Overexpression of erythrocyte glutathione S-transferase in uremia and dialysis.

نویسندگان

  • F Galli
  • S Rovidati
  • S Benedetti
  • U Buoncristiani
  • C Covarelli
  • A Floridi
  • F Canestrari
چکیده

BACKGROUND Overexpression of glutathione S-transferase (GST; EC 2.5. 1.18) has been documented in the erythrocytes of patients with chronic renal failure, and this event may well be of relevance from a clinical standpoint. In fact, it could serve as a marker of uremic toxicity overall, which can contribute to impair the function and survival of the erythrocytes. However, the biochemical details of this phenomenon are poorly understood. METHODS In this study, we characterized the expression of GST in erythrocytes of 118 uremic patients under different clinical conditions. The mechanisms responsible for the regulation of protein expression and enzyme activity were investigated in light of different dialysis approaches, oxidative stress, uremic toxins, erythrocyte age, and erythropoietin (EPO) supplementation. RESULTS Mean GST activity in uremic patients was highly overexpressed with respect to controls, and this phenomenon was exclusively attributable to an increased expression of GST. Overexpression of GST did not appear to be dependent on oxidative stress and was not influenced by vitamin E supplementation. In the same manner, both erythrocyte age and EPO supplementation apparently did not interfere with the GST concentrations, which were the same in controls and patients. Preliminary experiments suggested that high-molecular weight or protein-bound toxins could play some role in the overexpression of GST. CONCLUSIONS GST expression may be a useful marker for the individual accumulation of uremic toxins as well as of the efficiency of new dialysis strategies in removing them.

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

Binding of heme by glutathione S-transferase: a possible role of the erythrocyte enzyme.

Human erythrocyte glutathione S-transferase activity is inhibited, probably competitively, by hemin with a Ki of 10(-7) M. It is postulated that glutathione S-transferase functions physiologically as a hemin-binding and/or transport protein in developing erythroid cells.

متن کامل

CHANGES IN GLUTATHIONE S-TRANSFERASE ACTIVITY AND ZEARALENONE CONTENT IN SUSCEPTIBLE AND TOLERANT WHEAT HEADS INOCULATED WITH FUSARIUM GRAMINEARUM, THE CAUSAL AGENT OF FUSARIUM HEAD SCAB

Glutathione S-transferase (GST) activity pattern was determined in tolerant (cv. Sumai#3) and susceptible (cv. Falat) wheat heads inoculated with Fusarium graminearum, the causal agent of head scab disease (FHB), during various developmental stages. GST specific activity exhibited a transient pattern in Sumai#3 reaching a maximum level at the milk stage and declining thereafter. GST level in Su...

متن کامل

Expression of cytochrome P450 and glutathione S-transferase in human bone marrow mesenchymal stem cells

Currently several studies are being carried out on various properties of mesenchymal stem cells (MSCs)however there are a few investigations about drug metabolizing properties of these cells. The aim of thisstudy was to measure the key factors involved in drug metabolism in human bone marrow MSCs. For thispurpose, cellular glutathione (GSH), glutathione Stransferase (GSTs) and...

متن کامل

بررسی پلی‌مورفیسم ژنی ایزوآنزیم‌های GSTM1 و GSTP1 و فعالیت آنزیم گلوتاتیون S-ترانسفراز: مردان نابارور ایرانی

Background: Pi-GST and Mu-GST are subclasses of glutathione S-transferase that present on human sperm surface and play an important role against oxidative stress. Therefore, any defects in the enzyme activity may be associated with male infertility.In this study the polymorphisms of GSTM1 and GSTP1 in association with enzyme activity and sperm parameters were studied. Methods: This case-contro...

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:
  • Clinical chemistry

دوره 45 10  شماره 

صفحات  -

تاریخ انتشار 1999