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From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
INTRODUCTION A field of inquiry may be said to have come of
age when conclusions initially viewed as remarkable or even
unbelievable are accepted as commonplace. Study of the biology of the
superoxide anion radical and of related free radicals, and the defenses
thereto, has now reached this happy state of maturity. Superoxide and
even hydroxyl radicals are now known to be produced in living systems, and elaborate systems of defense and repair, which minimize the ravages
of these reactive species, have been described. New members of the
superoxide dismutase, catalase, and peroxidase families of defensive
enzymes are being found, as are new targets that are modified by
O Measurement of O Because of the spin restriction, the univalent reduction of
O2 to O Detection and measurement of fluxes of O Another luminescent method that is misused to measure O One additional artifactual detector of O Is there any method which can reliably be used as a measure of
intracellular O Aconitase can be inactivated by oxidants other than O Oxidants from O Although O There is a mechanism pertinent to living cells, and we may call it the
in vivo Haber-Weiss reaction. It is a process in which O Mutations and Complementations of Superoxide Dismutases The primary defense against the damage that can be caused by
O Support for the free radical theory of senescence was provided by the
shortened lifespan of Drosophila with a mutational defect in
Cu,Zn-SOD (40). These flies were also hypersensitive toward paraquat
and were sterile. A curtailed lifespan was also evident in
Caenorhabditis elegans, which had only half the normal
complement of SOD (41). Mice lacking Cu,Zn-SOD appeared normal while
young but were less able to recover from axonal injury (43) and could not successfully reproduce. They also exhibited a shortened
lifespan.2 Lack of Mn-SOD imposed more
serious consequences (44, 45). These animals lived only a week or two
and exhibited faulty mitochondrial activities in several tissues,
especially the heart.
The familial form of amyotrophic lateral sclerosis, or FALS, has been
shown to be associated with defects in the gene encoding Cu,Zn-SOD
(sod 1) (46-48). That this disease was due to a toxic gain
of function of the mutated protein, rather than to a loss of SOD
activity, was suggested by its genetic dominance and was demonstrated
by the ability of the G93A transgene in mice to impose late onset
progressive paralysis (49, 50). There is evidence for two different
gains of function. One of these is a peroxidase activity (51), and the
other is the ability to catalyze nitration of neurofilaments by
peroxynitrite (52). Yet another novel activity of a FALS-associated
Cu,Zn-SOD (H48Q) has been observed,3 and
that is a superoxide-dependent peroxidase activity.
Cu,Zn-SOD has been reported to catalyze the production of HO·
from H2O2 (53), and the FALS-associated G93A
mutant has been shown to be more active in this regard than the
wild-type enzyme (54). However, reasons for attributing these
observations to the peroxidase activity of the enzyme, rather than to
the production of free HO·, have been delineated (6). It may be
that all of these contribute to the observed pathology in FALS.
Sporadic amyotrophic lateral sclerosis is clinically indistinguishable
from FALS so a related mechanism might be suspected. A recent report
(55) that apparent cases of sporadic amyotrophic lateral sclerosis were
homozygous with respect to Asp90-Ala Cu,Zn-SOD supports
this notion.
Another genetic disease that may be due to faulty superoxide dismutases
is progeria. Polymorphisms in the signal sequence of the gene coding
for Mn-SOD have been reported (56). This led to the proposal that
progeria might be due to faulty localization of Mn-SOD.
Down's syndrome (trisomy 21) is associated with a ~50%
overproduction of Cu,Zn-SOD, since the gene coding for this enzyme is
located on human chromosome 21. It has been suggested that this
overproduction causes the symptoms of this syndrome (57). However, this
seems unlikely. Thus a partial trisomy 21 with overdosages of Cu,Zn-SOD
was associated with none of the usual symptoms (58). This lack of
correlation of symptoms with overdosage has been replicated (59).
