کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10739126 | 1046862 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Catalytically inactive heme oxygenase-2 mutant is cytoprotective
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کلمات کلیدی
HEKNADPHPBSDNPH2,4-dinitrophenylhydrazine - 2،4-dinitrophenylhydrazineMTT - MTTHydrogen peroxide - آب اکسیژنهIron - آهنCPR - احیای قلبی ریویBilirubin - بیلیروبینcytochrome P450 reductase - سیتوکروم P450 ردوکتازPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریcarbon monoxide - منوکسیدکربنwildtype - نوع وحشیnicotinamide adenine dinucleotide phosphate - نیکوتین آمید adenine dinucleotide phosphateheme oxygenase - همگام اکسژنازHemin - همینhuman embryonic kidney - کلیه جنین انسان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Catalytically inactive heme oxygenase-2 mutant is cytoprotective Catalytically inactive heme oxygenase-2 mutant is cytoprotective](/preview/png/10739126.png)
چکیده انگلیسی
Heme oxygenase (HO) catalyzes the rate-limiting step in heme degradation, producing iron, carbon monoxide, and bilirubin/biliverdin. HO consists of two isozymes: HO-1, which is an oxidative stress-response protein, and HO-2, which is constitutively expressed. HO-2 accounts for most HO activity within the nervous system. Its posttranslational modifications and/or interactions with other proteins make HO-2 a unique regulator of cellular homeostasis. Our previous results revealed that brain infarct volume was enlarged in HO-2 knockout mice. A similar neuroprotective role of HO-2 was shown using primary cortical neurons. To better understand the neuroprotective mechanism of HO-2, we used a catalytically inactive mutant, HO-2H45A, and investigated its cellular effects in response to hemin and hydrogen peroxide-induced cytotoxicity. We observed that HO-2WT overexpression in the HEK293 cell lines became less sensitive to hemin, whereas the inactive mutant HO-2H45A was more sensitive to hemin as compared to control. Interestingly, HO-2WT- and HO-2H45A-overexpressing cells were both protected against H2O2-induced oxidative stress and had less oxidatively modified proteins as compared to control cells. These data indicate that when HO-2 cannot metabolize the prooxidant heme, more cytotoxicity is found, whereas, interestingly, the catalytically inactive HO-2H45A was also able to protect cells against oxidative stress injury. These results suggest the multiplicity of action of the HO-2 protein itself.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 39, Issue 4, 15 August 2005, Pages 558-564
Journal: Free Radical Biology and Medicine - Volume 39, Issue 4, 15 August 2005, Pages 558-564
نویسندگان
Yun-Sook Kim, Sylvain Doré,