**9. References**


<sup>\*</sup> Corresponding Authors

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56 Dehydrogenases

**Author details** 

Paul M. Bingham\*

**9. References** 

 \*

Cancer cell 11: 37-51.

Corresponding Authors

**Acknowledgement** 

metabolism relative to its normal cell condition.

and Zuzana Zachar

*Cornerstone Pharmaceuticals, 1 Duncan Drive, Cranbury, NJ* 

*Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY* 

Pharmaceuticals, Inc. the clinical developer of thioctoids, including CPI-613.

and Are Potent Anticancer Agents *In Vivo*. J. mol. med. 89: 1137-1148.

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complexes is strongly controlled by the dynamic status of their lipoate residues, reflecting a moment-to-moment polling of the mitochondrial matrix. Finally, evidence and theory also indicate that some or most of these lipoate-dependent regulatory processes are very significantly altered in support of the substantial repurposing of tumor cell mitochondrial

Collectively, these results indicate that the regulatory reprogramming of these dehydrogenases may represent a target-rich environment for developing new anti-tumor drugs that have the crucial properties that may be required to impart new efficacy to cancer chemotherapy – targets that are both essential to the malignant condition and nonredundant in their function. The preclinical and early clinical properties of agents directed at

This work was largely supported by Cornerstone Pharmaceuticals, Inc. with additional support from the Carol M. Baldwin Breast Cancer Research Fund; Stony Brook University Center for Biotechnology, and from the Department of Biochemistry and Cell Biology and the School of Medicine at Stony Brook University. We are grateful to many colleagues for helpful discussions, including Robert Shorr, Robert Rodriguez, King Lee, Shawn D. Stuart, Sunita Gupta, and Alexandra Schauble. Both authors have a financial stake in Cornerstone

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**Section 2** 

**Dehydrogenases and Some Diseases** 

**Dehydrogenases and Some Diseases** 

62 Dehydrogenases

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**Chapter 4** 

© 2012 Allahverdiyev et al., licensee InTech. This is an open access chapter distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

© 2012 The Author(s). Licensee InTech. This chapter is distributed under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution,

**Glucose-6-Phosphate Dehydrogenase** 

**Primaquine-Induced Hemolysis** *in vitro*

Adil M. Allahverdiyev, Malahat Bagirova, Serhat Elcicek, Rabia Cakir Koc, Sezen Canim Ates, Serap Yesilkir Baydar, Serkan Yaman, Emrah Sefik Abamor and Olga Nehir Oztel

Additional information is available at the end of the chapter

http://dx.doi.org/10.5772/48403

**1. Introduction** 

1989).

**Deficiency and Malaria: A Method to Detect** 

Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common enzymopathological disease in humans. This disease is described as a widespread, heritable, X-chromosome linked abnormality (Reclos*, et al.*, 2000). It is estimated that it affects approximately 400 million people worldwide (Noori-Daloii*, et al.*, 2004). This disease is seen most frequently in approximately all of Africa, Asia, and the countries near the Mediterranean Sea (Frank, 2005). G6PD enzyme was demonstrated to play an active role in survival of erythrocytes. It is known that in the pentose phosphate pathway of erythrocytes, glucose-6 phosphate dehydrogenase (G6PD) enzyme provides the production of NADPH and GSH. GSH, produced by pentose phosphate pathway can react with H2O2 and reduce it to H2O. This prevents the generation of oxidative stress within red blood cells; oxidative stress can be induced in erythrocytes whose G6PD enzymes are deficient. In this situation, GSH is not produced and H2O2 is not reduced to H2O, leading to oxidative stress and hemolysis. This is the only mechanism available for the erythrocyte in order to generate reducing equivalence, therefore making it essential for the survival of erythrocytes. In individuals whose G6PD enzyme is deficient, different kinds of hemolysis from mild to severe are seen bound to differences in variants of the disease (Beutler, 1983, Luzzatto,

In epidemiological studies, it was shown that the prevalence of G6PD deficiency significantly related to malaria. Malaria is known as a parasitic disease that affects 300-500 million people all over the world. It is widespread in tropical and subtropical regions of Asia, Africa and American continents. Five different types of *Plasmodium* species—*P.* 

and reproduction in any medium, provided the original work is properly cited.
