کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10738691 | 1046721 | 2011 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Inhibition by 4-hydroxynonenal (HNE) of Ca2+ transport by SERCA1a: Low concentrations of HNE open protein-mediated leaks in the membrane
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کلمات کلیدی
octaethylene glycol mono-n-dodecyl etherHNERNSDTNBA23187GSHEGTAC12E8DNPHHCCA4-Hydroxy-2-nonenal (HNE)PVDFTMA-DPHSERCA1aNaBH4MALDI-TOFFITCFluorescein 5-isothiocyanatepolyvinylidene-difluoride2,4-dinitrophenylhydrazine - 2،4-dinitrophenylhydrazine4-hydroxy-2-nonenal - 4-هیدروکسی-2 غیرنالBSA - BSACa2+-ATPase - Ca2 + -ATPaseCa2+ Transport - Ca2 + حمل و نقلDMSO - DMSOPCA - PCAROS - ROSbovine serum albumin - آلبومین سرم گاوα-cyano-4-hydroxycinnamic acid - اسید α-سینو-4-هیدروکسی سدیمPerchloric acid - اسید پرکلریکSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدsodium dodecyl sulphate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اکریللید سدیم دودسیل سولفاتSodium borohydride - بورو هیدرید سدیمDimethyl sulfoxide - دیمتیل سولفواکسیدSarcoplasmic reticulum - رتیکولوم سارکوپلاسمیکATPase activity - فعالیت ATPasePassive permeability - نفوذ پذیری غیر فعالreduced glutathione - کاهش گلوتاتیونcalcimycin - کلسیمایسینreactive nitrogen species - گونه های واکنش پذیر نیتروژنReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Inhibition by 4-hydroxynonenal (HNE) of Ca2+ transport by SERCA1a: Low concentrations of HNE open protein-mediated leaks in the membrane Inhibition by 4-hydroxynonenal (HNE) of Ca2+ transport by SERCA1a: Low concentrations of HNE open protein-mediated leaks in the membrane](/preview/png/10738691.png)
چکیده انگلیسی
Exposure of sarcoplasmic reticulum membranes to 4-hydroxy-2-nonenal (HNE) resulted in inhibition of the maximal ATPase activity and Ca2+ transport ability of SERCA1a, the Ca2+ pump in these membranes. The concomitant presence of ATP significantly protected SERCA1a ATPase activity from inhibition. ATP binding and phosphoenzyme formation from ATP were reduced after treatment with HNE, whereas Ca2+ binding to the high affinity sites was altered to a lower extent. HNE reacted with SH groups, some of which were identified by MALDI-TOF mass spectrometry, and competition studies with FITC indicated that HNE also reacted with Lys515 within the nucleotide binding pocket of SERCA1a. A remarkable fact was that both the steady-state ability of SR vesicles to sequester Ca2+ as well as the ATPase activity of SR membranes in the absence of added ionophore or detergent were sensitive to concentrations of HNE much smaller than those which affected the maximal ATPase activity of SERCA1a. This was due to increase in the passive permeability to Ca2+ of HNE-treated SR vesicles, an increase in permeability which did not arise from alteration of the lipid component of these vesicles. Judging from immunodetection with an anti-HNE antibody, this HNE-dependent increase in permeability probably arose from modification of proteins of about 150-170Â kDa, present in very low abundance in longitudinal SR membranes (and in slightly larger abundance in SR terminal cisternae). HNE-induced promotion, via these proteins, of Ca2+ leakage pathways, might be involved in the general toxic effects of HNE.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 50, Issue 11, 1 June 2011, Pages 1700-1713
Journal: Free Radical Biology and Medicine - Volume 50, Issue 11, 1 June 2011, Pages 1700-1713
نویسندگان
MarÃa P. Hortigón-Vinagre, Solenne Chardonnet, Cédric Montigny, Yolanda Gutiérrez-MartÃn, Philippe Champeil, Fernando Henao,