Varieties of Superoxide Dismutase The SOD family has been growing. The eukaryotic cytosolic
Cu,Zn-SOD and the mitochondrial Mn-SOD are now joined by an
extracellular Cu,Zn-SOD, which is referred to as EC-SOD. The human
enzyme is a homotetrameric protein with a Mr = 135,000. It shows some sequence homology to the cytosolic Cu,Zn-SOD but
is designed for function in the extracellular spaces and is secreted by
the cells that produce it. It is glycosylated and exhibits affinity for
sulfated polysaccharides, such as heparin or heparan sulfate. Thus,
although detectable in blood plasma, most of it exists bound onto the
extracellular matrix (60-62). Its location positions EC-SOD to
intercept O An entirely new SOD, with nickel at its active site, has been found in
Streptomyces (67). This is a homotetrameric enzyme whose
subunit weight is 13,000. It bears no obvious sequence homology to
known Mn-SODs or Fe-SODs.
Cu,Zn-SODs have been reported in a few species of bacteria and were
considered unusual. However, such Cu,Zn-SODs have been described with
increasing frequency (68-72), and it is now likely that they occur in
most Gram-negative bacteria where they are apt to be localized to the
periplasm (68, 69). The E. coli Cu,Zn-SOD appears to be
unusual in that it is monomeric (70), rather than being dimeric as are
other Cu,Zn-SODs. Null mutants in Cu,Zn-SOD have been prepared; the
Caulobacter crescentis null exhibited increased sensitivity
toward citrate and toward deficiencies in Ca(II) or Mg(II) (71),
whereas the Legionella null showed decreased survival in
stationary phase (72). Sequence analysis and comparisons make it clear
that Cu,Zn-SOD arose prior to the divergence of eukaryotes and
eubacteria (73). It may be that the periplasmic Cu,Zn-SOD serves as a
defense against exogenous O SoxRS Regulon Nothing illustrates the many faceted nature of the defense against
oxidative stress more than does the SoxRS regulon. This group of
coordinately regulated genes is turned on by any condition that
increases O Much remains to be told of that which is already known and much remains
to be learned. I apologize to those workers who may feel slighted
because their important contributions do not appear in the list of
references and to the readers whose special interests are not
discussed. The impossibility of fairly treating the field and those
whose work created it in a minireview may be taken as another
indication of the rapid growth of knowledge in this area.
FOOTNOTES REFERENCES
Volume 272, Number 30,
Issue of July 25, 1997
pp. 18515-18517
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
MINIREVIEW:
2), Superoxide
Dismutases, and Related Matters*
INTRODUCTION
Measurement of O
2 in Vitro and in Vivo
Oxidants from O2 in Vitro and in Vivo
Mutations and Complementations of Superoxide Dismutases
Varieties of Superoxide Dismutase
SoxRS Regulon
FOOTNOTES
REFERENCES
2. In addition, the involvement of O2 in both physiological and pathological processes is being established. A
weighty tome would be needed to encompass a comprehensive coverage of
this field of study. This review will describe only aspects of the
biology of oxygen radicals that currently engage the interest of the
writer. Hopefully they will also be of interest to the reader. Other
recent reviews may serve to fill the gaps in this one (1-6).
2 in Vitro and in Vivo
2 is a facile process, and O2
production by spontaneous as well as enzyme-catalyzed reactions has
been demonstrated. The instability of O2 in aqueous solutions
is a hindrance to its detection and measurement. This has been
circumvented by exploiting its reaction with various "detector"
molecules such as ferricytochrome c or spin-trapping agents.
These agents are not specific for O2. Thus, reductants other
than O2 can reduce ferricytochrome c, and oxidants
other than O2 can convert the spin traps to their epr-detectable hydroperoxy derivatives (7, 8). Inhibition by
SOD1 is used to lend specificity to these
methods.
2 within cells is a
goal as difficult as it is desirable. Unfortunately enthusiasm for
achieving this goal has led many investigators to use flawed methods.
An example is the luminescence that can be elicited from lucigenin.
Early studies of the lucigenin luminescence elicited by the xanthine
oxidase reaction led to the realization that the lucigenin dication
must be univalently reduced to the corresponding monocation before
reacting with O2 in the process that leads to luminescence (9,
10). The chemistry involved was discussed in a more recent review (11).
