ArticlePloS one2014
First report of a thioredoxin homologue in jellyfish: molecular cloning, expression and antioxidant activity of CcTrx1 from Cyanea capillata.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Structure and Function Analyses of the Thioredoxin 2 and Thioredoxin Reductase Gene in Pacific White Shrimp (Animals : an open access journal from MDPI · 2025Article
- Reduced Thioredoxin Regulates IL-1β Secretion via NLRP3 of IL-1β+ Alveolar Macrophages in COPD.Journal of inflammation research · 2025Article
- Role of thioredoxin in chronic obstructive pulmonary disease (COPD): a promising future target.Respiratory research · 2023Review
- Protective Effects of a Jellyfish-Derived Thioredoxin Fused with Cell-Penetrating Peptide TAT-PTD on HInternational journal of molecular sciences · 2023Article
- Collective Locomotion of Human Cells, Wound Healing and Their Control by Extracts and Isolated Compounds from Marine Invertebrates.Molecules (Basel, Switzerland) · 2020Review
- Barrel Jellyfish (Marine drugs · 2019Article
- Stress-Induced Mucus Secretion and Its Composition by a Combination of Proteomics and Metabolomics of the JellyfishMarine drugs · 2018Article
- Characterization of a protozoan Phosducin-like protein-3 (PhLP-3) reveals conserved redox activity.PloS one · 2018Article
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
Thioredoxins (Trx proteins) are a family of small, highly-conserved and ubiquitous proteins that play significant roles in the resistance of oxidative damage. In this study, a homologue of Trx was identified from the cDNA library of tentacle of the jellyfish Cyanea capillata and named CcTrx1. The full-length cDNA of CcTrx1 was 479 bp with a 312 bp open reading frame encoding 104 amino acids. Bioinformatics analysis revealed that the putative CcTrx1 protein harbored the evolutionarily-conserved Trx active site 31CGPC34 and shared a high similarity with Trx1 proteins from other organisms analyzed, indicating that CcTrx1 is a new member of Trx1 sub-family. CcTrx1 mRNA was found to be constitutively expressed in tentacle, umbrella, oral arm and gonad, indicating a general role of CcTrx1 protein in various physiological processes. The recombinant CcTrx1 (rCcTrx1) protein was expressed in Escherichia coli BL21 (DE3), and then purified by affinity chromatography. The rCcTrx1 protein was demonstrated to possess the expected redox activity in enzymatic analysis and protection against oxidative damage of supercoiled DNA. These results indicate that CcTrx1 may function as an important antioxidant in C. capillata. To our knowledge, this is the first Trx protein characterized from jellyfish species.
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