to both water and land environments and is easily damaged by environmental stressors, such as microorganisms, ultraviolet radiation, and heavy metal ions (Xu & Lai, 2015; Zhang, 2015). |
---|---|
ISSN: | 2095-8137 0254-5853 |
DOI: | 10.24272/j.issn.2095-8137.2022.069 |