Nevertheless the use of lucigenin as a "specific" detector of
O2 continues. Quite recently it was shown that the lucigenin
monocation radical can autoxidize and thus produce O2, even in
cases where no O2 was being produced in the absence of
lucigenin (12). In studies with Escherichia coli, lucigenin
was shown to function, much as does paraquat, to increase intracellular
O2 production (13). Hopefully the widespread but inappropriate
use of lucigenin luminescence as a measure of O2 will
stop.
2 is
based on luminol. In this case the compound must be univalently oxidized to a luminol radical, which reacts with O2 before the light-emitting pathway is entered upon. The problem in this case is
that the luminol radical can spontaneously reduce O2 to
O2. Luminol luminescence thus can be caused by a variety of
oxidants and in all cases SOD inhibits (14, 15). Here again the
detector is acting as a source of O2.
2 needs to be
mentioned because of its widespread misuse, and that is nitroblue
tetrazolium. Many enzymes can cause the reduction of tetrazolium salts
to the corresponding formazans. Reduction of nitroblue tetrazolium to the monoformazan requires two electrons and to the diformazan four
electrons. When proceeding by a univalent pathway, which is usual, one
encounters tetrazoinyl radical intermediates (16), which reduce
O2 to O2 in a reversible process. SOD by removing O2 displaces this oxidation to the right and thus prevents
production of the formazan. For this reason many aerobic tetrazolium
reductions are inhibitable by SOD even though O2 was not being
produced in the system in the absence of the tetrazolium (17).
2? There is and it is based on the rapid
inactivation of [4Fe-4S]-containing dehydratases, such as aconitase.
O2 oxidizes the clusters of these dehydratases resulting in
loss of Fe(II), and that is reversible by reduction and reincorporating
of Fe(II). The balance between these opposing processes can be used
as a measure of O2 and has been so used in E. coli
(18) and in mammalian cells (19). The inactivation of aconitase by
O2 provides an explanation for previously inexplicable
observations. Thus high pO2 (291 mm) increased both glucose
utilization and lactate production, by 4-6-fold, in WI38 cells (20).
Raising pO2 would increase O2 production, and
inactivation of aconitase by O2 would force the cells to rely
on fermentation of glucose for energy. In another example
Aspergillus niger was reported (21) to accumulate less citrate in the medium when supplied with 0.1 mg/liter Mn(II). In this
instance enrichment of the medium with Mn(II) would increase the level
of Mn-SOD in the mitochondria, and that in turn would decrease
O2 and thus raise aconitase. The final effect would be
increased metabolism of citrate via the Krebs cycle and less citrate
excretion. Near UV irradiation of E. coli inhibited growth on succinate more than growth on glucose (22) and inhibited respiration
(23). Both of these effects can be explained by the inactivation of
aconitase by photosensitized production of O2.
2. Of
these peroxynitrite is particularly relevant to biology, but in NO-producing cells the level of peroxynitrite is itself dependent upon
O2 production. Inactivation by H2O2 is
relatively unimportant.
2 in Vitro and in Vivo
2 can initiate and propagate free radical
oxidations of leukoflavins, tetrahydropterins, catecholamines, and
related compounds and can inactivate [4Fe-4S]-containing
dehydratases, it does not significantly attack polyunsaturated lipids
or DNA. Yet defects in SODs, which would have the effect of raising
intracellular [O2], do lead to cell envelope damage (24) and
to enhanced mutagenesis (25). Mechanisms by which O2 can give
rise to more potent oxidants could explain these seeming anomalies, and
there are several such mechanisms. The simplest of these is protonation to hydroperoxyl radical, whose pKa is 4.8 and which
is a much stronger oxidant than is O2. Association of
O2 with other cationic centers such as vanadate (26) or Mn(II)
(27) also have this effect, but these mechanisms are unlikely to apply
generally within cells.
2 increases "free" iron by oxidizing the [4Fe-4S]
center of dehydrases such as dihydroxy acid dehydrase (28),
6-phosphogluconate dehydrase (29), fumarases A and B (30), and
aconitase (31, 32). The released iron is kept reduced by cellular
reductants, and the Fe(II) reacts with H2O2, as
in the Fenton reaction, to yield Fe(III) + HO· or its formal
equivalent, Fe(II)O. This was proposed (33) to provide an explanation
for the enhanced O2-dependent mutagenesis exhibited by sodA sodB E. coli, and it has been
experimentally verified (34, 35). The importance of release of iron by
O2 from [4Fe-4S] clusters of dehydrases was underscored by
the recent observation of the complementation of sodA sodB E. coli by insertion and overexpression of rubredoxin reductase (36).
