On the evolution of erythrocyte programmed cell death:: apoptosis of Rana esculenta nucleated red blood cells involves cysteine proteinase activation and mitochondrion permeabilization

被引:11
作者
Bratosin, D
Estaquier, J
Slomianny, C
Tissier, JP
Quatannens, B
Bulai, T
Mitrofan, L
Marinescu, A
Trandaburu, L
Ameisen, JC
Montreuil, J [1 ]
机构
[1] Univ Lille 1, Chim Biol Lab, UMR USTL CNRS 8576, F-59655 Villeneuve Dascq, France
[2] Inst Natl Cercetare Dezvoltare Pentru Stiinte Bio, Bucharest 77748, Romania
[3] Inst Pasteur, Unite Physiopathol Infect Lentivirales, F-75015 Paris, France
[4] Univ Lille 1, Lab Physiol Cellulaire, F-59655 Villeneuve Dascq, France
[5] INRA Stn, F-59650 Villeneuve Dascq, France
[6] Inst Biol Lille, CNRS, UMR 8526, F-59019 Lille, France
[7] Alexandru Ioan Cuza Univ, Fac Chim, Iasi 6600, Romania
[8] Inst Biol Acad Romane, Bucharest, Romania
[9] Univ Paris 07, CHU Bichat, IFR 02, INSERM,EMI U9922, F-75018 Paris, France
关键词
apoptosis; cell death; red blood cells; mitochondria; calpain; caspase; amphibians;
D O I
10.1016/j.biochi.2004.03.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Batracian Rana esculenta erythrocytes cell death induced by either calcium influx, or staurosporine, involves typical apoptotic phenotype. Our data reveal: (i) a drastic modification of the cell morphology with loss of the ellipsoidal form as assessed by phase contrast microscopy and scanning electron microscopy; (ii) an exposure of the phosphatidylserine residues in the outer leaflet of the cell membrane; (iii) a caspase-3-like activity; (iv) a mitochondrial membrane potential (DeltaPsim) loss; and (v) a chromatin condensation and fragmentation. Erythrocyte chromatin condensation and fragmentation are prevented by caspase and calpain peptide inhibitors. These inhibitors also prevent DeltaPsim loss supporting the idea that mitochondria is a central sensor for Rana erythrocytes cell death. Our observations highlight the conservation of the programmed cell death machinery in erythrocytes across kingdom. (C) 2004 Elsevier SAS. All rights reserved.
引用
收藏
页码:183 / 192
页数:10
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