Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2008-3-5
pubmed:abstractText
A domain (RKKRRQRRR) derived from HIV-1 Tat is one of the most efficient protein transduction domains (PTD) for delivering macromolecules including proteins into cells and tissues. Antioxidant enzymes such as superoxide dismutase (SOD) and catalase are major cellular defenses against oxidative stress which results in various diseases including skin inflammation. In this study, we examined the effect of SOD fused with HIV-1 Tat PTD (Tat-SOD) on TPA-induced skin inflammation in mice. Topical application of Tat-SOD to mice ears 1h after TPA application once a day for 3 days dose-dependently inhibited TPA-induced ear edema in mice. Topical application on mice ears of Tat-SOD also suppressed TPA-induced expression of proinflammatory cytokines such as TNF-alpha, IL-1beta, and IL-6 as well as cyclooxygenase-2 (COX-2) and production of PGE(2). Furthermore, topical application of Tat-SOD resulted in significant reduction in activation of NF-kappaB and mitogen-activated protein kinases (MAPK) in the mice ears treated with TPA. These data demonstrates that Tat-SOD inhibits TPA-induced inflammation in mice by reducing the levels of expression of proinflammatory cytokines and enzymes regulated by the NF-kappaB and MAPK and can be used as a therapeutic agent against skin inflammation related to oxidative damage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Inflammatory Agents, http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2, http://linkedlifedata.com/resource/pubmed/chemical/Cytokines, http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II, http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Ptgs2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase, http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate, http://linkedlifedata.com/resource/pubmed/chemical/tat Gene Products, Human...
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1873-2968
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1348-57
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18164693-Administration, Cutaneous, pubmed-meshheading:18164693-Animals, pubmed-meshheading:18164693-Anti-Inflammatory Agents, pubmed-meshheading:18164693-Cell Line, pubmed-meshheading:18164693-Cyclooxygenase 2, pubmed-meshheading:18164693-Cytokines, pubmed-meshheading:18164693-Dinoprostone, pubmed-meshheading:18164693-HIV-1, pubmed-meshheading:18164693-Humans, pubmed-meshheading:18164693-Inflammation, pubmed-meshheading:18164693-Male, pubmed-meshheading:18164693-Mice, pubmed-meshheading:18164693-Mice, Inbred ICR, pubmed-meshheading:18164693-Mitogen-Activated Protein Kinases, pubmed-meshheading:18164693-Nitric Oxide Synthase Type II, pubmed-meshheading:18164693-Protein Structure, Tertiary, pubmed-meshheading:18164693-Reactive Oxygen Species, pubmed-meshheading:18164693-Recombinant Fusion Proteins, pubmed-meshheading:18164693-Skin Diseases, pubmed-meshheading:18164693-Superoxide Dismutase, pubmed-meshheading:18164693-Tetradecanoylphorbol Acetate, pubmed-meshheading:18164693-tat Gene Products, Human Immunodeficiency Virus
pubmed:year
2008
pubmed:articleTitle
Topical transduction of superoxide dismutase mediated by HIV-1 Tat protein transduction domain ameliorates 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced inflammation in mice.
pubmed:affiliation
Department of Biomedical Science, Hallym University, 1 Okchun-dong, Chunchon, Kangwon-Do 200-702, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't