Rubredoxin reductase may play a role in reconstitution of the
oxidatively disassembled [4Fe-4S] clusters of dehydrases and thereby
lower the "free" iron in aerobic SOD-null E.
coli, or it may somehow scavenge O2 within
cells.
2, and by its reactive progeny, is the SODs. The importance of these enzymes has been clarified by the phenotypic deficits of
mutants defective in their production and in a number of cases by the
complementing effects of homologous or heterologous SODs. These
demonstrations have been achieved in bacteria (25, 37), yeast (38, 39),
Drosophila (40), a nematode (41), Neurospora (42), and even mice (43-45). The consequences of a lack of both the
constitutive Fe-SOD (SOD B) and the inducible Mn-SOD (SOD A) in
E. coli include oxygen dependent decrease of growth rate, nutritional auxotrophies, hypersensitivity toward redox cycling compounds such as paraquat and quinones, and an increase in the rate of
spontaneous mutagenesis. In yeast similar problems were seen in strains
lacking either the cytosolic Cu,Zn-SOD or the mitochondrial Mn-SOD.
Envelope damage was made evident by the ability of osmolytes to
facilitate the aerobic growth of the sodA sodB E. coli and
to partially suppress the amino acid requirements (24).
2 released by phagocytic leukocytes and other
cell types. It may be important for decreasing the very rapid reaction
of O2 with NO (63) and thus for increasing the lifetime of
NO while decreasing net production of the powerfully oxidizing
peroxynitrite (64). Knockout mice lacking EC-SOD develop normally but
were found more susceptible to the toxic effects of 1 atm of
O2 (65). Extracellular superoxide dismutase has been
reported in a variety of organisms including plants, bacteria,
Onchocerca, parasitic nematodes, and Schistosoma.
In the case of Nocardia asteroides, the extracellular SOD
has been shown to be a pathogenicity factor (66).
2.
2 production in E. coli (74, 75). Its
products include: Mn-SOD, to eliminate O2; glucose-6-phosphate
dehydrogenase, to ensure a supply of NADPH; endonuclease IV, to repair
oxidatively damaged DNA; the stable fumarase c, to replace
the O2-sensitive fumarases a and b;
ferredoxin reductase, to reductively repair oxidatively disassembled
[4Fe-4S] clusters; micF, to decrease the porosity of the outer
membrane; aconitase A, to replace the aconitase inactivated by
O2; and others as well. SoxR serves as the redox sensor, which
activates production of SoxS, which then turns on the entire regulon.
SoxR contains a [2Fe-2S] cluster and is a transcriptional activator
only in its oxidized state. The SoxRS regulon is itself only half of
the orchestrated defense against oxidative stress. There is another
independent regulon turned on in response to
H2O2 and referred to as the oxyR regulon (76).
To whom correspondence should be addressed. Tel.: 919-684-5122;
Fax: 919-684-8885.
1
The abbreviations used are: SOD, superoxide
dismutase; FALS, familial amyotrophic lateral sclerosis; EC-SOD,
extracellular SOD.
