An analysis of the characterization of the CYP2D protein from human brain cerebellum.
Written in 2005; 14,400 words; 0 sources; APA; $ 249.95
Paper Summary:
The CYP2D protein in the human brain is expressed as CYP2D6 in liver and is known to metabolize a variety of drugs such as psychoactive, antihypertensives, and environmental toxins. Every person has a unique rate of metabolism. Metabolic rates in children are particularly susceptible to environmental toxicants which affect the way in which their systems absorb, distribute, metabolize and excrete chemicals. To date, knowledge in characterization of CYP proteins has been limited to immunoblotting, RT-PCR, immunohistochemistry and so forth; therefore, this paper investigates:
1) What kind of CYP2D protein is present in brain with modern proteomic tools;
2) Whether, CYP2D6 is the same as liver CYP2D6; and
3) If CYP2D7 is present, can CYP2D6 polymorphism be found in the brain?
To answer these questions, this study uses a one-step method of isolation of protein by immunoprecipitation followed by its identification using 2D-blots, nanospray LCMS, immunoblots and immunohistochemistry.
Table of Contents
Introduction
Problem Statement
Hypothesis
Rationale
Literature Review
Results
Discussion
Conclusion
References
Appendix
From the Paper:
"The most promising area of pharmacogenetic research today may be in providing patients with customized treatments for specific cancer types. For instance, Christensen points out that Herceptin and Gleevec are two drugs that affect only cancerous tissues expressing certain genes. In the case of Herceptin, it binds to a protein that stimulates rapid tumor growth; this substance has been found to be present in excess in approximately 33 percent of breast cancers. Prior to prescribing the drug to their patients, doctors can now test how many copies of the gene for HER2/neu, which encodes this protein, are present or measure concentrations of the protein itself. Patients who do not have the excess HER2/neu protein or its gene would therefore not receive the drug. Gleevec takes advantage of a particular enzyme that is mutated in a few rare cancers, such as chronic myeloid leukemia. When Gleevec blocks the mutated enzyme, growth of the cancer cells stops; however, the drug has minimal effects on healthy dividing cells (Christensen, 2002)."
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