期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 24, 期 8, 页码 -出版社
MDPI
DOI: 10.3390/ijms24087340
关键词
thioredoxin; oxidative stress; jellyfish; protein transduction domain; antioxidant
This study confirms that the fusion protein PTD-CcTrx1 obtained from the jellyfish Cyanea capillata has antioxidant abilities and can protect skin cells from oxidative damage. The findings provide critical evidence for the future application of PTD-CcTrx1 as a treatment for skin oxidative damage.
Thioredoxin (Trx) plays a critical role in maintaining redox balance in various cells and exhibits anti-oxidative, anti-apoptotic, and anti-inflammatory effects. However, whether exogenous Trx can inhibit intracellular oxidative damage has not been investigated. In previous study, we have identified a novel Trx from the jellyfish Cyanea capillata, named CcTrx1, and confirmed its antioxidant activities in vitro. Here, we obtained a recombinant protein, PTD-CcTrx1, which is a fusion of CcTrx1 and protein transduction domain (PTD) of HIV TAT protein. The transmembrane ability and antioxidant activities of PTD-CcTrx1, and its protective effects against H2O2-induced oxidative damage in HaCaT cells were also detected. Our results revealed that PTD-CcTrx1 exhibited specific transmembrane ability and antioxidant activities, and it could significantly attenuate the intracellular oxidative stress, inhibit H2O2-induced apoptosis, and protect HaCaT cells from oxidative damage. The present study provides critical evidence for application of PTD-CcTrx1 as a novel antioxidant to treat skin oxidative damage in the future.
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