2
A. Reaume, personal communication.
3
S. I. Liochev, L. L. Chen, R. A. Hallewell, and
I. Fridovich, unpublished observation.
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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 S. D. Brydges and V. B. Carruthers Mutation of an unusual mitochondrial targeting sequence of SODB2 produces multiple targeting fates in Toxoplasma gondii J. Cell Sci., November 15, 2003; 116(22): 4675 - 4685. [Abstract] [Full Text] [PDF]
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 N. Esfandiari, R. K. Sharma, R. A. Saleh, A. J. Thomas Jr., and A. Agarwal Utility of the Nitroblue Tetrazolium Reduction Test for Assessment of Reactive Oxygen Species Production by Seminal Leukocytes and Spermatozoa J Androl, November 1, 2003; 24(6): 862 - 870. [Abstract] [Full Text] [PDF]
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 J. L. CADET, S. JAYANTHI, and X. DENG Speed kills: cellular and molecular bases of methamphetamine-induced nerve terminal degeneration and neuronal apoptosis FASEB J, October 1, 2003; 17(13): 1775 - 1788. [Abstract] [Full Text] [PDF]
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T. B. Bartnikas and J. D. Gitlin Mechanisms of Biosynthesis of Mammalian Copper/Zinc Superoxide Dismutase J. Biol. Chem., August 29, 2003; 278(35): 33602 - 33608. [Abstract] [Full Text] [PDF]
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C. Cao, Y. Leng, and D. Kufe Catalase Activity Is Regulated by c-Abl and Arg in the Oxidative Stress Response J. Biol. Chem., August 8, 2003; 278(32): 29667 - 29675. [Abstract] [Full Text] [PDF]
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 P. A.C. 't Hoen, C. A.C. Van der Lans, M. Van Eck, M. K. Bijsterbosch, T. J.C. Van Berkel, and J. Twisk Aorta of ApoE-Deficient Mice Responds to Atherogenic Stimuli by a Prelesional Increase and Subsequent Decrease in the Expression of Antioxidant Enzymes Circ. Res., August 8, 2003; 93(3): 262 - 269. [Abstract] [Full Text] [PDF]
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 R. Janulczyk, S. Ricci, and L. Bjorck MtsABC Is Important for Manganese and Iron Transport, Oxidative Stress Resistance, and Virulence of Streptococcus pyogenes Infect. Immun., May 1, 2003; 71(5): 2656 - 2664. [Abstract] [Full Text] [PDF]
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 T. J. Bivalacqua, J. S. Armstrong, J. Biggerstaff, A. B. Abdel-Mageed, P. J. Kadowitz, W. J. G. Hellstrom, and H. C. Champion Gene transfer of extracellular SOD to the penis reduces O Am J Physiol Heart Circ Physiol, April 1, 2003; 284(4): H1408 - H1421. [Abstract] [Full Text] [PDF]
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A. G. Saez, A. Tatarenkov, E. Barrio, N. H. Becerra, and F. J. Ayala Patterns of DNA sequence polymorphism at Sod vicinities in Drosophila melanogaster: Unraveling the footprint of a recent selective sweep PNAS, February 18, 2003; 100(4): 1793 - 1798. [Abstract] [Full Text] [PDF]
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I. T. Demchenko, T. D. Oury, J. D. Crapo, and C. A. Piantadosi Regulation of the Brain's Vascular Responses to Oxygen Circ. Res., November 29, 2002; 91(11): 1031 - 1037. [Abstract] [Full Text] [PDF]
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K. SATO, M. B. KADIISKA, A. J. GHIO, J. CORBETT, Y. C. FANN, S. M. HOLLAND, R. G. THURMAN, and R. P. MASON In vivo lipid-derived free radical formation by NADPH oxidase in acute lung injury induced by lipopolysaccharide: a model for ARDS FASEB J, November 1, 2002; 16(13): 1713 - 1720. [Abstract] [Full Text] [PDF]
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 P. A. Ortiz and J. L. Garvin Superoxide stimulates NaCl absorption by the thick ascending limb Am J Physiol Renal Physiol, November 1, 2002; 283(5): F957 - F962. [Abstract] [Full Text] [PDF]
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 M. Aikawa, S. Sugiyama, C. C. Hill, S. J. Voglic, E. Rabkin, Y. Fukumoto, F. J. Schoen, J. L. Witztum, and P. Libby Lipid Lowering Reduces Oxidative Stress and Endothelial Cell Activation in Rabbit Atheroma Circulation, September 10, 2002; 106(11): 1390 - 1396. [Abstract] [Full Text] [PDF]
