Abstract
Phosphorylation, the addition of a phosphate group to a molecule, is an effective way of regulating the biological properties of that molecule. Protein phosphorylation is a post-translational modification of proteins and affects cellular signaling transduction. Protein kinases induce phosphorylation by catalyzing the transfer of phosphate groups to serine, threonine, and tyrosine residues on protein substrates. Consistent with their roles in cancer, protein kinases have emerged as one of the most clinically useful target molecules in pharmacological cancer therapy. Intrinsic or acquired resistance of cancers against anti-cancer therapeutics, such as ionizing radiation, is a major obstacle for the effective treatment of many cancers. In this review, we describe key aspects of various kinases acting on proteins. We also discuss the roles of protein kinases in the pathophysiology and treatment of cancer. Because protein kinases correlate with radiation resistance in various types of cancer, we focus on several kinases responsible for radiation resistance and/or sensitivity and their therapeutic implications. Finally, we suggest some ongoing radiation-sensitization strategies using genetic loss and/or kinase inhibitors that can counteract radiation resistance-related protein kinases.
Keywords: Kinase, protein, cancer, resistance, ionizing radiation, therapeutic target, radiation-sensitization strategies.
Current Pharmaceutical Design
Title:Role of Protein Kinases and Their Inhibitors in Radiation Response of Tumor Cells
Volume: 23 Issue: 29
Author(s): Byeong Mo Kim*, Wonsuck Yoon, Jung-Hyun Shim, Haiyoung Jung, Ji Hong Lim, Hyun-Jung Choi, MiRan Seo, Tae Ho Lee and Sang-Hyun Min*
Affiliation:
- Severance Integrative Research Institute for Cerebral & Cardiovascular Diseases (SIRIC), Yonsei University College of Medicine, 50 Yonsei-ro, Seodaemun-gu, Seoul 03722,Korea
- New Drug Development Center, DGMIF, 80 Chumbok-ro, Dong-gu, Daegu 41061,Korea
Keywords: Kinase, protein, cancer, resistance, ionizing radiation, therapeutic target, radiation-sensitization strategies.
Abstract: Phosphorylation, the addition of a phosphate group to a molecule, is an effective way of regulating the biological properties of that molecule. Protein phosphorylation is a post-translational modification of proteins and affects cellular signaling transduction. Protein kinases induce phosphorylation by catalyzing the transfer of phosphate groups to serine, threonine, and tyrosine residues on protein substrates. Consistent with their roles in cancer, protein kinases have emerged as one of the most clinically useful target molecules in pharmacological cancer therapy. Intrinsic or acquired resistance of cancers against anti-cancer therapeutics, such as ionizing radiation, is a major obstacle for the effective treatment of many cancers. In this review, we describe key aspects of various kinases acting on proteins. We also discuss the roles of protein kinases in the pathophysiology and treatment of cancer. Because protein kinases correlate with radiation resistance in various types of cancer, we focus on several kinases responsible for radiation resistance and/or sensitivity and their therapeutic implications. Finally, we suggest some ongoing radiation-sensitization strategies using genetic loss and/or kinase inhibitors that can counteract radiation resistance-related protein kinases.
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Cite this article as:
Kim Mo Byeong*, Yoon Wonsuck, Shim Jung-Hyun , Jung Haiyoung, Lim Hong Ji , Choi Hyun-Jung, Seo MiRan , Lee Ho Tae and Min Sang-Hyun*, Role of Protein Kinases and Their Inhibitors in Radiation Response of Tumor Cells, Current Pharmaceutical Design 2017; 23 (29) . https://dx.doi.org/10.2174/1381612823666170608084355
DOI https://dx.doi.org/10.2174/1381612823666170608084355 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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