Linked Life Data

19326452

Source:http://linkedlifedata.com/resource/pubmed/id/19326452

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2009-4-20
pubmed:abstractText
Apoptin protein harbors tumor-selective cell death activity, which makes it a potential anticancer therapy candidate. This study reports an apoptin therapy approach based on protein transduction domain 4 (PTD4)-mediated transduction of recombinant apoptin protein. In vitro, the PTD4-apoptin fusion protein is located in the nucleus and induces cell death in, e.g., human hepatocarcinoma HepG2 cells. In normal human L-02 hepatocytes, PTD4-apoptin protein retained mainly cytoplasmic and did not induce detectable levels of cell death, illustrating that the PTD4 domain does not affect apoptin's tumor-selective characteristics. In vivo, liver, cervix and gastric carcinoma xenografts treated with PTD4-apoptin protein for 6 days via the tumor epidermis exhibited a significant tumor growth inhibition because of apoptin-mediated cell death. In addition, treatment of human hepatocarcinoma xenografts during 3 weeks showed that PTD4-apoptin protein has significant anticancer activity, whereas control treatment with PTD4-enhanced green fluorescence protein or saline did not. Cell death and disruption of the tumor integrity were apparent in the PTD4-apoptin transduced xenografted tumors. As important, although PTD4-apoptin protein could be detected in the epidermal tissue covering the subcutaneous tumor tissue and in several organs, such as liver and brain, of the treated mice, no tissue disruption or signs of cell death could be detected. Our in vivo data reveal that apoptin protein delivery constitutes a novel powerful and safe anticancer therapy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1097-0215
pubmed:author
pubmed:copyrightInfo
Copyright 2008 UICC.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2973-81
pubmed:dateRevised
2011-4-26
pubmed:meshHeading
pubmed-meshheading:19326452-Animals, pubmed-meshheading:19326452-Apoptosis Regulatory Proteins, pubmed-meshheading:19326452-Capsid Proteins, pubmed-meshheading:19326452-Carcinoma, Hepatocellular, pubmed-meshheading:19326452-Carrier Proteins, pubmed-meshheading:19326452-Cell Nucleus, pubmed-meshheading:19326452-Cells, Cultured, pubmed-meshheading:19326452-Colony-Forming Units Assay, pubmed-meshheading:19326452-Female, pubmed-meshheading:19326452-Flow Cytometry, pubmed-meshheading:19326452-Hepatocytes, pubmed-meshheading:19326452-Humans, pubmed-meshheading:19326452-In Situ Nick-End Labeling, pubmed-meshheading:19326452-Liver Neoplasms, pubmed-meshheading:19326452-Mice, pubmed-meshheading:19326452-Mice, Inbred BALB C, pubmed-meshheading:19326452-Mice, Nude, pubmed-meshheading:19326452-Nuclear Localization Signals, pubmed-meshheading:19326452-Recombinant Fusion Proteins, pubmed-meshheading:19326452-Stomach Neoplasms, pubmed-meshheading:19326452-Subcellular Fractions, pubmed-meshheading:19326452-Uterine Cervical Neoplasms
pubmed:year
2009
pubmed:articleTitle
PTD4-apoptin protein therapy inhibits tumor growth in vivo.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't