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S. Ricci, R. Janulczyk, and L. Bjorck The Regulator PerR Is Involved in Oxidative Stress Response and Iron Homeostasis and Is Necessary for Full Virulence of Streptococcus pyogenes Infect. Immun., September 1, 2002; 70(9): 4968 - 4976. [Abstract] [Full Text] [PDF]
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M. G. Espey, D. D. Thomas, K. M. Miranda, and D. A. Wink Focusing of nitric oxide mediated nitrosation and oxidative nitrosylation as a consequence of reaction with superoxide PNAS, August 20, 2002; 99(17): 11127 - 11132. [Abstract] [Full Text] [PDF]
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 A. M. Chinn, D. Ciais, S. Bailly, E. Chambaz, J. LaMarre, and J.-J. Feige Identification of Two Novel ACTH-Responsive Genes Encoding Manganese-Dependent Superoxide Dismutase (SOD2) and the Zinc Finger Protein TIS11b [Tetradecanoyl Phorbol Acetate (TPA)-Inducible Sequence 11b] Mol. Endocrinol., June 1, 2002; 16(6): 1417 - 1427. [Abstract] [Full Text] [PDF]
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 G Tozzi, M Nuccetelli, M Lo Bello, S Bernardini, L Bellincampi, S Ballerini, L M Gaeta, C Casali, A Pastore, G Federici, et al. Antioxidant enzymes in blood of patients with Friedreich's ataxia Arch. Dis. Child., May 1, 2002; 86(5): 376 - 379. [Abstract] [Full Text] [PDF]
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A. R. Krapp, R. E. Rodriguez, H. O. Poli, D. H. Paladini, J. F. Palatnik, and N. Carrillo The Flavoenzyme Ferredoxin (Flavodoxin)-NADP(H) Reductase Modulates NADP(H) Homeostasis during the soxRS Response of Escherichia coli J. Bacteriol., March 1, 2002; 184(5): 1474 - 1480. [Abstract] [Full Text] [PDF]
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 M. Rathaus and J. Bernheim Oxygen species in the microvascular environment: regulation of vascular tone and the development of hypertension Nephrol. Dial. Transplant., February 1, 2002; 17(2): 216 - 221. [Abstract] [Full Text] [PDF]
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 H.U. HINK and T. FUKAI Extracellular Superoxide Dismutase, Uric Acid, and Atherosclerosis Cold Spring Harb Symp Quant Biol, January 1, 2002; 67(0): 483 - 490. [Abstract] [PDF]
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S. Dubrac and D. Touati Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli Microbiology, January 1, 2002; 148(1): 147 - 156. [Abstract] [Full Text] [PDF]
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A. L. Farre and S. Casado Heart Failure, Redox Alterations, and Endothelial Dysfunction Hypertension, December 1, 2001; 38(6): 1400 - 1405. [Abstract] [Full Text] [PDF]
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 Manganese Superoxide Dismutase (Mn SOD or Sod2) Sci. Aging Knowl. Environ., October 3, 2001; 2001(1): tg12 - 12. [Full Text]
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J.-L. Frendo, P. Therond, T. Bird, N. Massin, F. Muller, J. Guibourdenche, D. Luton, M. Vidaud, W. B. Anderson, and D. Evain-Brion Overexpression of Copper Zinc Superoxide Dismutase Impairs Human Trophoblast Cell Fusion and Differentiation Endocrinology, August 1, 2001; 142(8): 3638 - 3648. [Abstract] [Full Text] [PDF]
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R. W. Seyler Jr., J. W. Olson, and R. J. Maier Superoxide Dismutase-Deficient Mutants of Helicobacter pylori Are Hypersensitive to Oxidative Stress and Defective in Host Colonization Infect. Immun., June 1, 2001; 69(6): 4034 - 4040. [Abstract] [Full Text] [PDF]
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 H. L. Reeve, E. Michelakis, D. P. Nelson, E. K. Weir, and S. L. Archer Alterations in a redox oxygen sensing mechanism in chronic hypoxia J Appl Physiol, June 1, 2001; 90(6): 2249 - 2256. [Abstract] [Full Text] [PDF]
