Correlation of Reduced Glutathione with Brest Cancer Using High Performance Liquid Chromatography
Journal Title: Biomedical Journal of Scientific & Technical Research (BJSTR) - Year 2017, Vol 1, Issue 5
Abstract
Cancer is a group of diseases that cause cells in the body to change and grow out of control. Most types of cancer cells eventually form a lump or mass called a tumor, and are named after the part of the body where the tumor originates. Breast cancer begins in the breast tissue that is made up of glands for milk production, called lobules, and the ducts that connect the lobules to the nipple. The remainder of the breast is made up of fatty, connective, and lymphatic tissues [1]. Glutathione (GSH) is a tripeptide of glycine, cysteine and glutamic acid that is found in high concentration intracellularly, being the most abundant low molecular mass thiol [2]. Synthesis of GSH requires the consecutive action of two enzymes, first glutamate-cysteine ligase (GCLC) that conjugates glutamic acid and cysteine forming gamma-glutamyl cysteine. This compound containing cysteine with a sulfhydryl group (SH) is responsible for the antioxidant activity of GSH. The second reaction is the binding of gamma glutamyl cysteine with glycine by the enzyme glutathione synthetase (GSS), giving rise to the tripeptide gamma glutamyl cysteine glycine-glutathione. When there is an excessive production of reactive oxidative species (ROS), the antioxidant defense system is triggered, which is of great importance in the physiopathology of diverse cancer types, including breast cancer [3,4]. The consequence of this process is the loss of cellular function and progression towards cell death. Moreover, oxidative stress leads to DNA damage and mutations in tumor suppressor genes, events that can be important in the initiation of carcinogenesis.
Authors and Affiliations
Mufeed Jalil Ewadh, Ali Mohammed Jawad, Alaa Sadiq Al awad
Keywords
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- EP ID EP571842
- DOI 10.26717/BJSTR.2017.01.000421
- Views 144
- Downloads 0
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