Amyloid-beta peptide affects the oxygen dependence of erythrocyte metabolism: A role for caspase 3

被引:30
作者
Clementi, M. Elisabetta
Giardina, Bruno
Colucci, Deborah
Galtieri, Antonio
Misiti, Francesco
机构
[1] Univ Cassino, Dept Hlth & Motor Sci, I-03043 Cassino, FR, Italy
[2] Catholic Univ, Sch Med, Biochem & Clin Biochem Inst, I-00168 Rome, Italy
[3] CNR, ICRM, I-00168 Rome, Italy
[4] Univ Messina, Dept Organ & Biol Chem, I-98100 Messina, Italy
关键词
band; 3; pentose pathway; erythrocyte; caspase; amyloid-beta peptide;
D O I
10.1016/j.biocel.2006.11.013
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
Human erythrocyte metabolism is modulated by the cell oxygenation state. Among other mechanisms, competition of deoxyhemoglobin and some glycolytic enzymes for the cytoplasmic domain of band 3 is probably involved in modulation. This metabolic modulation is connected to variations in intracellular NADPH and ATP levels as a function of the oxygenation state of the cell, and, consequently, it should have physiologic relevance. The present study investigates the effect of amyloid-beta peptide exposure on this metabolic modulation and its relationship with the activity of erythrocyte caspase 3. Metabolic differences between erythrocytes incubated at high and low oxygen saturation disappear following to 24 h exposure to amyloid-beta peptide. Western blotting analysis shows that caspase 3 is concurrently activated. Pre-incubation of amyloid-beta peptide-treated erythrocytes with a specific inhibitor of caspase 3, partially restores the oxygen-dependent modulation. This finding suggests that human erythrocytes following to exposure to amyloid-beta peptide show it complete loss of the oxygen-dependent metabolic modulation, which is partially restored by caspase 3 inhibitor-treatment. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码:727 / 735
页数:9
相关论文
共 52 条
[1]   Erythrocyte signal transduction pathways, their oxygenation dependence and functional significance [J].
Barvitenko, NN ;
Adragna, NC ;
Weber, RE .
CELLULAR PHYSIOLOGY AND BIOCHEMISTRY, 2005, 15 (1-4) :1-18
[2]  
BENNETT V, 1980, J BIOL CHEM, V255, P6424
[3]  
Beutler E., 1975, A manuel of biochemical methods, V2nded
[4]   RED BLOOD-CELL ABNORMALITIES IN ALZHEIMER-DISEASE [J].
BLASS, JP ;
HANIN, I ;
BARCLAY, L ;
KOPP, U ;
REDING, MJ .
JOURNAL OF THE AMERICAN GERIATRICS SOCIETY, 1985, 33 (06) :401-405
[5]   ERYTHROCYTE-MEMBRANE CHARACTERISTICS INDICATE ABNORMAL CELLULAR AGING IN PATIENTS WITH ALZHEIMERS-DISEASE [J].
BOSMAN, GJCGM ;
BARTHOLOMEUS, IGP ;
DEMAN, AJM ;
VANKALMTHOUT, PJC ;
DEGRIP, WJ .
NEUROBIOLOGY OF AGING, 1991, 12 (01) :13-18
[6]   Erythrocyte aging: A more than superficial resemblance to apoptosis? [J].
Bosman, GJCGM ;
Willekens, FLA ;
Werre, JM .
CELLULAR PHYSIOLOGY AND BIOCHEMISTRY, 2005, 16 (1-3) :1-8
[7]  
BUTTERFIELD DA, 1997, CHEM RES TOXICOL, V10, P56
[8]   PLATELETS ARE THE PRIMARY SOURCE OF AMYLOID BETA-PEPTIDE IN HUMAN BLOOD [J].
CHEN, M ;
INESTROSA, NC ;
ROSS, GS ;
FERNANDEZ, HL .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1995, 213 (01) :96-103
[9]   Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3 [J].
Chu, Haiyan ;
Low, Philip S. .
BIOCHEMICAL JOURNAL, 2006, 400 :143-151
[10]   Methionine 35 oxidation reduces toxic effects of the amyloid β-protein fragment (31-35) on human red blood cell [J].
Clementi, ME ;
Martorana, GE ;
Pezzotti, M ;
Giardina, B ;
Misiti, F .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2004, 36 (10) :2066-2076