TECHNOLOGY BRIEF
DNA-DEPENDENT PROTEIN KINASE ASSAY
For further information, contact Christine Brakel
Description: Protein phosphorylation has long been recognized as a major mechanism in mediating cellular responses to environmental conditions. Protein phosphorylation is central to signal transduction pathways and cell cycle regulation. DNA-Dependent Protein Kinase (DNA-PK) is a nuclear threonine-serine protein kinase involved in DNA double-stranded break repair and V(D)J recombination. The present invention provides tools for monitoring the activity of the enzyme in cells, providing highly specific peptide substrates and nucleic acid co-factors in addition to genetic constructs for expression of protein substrates.
Commercial and Technical Merit: The role of this enzyme in the regulation of cell growth and in the development of immunity makes this assay a potent tool for assessing the efficacy of effector molecules. Drugs that alter the DNA-PK activity of cells might be used in the design of new anticancer chemotherapeutic strategies such as the development of agents that potentiate the effect of chemotherapeutic drugs so as to make them less toxic to non-cancerous tissue. Effectors of DNA-PK activity might also be used as therapeutic modulators in the treatment of various disorders of the immune system.
Competitive Advantage: The materials disclosed in the present invention provide immediate access to determining the status of the DNA-PK activity in living cells. The disclosures include methods for identifying agents that specifically alter the activity of this critical cellular enzyme.
Developmental Status: Reagents and materials for this assay have been developed. Methods for monitoring the enzyme activity in living cells are available through this technology.
Inventors: Carl W. Anderson and Margery A. Connelly
Patent Status: U. S. Patent 6,803,203
License Status: Available on a negotiable basis.
Literature References: Sakaguchi, K., et al. (1997) Biochemistry 36 10117-10124; Connelly, M. A., et al. (1996) Gene 175, 271-273; Sakamoto, H., et al. (1996) Intl=l. J. of Peptide and Protein Res. 48, 429-442.