Increased release of free Fe ions in human erythrocytes during aging in the circulation

被引:13
作者
Ando, K [1 ]
Ogawa, K [1 ]
Misaki, S [1 ]
Kikugawa, K [1 ]
机构
[1] Tokyo Univ Pharm & Life Sci, Sch Pharm, Hachioji, Tokyo 1920392, Japan
关键词
aging; bleomycin; desferrioxamine; erythrocyte; Fe ion; hemoglobin; oxidative damage;
D O I
10.1080/1071576021000028307
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
We investigated whether free Fe ions were released in erythrocytes during aging process in the circulation. Young and senescent erythrocytes were separated from freshly drawn human blood by Percoll density gradient centrifugation. Two different methods were employed for determination of free Fe ions in erythrocytes, desferrioxamine (DFO) method and bleomycin method. DFO-chelatable Fe ions were detected in whole erythrocytes from 2 donors, and the DFO-chelatable free Fe ion levels in senescent erythrocytes were higher than those in young erythrocytes. Bleomycin-sensitive Fe ions, which was rather lower than DFO-chelatable Fe ions, were also detected in whole erythrocytes from 5 donors, and the free Fe ion levels in senescent erythrocytes were also higher than those in young erythrocytes. Free Fe ions may be derived from oxidative damage of hemoglobin, because treatment of whole erythrocytes or purified oxyhemoglobin with hydrogen peroxide gave increased free Fe ions. The results indicated that free Fe ions were released from erythrocytes during aging process in the circulation. Released free Fe ions would promote oxidative damages of the cells during aging process.
引用
收藏
页码:1079 / 1084
页数:6
相关论文
共 30 条
[1]   Membrane proteins of human erythrocytes are modified by advanced glycation end products during aging in the circulation [J].
Ando, K ;
Beppu, M ;
Kikugawa, K ;
Nagai, R ;
Horiuchi, S .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 258 (01) :123-127
[2]  
ANDO K, 1995, BIOL PHARM BULL, V18, P659
[3]  
ANDO K, 1994, J BIOL CHEM, V269, P19394
[4]   Induction of band 3 aggregation in erythrocytes results in anti-band 3 autoantibody binding to the carbohydrate epitopes of band 3 [J].
Ando, K ;
Kikugawa, K ;
Beppu, M .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1997, 339 (01) :250-257
[5]   AGING OF THE ERYTHROCYTE .12. PROTEIN-COMPOSITION OF THE MEMBRANE [J].
BARTOSZ, G ;
SOSZYNSKI, M ;
WASILEWSKI, A .
MECHANISMS OF AGEING AND DEVELOPMENT, 1982, 19 (01) :45-52
[6]  
BEPPU M, 1990, J BIOL CHEM, V265, P3226
[7]   The molecular pathobiology of cell membrane iron: The sickle red cell as a model [J].
Browne, P ;
Shalev, O ;
Hebbel, RP .
FREE RADICAL BIOLOGY AND MEDICINE, 1998, 24 (06) :1040-1048
[8]  
CASEY JR, 1991, J BIOL CHEM, V266, P15726
[9]   Iron release in erythrocytes from patients with β-thalassemia [J].
Ciccoli, L ;
Signorini, C ;
Scarano, C ;
Rossi, V ;
Bambagioni, S ;
Ferrali, M ;
Comporti, M .
FREE RADICAL RESEARCH, 1999, 30 (05) :407-413
[10]   Oxidatively damaged erythrocytes are recognized by membrane proteins of macrophages [J].
Eda, S ;
Kikugawa, K ;
Beppu, M .
FREE RADICAL RESEARCH, 1997, 27 (01) :23-30