(gst-Pi) in breast carcinoma

نویسنده

  • MohaMad Nidal Khabaz
چکیده

Breast carcinoma is the most common cancer and cause of death among females worldwide, including Jordan. The risk factors for breast carcinoma are linked to DNA mutation and failure of DNA repair or detoxification systems. Identification of susceptibility factors that predispose individuals to breast carcinoma if they are exposed to particular environmental agents might give further insight into the etiology of this malignancy. The glutathione S-transferase (GST) enzyme family detoxifies carcinogenic compounds. Several genes that code for these enzymes are polymorphic, with particular genotypes previously shown to confer an increased carcinoma risk. The present study investigates GST-pi polymorphism in 100-tissue samples previously diagnosed as breast carcinoma, and in 48 non-cancer age-matched breast tissues, using the restriction fragment length polymorphism (RFLP) method for the polymerase chain reaction (PCR) product. Among breast cancer cases, 58%, 40% and 2% were homozygous (Ile/Ile), heterozygous (Ile/Val) and homozygous (Val/Val) respectively. In the control group, 58%, 37.5% and 4.2% were homozygous (Ile/Ile), heterozygous (Ile/Val), and homozygous (Val/Val) respectively. Our results did not support the involvement of GST-pi gene polymorphism in susceptibility to breast carcinoma in the tested North Jordanian female population.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors.

The development of multidrug resistance in MCF-7 human breast cancer cells and the acquisition of broad resistance to xenobiotics in rat hyperplastic nodules are both associated with increased P-glycoprotein (mdr) gene expression as well as changes in activities of intracellular detoxication enzymes; among these changes is a significant increase in the activity of the anionic isozyme of glutath...

متن کامل

Glutathione transferase activity and isoenzyme composition in primary human breast cancers.

The human glutathione transferases (GSTs) are a multigene family of detoxication enzymes with patterns of expression that are both tissue specific and genetically determined. Changes in the levels of one or more GST isoenzymes have been associated with the development of anticancer drug resistance in cultured cell lines. In this study, total GST activity and GST isoenzyme composition have been ...

متن کامل

Brostallicin, a novel anticancer agent whose activity is enhanced upon binding to glutathione.

Brostallicin (PNU-166196) is a synthetic alpha-bromoacrylic, second-generation DNA minor groove binder structurally related to distamycin A, presently in Phase II trials in Europe and the United States. The compound shows broad antitumor activity in preclinical models and dramatically reduced in vitro myelotoxicity in human hematopoietic progenitor cells compared with that of other minor groove...

متن کامل

Glutathione-S-transferase-pi (GST-pi) expression in renal cell carcinoma

Multidrug resistance correlates with unfavourable treatment outcomes in numerous cancers including renal cell carcinoma. The expression and clinical relevance of Glutathione-S-transferase-pi (GST-pi), a multidrug resistance factor, in kidney tumors remain controversial. We analyzed the expression of GST-pi in 60 formalin-fixed, paraffin-embedded renal cell carcinoma samples by immunohistochemis...

متن کامل

Glutathione S-transferases in human liver cancer.

An immunohistochemical study of glutathione S-transferase (GST) expression in hepatocellular carcinoma and cholangiocarcinoma is described. Unlike most animal models of hepatic malignancy pi class GST was not consistently overexpressed in hepatocellular carcinoma. This tumour type either predominantly expressed alpha class GST or failed to express GST. By contrast, cholangiocarcinoma always exp...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2014