Expression of mortalin in patients with chronic atrial fibrillation

被引：27
作者：
Kirmanoglou, K [1 ]
Hannekum, A [1 ]
Schäfler, AE [1 ]
机构：
[1] Univ Ulm, Dept Cardiac Surg, D-89075 Ulm, Germany
来源：
BASIC RESEARCH IN CARDIOLOGY | 2004年 / 99卷 / 06期
关键词：
mortalin; atrial fibrillation; heat shock proteins; actin; western blot;
D O I：
10.1007/s00395-004-0477-4
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
Background In myocardium of patients with chronic atrial fibrillation (AF) the expression of the mitochondrial heat shock proteins HSP60 and HSP10 is increased. They are responsible for folding and translocation of proteins inside the mitochondria. Import of these proteins is accomplished by mortalin. The aim of our study was to investigate if the expression of the heat shock protein mortalin is also increased in patients with AF. Methods Right atrial samples from 18 patients undergoing elective cardiac surgery were excised and immediately frozen in liquid nitrogen: 8 patients had chronic AF (greater than or equal to3 month) and 10 patients were in sinus rhythm (SR). Mortalin was determined by SDS-PAGE, Western blot and quantified by optical densitometry. Results In myocardial samples from patients with chronic AF we found a more than 2-fold increase in mortalin expression. Conclusions The increased expression of mortalin may represent an adaptive heat shock response to restore cellular homeostasis.
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收藏
页码：404 / 408
页数：5
相关论文
共 24 条
[1]  
Allen SL, 2002, COMP LITERATURE, V54, P2
[2]   PBP74, A NEW MEMBER OF THE MAMMALIAN 70-KDA HEAT-SHOCK PROTEIN FAMILY, IS A MITOCHONDRIAL PROTEIN [J].
DAHLSEID, JN ;
LILL, R ;
GREEN, JM ;
XU, XX ;
QIU, Y ;
PIERCE, SK .
MOLECULAR BIOLOGY OF THE CELL, 1994, 5 (11) :1265-1275
[3]   Remodeling of cardiomyocyte ion channels in human atrial fibrillation [J].
Dobrev, D ;
Ravens, U .
BASIC RESEARCH IN CARDIOLOGY, 2003, 98 (03) :137-148
[4]   Mitochondrial import driving forces: Enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins [J].
Geissler, A ;
Rassow, J ;
Pfanner, N ;
Voos, W .
MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (20) :7097-7104
[5]   STRUCTURE AND FUNCTION OF BACTERIAL SIGMA FACTORS [J].
HELMANN, JD ;
CHAMBERLIN, MJ .
ANNUAL REVIEW OF BIOCHEMISTRY, 1988, 57 :839-872
[6]   Effect of atrial dilatation on electrophysiologic properties and inducibility of atrial fibrillation [J].
Huang, JL ;
Tai, CT ;
Chen, JT ;
Ting, CT ;
Chen, YT ;
Chang, MS ;
Chen, SA .
BASIC RESEARCH IN CARDIOLOGY, 2003, 98 (01) :16-24
[7]   Overexpressed mortalin (mot-2)/mthsp70/GRP75 and hTERT cooperate to extend the in vitro lifespan of human fibroblasts [J].
Kaul, SC ;
Yaguchi, T ;
Taira, K ;
Reddel, RR ;
Wadhwa, R .
EXPERIMENTAL CELL RESEARCH, 2003, 286 (01) :96-101
[8]  
Kawai A, 2001, J CELL SCI, V114, P3565
[9]   ANTIFOLDING ACTIVITY OF HSP60 COUPLES PROTEIN IMPORT INTO THE MITOCHONDRIAL MATRIX WITH EXPORT TO THE INTERMEMBRANE SPACE [J].
KOLL, H ;
GUIARD, B ;
RASSOW, J ;
OSTERMANN, J ;
HORWICH, AL ;
NEUPERT, W ;
HARTL, FU .
CELL, 1992, 68 (06) :1163-1175
[10]   Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role [J].
Krimmer, T ;
Rassow, J ;
Kunau, WH ;
Voos, W ;
Pfanner, N .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (16) :5879-5887
123