Protein Kinase C: Emerging Roles and Therapeutic Potential

Dean J. Pierce (Editor)

Series: Biochemistry Research Trends
BISAC: SCI013010

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In this compilation, the authors review the structural basis of PKC isozymes and focus on the C1 domain, as well as the plausible binding mechanisms of its activators. Additionally, the recent molecular dynamics simulation studies of how phorbol esters or bryostatin bind to the activator pocket are described and some of the key amino acid residues recently identified as important for activator binding are investigated. The following chapter focuses on the expression pattern and function of PKCá in cancer cells, and newly emerging PKCá-targeted cancer therapies. PKCá acts directly and/or indirectly in various signaling mechanisms in cancer cells, including proliferation, survival, invasion, migration, apoptosis and drug resistance. A final review is provided which dissects the crosstalk between p53 and PKCä in the context of apoptotic cell death and cancer therapy. PKCä is implicated in a transcriptional regulation of the p53 tumor suppressor that is critical for cell cycle arrest and apoptosis in response to DNA damage.

Preface

Chapter 1. Structural Basis of Protein Kinase C and the Interactions with Modulators
(Nuttee Sureea,Patcharapong Thangsunana, and Suriya Tateinga, Division of Biochemistry and Biochemical Technology Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai University, Chiang Mai, Thailand, and others)

Chapter 2. Protein Kinase Cá as a Therapeutic Target in Cancer
(Jeong-Hun Kang, Junichi Inokuchi, Takahito Kawano, and Masaharu Murata, Division of Biopharmaceutics and Pharmacokinetics, National Cerebral and Cardiovascular Center Research Institute, Fujishiro-dai, Suita, Osaka, Japan)

Chapter 3. Tumor Suppressive Functions of Protein Kinase Cä in DNA Damage Response
(Kiyotsugu Yoshida, Department of Biochemistry, Jikei University School of Medicine, Tokyo, Japan)

Chapter 4. Bibliography

Chapter 5. Related Nova Publications

Index

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