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 W. M. Armstead Vasopressin-Induced Protein Kinase C-Dependent Superoxide Generation Contributes to ATP-Sensitive Potassium Channel but Not Calcium-Sensitive Potassium Channel Function Impairment After Brain Injury Stroke, June 1, 2001; 32(6): 1408 - 1414. [Abstract] [Full Text] [PDF]
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 H. L Reeve, S. Tolarova, D. P Nelson, S. Archer, and E K. Weir Redox control of oxygen sensing in the rabbit ductus arteriosus J. Physiol., May 15, 2001; 533(1): 253 - 261. [Abstract] [Full Text] [PDF]
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 J. E. White and M.-F. Tsan Differential Induction of TNF-{alpha} and MnSOD by Endotoxin . Role of Reactive Oxygen Species and NADPH Oxidase Am. J. Respir. Cell Mol. Biol., February 1, 2001; 24(2): 164 - 169. [Abstract] [Full Text]
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 M. PASTO, E. SERRANO, E. UROCOSTE, M.-A. BARBACANNE, A. GUISSANI, A. DIDIER, M.-B. DELISLE, J. RAMI, and J.-F. ARNAL Nasal Polyp-Derived Superoxide Anion . Dose-Dependent Inhibition by Nitric Oxide and Pathophysiological Implications Am. J. Respir. Crit. Care Med., January 1, 2001; 163(1): 145 - 151. [Abstract] [Full Text]
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K. Arimura, K. Egashira, R. Nakamura, T. Ide, H. Tsutsui, H. Shimokawa, and A. Takeshita Increased inactivation of nitric oxide is involved in coronary endothelial dysfunction in heart failure Am J Physiol Heart Circ Physiol, January 1, 2001; 280(1): H68 - H75. [Abstract] [Full Text] [PDF]
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 R. M. Touyz and E. L. Schiffrin Signal Transduction Mechanisms Mediating the Physiological and Pathophysiological Actions of Angiotensin II in Vascular Smooth Muscle Cells Pharmacol. Rev., December 1, 2000; 52(4): 639 - 672. [Abstract] [Full Text] [PDF]
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W. M. Armstead NOC/oFQ PKC-dependent superoxide generation contributes to hypoxic-ischemic impairment of NMDA cerebrovasodilation Am J Physiol Heart Circ Physiol, December 1, 2000; 279(6): H2678 - H2684. [Abstract] [Full Text] [PDF]
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J. A. Leopold and J. Loscalzo Cyclic strain modulates resistance to oxidant stress by increasing G6PDH expression in smooth muscle cells Am J Physiol Heart Circ Physiol, November 1, 2000; 279(5): H2477 - H2485. [Abstract] [Full Text] [PDF]
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M. Kulkarni, W. M. Armstead, and H. A. Kontos Superoxide Generation Links Nociceptin/Orphanin FQ (NOC/oFQ) Release to Impaired N-Methyl-D-Aspartate Cerebrovasodilation After Brain Injury Editorial Comment Stroke, August 1, 2000; 31(8): 1990 - 1996. [Abstract] [Full Text] [PDF]
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S. Dubrac and D. Touati Fur Positive Regulation of Iron Superoxide Dismutase in Escherichia coli: Functional Analysis of the sodB Promoter J. Bacteriol., July 1, 2000; 182(13): 3802 - 3808. [Abstract] [Full Text]
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J. Vasquez-Vivar, B. Kalyanaraman, and M. C. Kennedy Mitochondrial Aconitase Is a Source of Hydroxyl Radical. AN ELECTRON SPIN RESONANCE INVESTIGATION J. Biol. Chem., May 5, 2000; 275(19): 14064 - 14069. [Abstract] [Full Text] [PDF]
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 Z. Dong, Y. Lavrovsky, M. A. Venkatachalam, and A. K. Roy Heme Oxygenase-1 in Tissue Pathology : The Yin and Yang Am. J. Pathol., May 1, 2000; 156(5): 1485 - 1488. [Full Text] [PDF]
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H. Atamna, A. Paler-Martinez, and B. N. Ames N-t-Butyl Hydroxylamine, a Hydrolysis Product of alpha -Phenyl-N-t-butyl Nitrone, Is More Potent in Delaying Senescence in Human Lung Fibroblasts J. Biol. Chem., March 15, 2000; 275(10): 6741 - 6748. [Abstract] [Full Text] [PDF]
