Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage

被引:84
作者
Reeder, BJ
Sharpe, MA
Kay, AD
Kerr, M
Moore, K
Wilson, MT
机构
[1] Univ Essex, Dept Biol Sci, Colchester CO4 3SQ, Essex, England
[2] Inst Neurol, Dept Neurochem, London WC1N 3BG, England
[3] So Gen Hosp, Dept Neurosurg, Inst Neurol Sci, Glasgow G53 4TF, Lanark, Scotland
[4] Univ Pittsburgh, Dept Neurosurg, Pittsburgh, PA 15260 USA
[5] UCL Royal Free & Univ Coll, Sch Med, Dept Med, London NW3 2QG, England
关键词
cerebrospinal fluid; haem proteins; haem-protein cross-linking;
D O I
10.1042/bst0300745
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
Haemolytic events, such as those following rhabdomyolysis and subarachnoid haemorrhage, often result in pathological complications such as vasoconstriction. Haem-protein cross-linked myoglobin and haemoglobin are generated by ferric-ferryl redox cycling, and thus can be used as markers of oxidative stress. We have found haem-protein cross-linked myoglobin in the urine of patients suffering from rhabdomyolysis and haem-protein cross-linked haemoglobin in the cerebrospinal fluid of patients following subarachnoid haemorrhage. These findings provide strong evidence that these respiratory haem proteins can be involved in powerful oxidation processes in vivo. We have previously proposed that these oxidation processes in rhabdomyolysis include the formation of potent vasoconstrictor molecules, generated by the myoglobin-catalysed oxidation of membranes, inducing nephrotoxicity and renal failure. Haem-protein cross-linked haemoglobin in cerebrospinal fluid suggests that a similar mechanism of lipid oxidation is present and that this may provide a mechanistic basis for the delayed vasospasm that follows subarachnold haemorrhage.
引用
收藏
页码:745 / 748
页数:4
相关论文
共 14 条
[1]  
CATALANO CE, 1989, J BIOL CHEM, V264, P10534
[2]   THE ROLE OF LIPID HYDROPEROXIDES IN THE MYOGLOBIN-DEPENDENT OXIDATION OF LDL [J].
HOGG, N ;
RICEEVANS, C ;
DARLEYUSMAR, V ;
WILSON, MT ;
PAGANGA, G ;
BOURNE, L .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1994, 314 (01) :39-44
[3]   Increased lipid peroxidation in patients with rhabdomyolysis [J].
Holt, S ;
Reeder, B ;
Wilson, M ;
Harvey, S ;
Marrow, JD ;
Roberts, LJ ;
Moore, K .
LANCET, 1999, 353 (9160) :1241-1241
[4]   A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure [J].
Moore, KP ;
Holt, SG ;
Patel, RP ;
Svistunenko, DA ;
Zackert, W ;
Goodier, D ;
Reeder, BJ ;
Clozel, M ;
Anand, R ;
Cooper, CE ;
Morrow, JD ;
Wilson, MT ;
Darley-Usmar, V ;
Roberts, LJ II .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (48) :31731-31737
[5]   A SERIES OF PROSTAGLANDIN-F2-LIKE COMPOUNDS ARE PRODUCED INVIVO IN HUMANS BY A NONCYCLOOXYGENASE, FREE RADICAL-CATALYZED MECHANISM [J].
MORROW, JD ;
HILL, KE ;
BURK, RF ;
NAMMOUR, TM ;
BADR, KF ;
ROBERTS, LJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (23) :9383-9387
[6]  
Osawa Y, 1996, ADV EXP MED BIOL, V387, P37
[7]   The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxidie consumption by myoglobin: A role for the protonated ferryl species [J].
Reeder, BJ ;
Wilson, MT .
FREE RADICAL BIOLOGY AND MEDICINE, 2001, 30 (11) :1311-1318
[8]   Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin [J].
Reeder, BJ ;
Svistunenko, DA ;
Sharpe, MA ;
Wilson, MT .
BIOCHEMISTRY, 2002, 41 (01) :367-375
[9]   Formation of novel D-ring and E-ring isoprostane-like compounds (D4/E4-neuroprostanes) in vivo from docosahexaenoic acid [J].
Reich, EE ;
Zackert, WE ;
Brame, CJ ;
Chen, Y ;
Roberts, LJ ;
Hachey, DL ;
Montine, TJ ;
Morrow, JD .
BIOCHEMISTRY, 2000, 39 (09) :2376-2383
[10]   PROOXIDANT EFFECTS OF CROSS-LINKED HEMOGLOBINS EXPLORED USING LIPOSOME AND CYTOCHROME-C-OXIDASE VESICLE MODEL MEMBRANES [J].
ROGERS, MS ;
PATEL, RP ;
REEDER, BJ ;
SARTI, P ;
WILSON, MT ;
ALAYASH, AI .
BIOCHEMICAL JOURNAL, 1995, 310 :827-833