Melatonin sensitizes human malignant glioma cells against TRAIL-induced cell death
Abstract Despite the common expression of death receptors, many types of cancer including gliomas are resistant to the death receptor ligand (TRAIL). Melatonin antitumoral actions have been extensively described, including oncostatic properties on several tumor types and improvement of chemotherapeu...
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| Published in | Cancer letters Vol. 287; no. 2; pp. 216 - 223 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
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28.01.2010
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| Abstract | Abstract Despite the common expression of death receptors, many types of cancer including gliomas are resistant to the death receptor ligand (TRAIL). Melatonin antitumoral actions have been extensively described, including oncostatic properties on several tumor types and improvement of chemotherapeutic regimens. Here, we found that melatonin effectively increase cell sensitivity to TRAIL-induced cell apoptosis in A172 and U87 human glioma cells. The effect seems to be related to a modulation of PKC activity which in turns decreases Akt activation leading to an increase in death receptor 5 (DR5) levels and a decrease in the antiapoptotic proteins survivin and bcl-2 levels. |
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| AbstractList | Abstract Despite the common expression of death receptors, many types of cancer including gliomas are resistant to the death receptor ligand (TRAIL). Melatonin antitumoral actions have been extensively described, including oncostatic properties on several tumor types and improvement of chemotherapeutic regimens. Here, we found that melatonin effectively increase cell sensitivity to TRAIL-induced cell apoptosis in A172 and U87 human glioma cells. The effect seems to be related to a modulation of PKC activity which in turns decreases Akt activation leading to an increase in death receptor 5 (DR5) levels and a decrease in the antiapoptotic proteins survivin and bcl-2 levels. Despite the common expression of death receptors, many types of cancer including gliomas are resistant to the death receptor ligand (TRAIL). Melatonin antitumoral actions have been extensively described, including oncostatic properties on several tumor types and improvement of chemotherapeutic regimens. Here, we found that melatonin effectively increase cell sensitivity to TRAIL-induced cell apoptosis in A172 and U87 human glioma cells. The effect seems to be related to a modulation of PKC activity which in turns decreases Akt activation leading to an increase in death receptor 5 (DR5) levels and a decrease in the antiapoptotic proteins survivin and bcl-2 levels. |
| Author | Casado-Zapico, Sara Antolín, Isaac Medina, Maria Rodriguez, Carmen Martín, Vanesa Sanchez-Sanchez, Ana García-Santos, Guillermo Rodriguez-Blanco, Jezabel |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19632770$$D View this record in MEDLINE/PubMed |
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| Keywords | Melatonin TRAIL Glioma Death receptors Apoptosis |
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| Snippet | Abstract Despite the common expression of death receptors, many types of cancer including gliomas are resistant to the death receptor ligand (TRAIL). Melatonin... Despite the common expression of death receptors, many types of cancer including gliomas are resistant to the death receptor ligand (TRAIL). Melatonin... |
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| SubjectTerms | Antineoplastic Combined Chemotherapy Protocols - pharmacology Apoptosis Apoptosis - drug effects Cancer Cancer therapies Cell death Cell growth Cell Line, Tumor Cell Survival - drug effects Death receptors Glioma Glioma - metabolism Glioma - pathology Hematology, Oncology and Palliative Medicine Humans Inhibitor of Apoptosis Proteins Melatonin Melatonin - pharmacology Microtubule-Associated Proteins - metabolism Phosphorylation Protein Kinase C - metabolism Proto-Oncogene Proteins c-akt - metabolism Proto-Oncogene Proteins c-bcl-2 - metabolism Receptors, TNF-Related Apoptosis-Inducing Ligand - metabolism Signal Transduction - drug effects TNF-Related Apoptosis-Inducing Ligand - pharmacology TRAIL Tumors |
| Title | Melatonin sensitizes human malignant glioma cells against TRAIL-induced cell death |
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