کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9028799 | 1130261 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Possible mechanisms underlying copper-induced damage in biological membranes leading to cellular toxicity
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کلمات کلیدی
DTNBN-ethyl-maleimidep-NitroanisoleDNBMDATTMTBATBARSPNAGSHTCA1-chloro-2,4-dinitrobenzene - 1-کلرو-2،4-دینیتروبنزن2-Thiobarbituric acid - 2-تیوباربیتوریک اسیدEDTA - اتیلن دی آمین تترا استیک اسید trichloroacetic acid - اسید ترشکلراکتیکThiols - تیولBiological membranes - غشاهای بیولوژیکmalondialdehyde - مالون دی آلدهیدCopper toxicity - مسمومیت مسthiobarbituric acid reactive substances - مواد واکنش پذیر اسید تیوباربیتوریکNEM - نهGlutathione - گلوتاتیون
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم محیط زیست
بهداشت، سم شناسی و جهش زایی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
It is generally accepted that copper toxicity is a consequence of the generation of reactive oxygen species (ROS) by copper ions via Fenton or Haber-Weiss reactions. Copper ions display high affinity for thiol and amino groups occurring in proteins. Thus, specialized proteins containing clusters of these groups transport and store copper ions, hampering their potential toxicity. This mechanism, however, may be overwhelmed under copper overloading conditions, in which copper ions may bind to thiol groups occurring in proteins non-related to copper metabolism. In this study, we propose that indiscriminate copper binding may lead to damaging consequences to protein structure, modifying their biological functions. Therefore, we treated liver subcellular membrane fractions, including microsomes, with Cu2+ ions either alone or in the presence of ascorbate (Cu2+/ascorbate); we then assayed both copper-binding to membranes, and microsomal cytochrome P450 oxidative system and GSH-transferase activities. All assayed sub-cellular membrane fractions treated with Cu2+ alone displayed Cu2+-binding, which was significantly increased in the presence of Zn2+, Hg2+, Cd2+, Ag+1 and As3+. Treatment of microsomes with Cu2+ in the μM range decreased the microsomal thiol content; in the presence of ascorbate, Cu2+ added in the nM concentrations range induced a significant microsomal lipoperoxidation; noteworthy, increasing Cu2+ concentration to â¥50 μM led to non-detectable lipoperoxidation levels. On the other hand, μM Cu2+ led to the inhibition of the enzymatic activities tested to the same extent in either presence or absence of ascorbate. We discuss the possible significance of indiscriminate copper binding to thiol proteins as a possible mechanism underlying copper-induced toxicity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemico-Biological Interactions - Volume 151, Issue 2, 15 January 2005, Pages 71-82
Journal: Chemico-Biological Interactions - Volume 151, Issue 2, 15 January 2005, Pages 71-82
نویسندگان
MarÃa Eugenia Letelier, Ana MarÃa Lepe, Mario Faúndez, Julia Salazar, Rigoberto MarÃn, Paula Aracena, Hernán Speisky,