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M. M. Whittaker and J. W. Whittaker Thermally Triggered Metal Binding by Recombinant Thermus thermophilus Manganese Superoxide Dismutase, Expressed as the Apo-enzyme J. Biol. Chem., December 3, 1999; 274(49): 34751 - 34757. [Abstract] [Full Text] [PDF]
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M. V. Brahmajothi and D. L. Campbell Heterogeneous Basal Expression of Nitric Oxide Synthase and Superoxide Dismutase Isoforms in Mammalian Heart : Implications for Mechanisms Governing Indirect and Direct Nitric Oxide-Related Effects Circ. Res., October 1, 1999; 85(7): 575 - 587. [Abstract] [Full Text] [PDF]
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 J. F. Palatnik, N. Carrillo, and E. M. Valle The Role of Photosynthetic Electron Transport in the Oxidative Degradation of Chloroplastic Glutamine Synthetase Plant Physiology, October 1, 1999; 121(2): 471 - 478. [Abstract] [Full Text]
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M. Usui, K. Egashira, S. Kitamoto, M. Koyanagi, M. Katoh, C. Kataoka, H. Shimokawa, and A. Takeshita Pathogenic Role of Oxidative Stress in Vascular Angiotensin-Converting Enzyme Activation in Long-Term Blockade of Nitric Oxide Synthesis in Rats Hypertension, October 1, 1999; 34(4): 546 - 551. [Abstract] [Full Text] [PDF]
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R. M. Touyz and E. L. Schiffrin Ang II-Stimulated Superoxide Production Is Mediated via Phospholipase D in Human Vascular Smooth Muscle Cells Hypertension, October 1, 1999; 34(4): 976 - 982. [Abstract] [Full Text] [PDF]
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J. Bai, A. M. Rodriguez, J. A. Melendez, and A. I. Cederbaum Overexpression of Catalase in Cytosolic or Mitochondrial Compartment Protects HepG2 Cells against Oxidative Injury J. Biol. Chem., September 10, 1999; 274(37): 26217 - 26224. [Abstract] [Full Text] [PDF]
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Y. A. Kuryshev, G. M. Brittenham, H. Fujioka, P. Kannan, C.-C. Shieh, S. A. Cohen, and A. M. Brown Decreased Sodium and Increased Transient Outward Potassium Currents in Iron-Loaded Cardiac Myocytes : Implications for the Arrhythmogenesis of Human Siderotic Heart Disease Circulation, August 10, 1999; 100(6): 675 - 683. [Abstract] [Full Text] [PDF]
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T. E. Peterson, V. Poppa, H. Ueba, A. Wu, C. Yan, and B. C. Berk Opposing Effects of Reactive Oxygen Species and Cholesterol on Endothelial Nitric Oxide Synthase and Endothelial Cell Caveolae Circ. Res., July 9, 1999; 85(1): 29 - 37. [Abstract] [Full Text] [PDF]
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K.-I Lin, P. Pasinelli, R. H. Brown, J. M. Hardwick, and R. R. Ratan Decreased Intracellular Superoxide Levels Activate Sindbis Virus-induced Apoptosis J. Biol. Chem., May 7, 1999; 274(19): 13650 - 13655. [Abstract] [Full Text] [PDF]
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E. Minc, P. de Coppet, P. Masson, L. Thiery, S. Dutertre, M. Amor-Gueret, and C. Jaulin The Human Copper-Zinc Superoxide Dismutase Gene (SOD1) Proximal Promoter Is Regulated by Sp1, Egr-1, and WT1 via Non-canonical Binding Sites J. Biol. Chem., January 1, 1999; 274(1): 503 - 509. [Abstract] [Full Text] [PDF]
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N. M. Brown, S. A. Anderson, D. W. Steffen, T. B. Carpenter, M. C. Kennedy, W. E. Walden, and R. S. Eisenstein Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1 PNAS, December 22, 1998; 95(26): 15235 - 15240. [Abstract] [Full Text] [PDF]
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A. Hausladen, A. J. Gow, and J. S. Stamler Nitrosative stress: Metabolic pathway involving the flavohemoglobin PNAS, November 24, 1998; 95(24): 14100 - 14105. [Abstract] [Full Text] [PDF]
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L.-J. Yan and R. S. Sohal Mitochondrial adenine nucleotide translocase is modified oxidatively during aging PNAS, October 27, 1998; 95(22): 12896 - 12901. [Abstract] [Full Text] [PDF]
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J.-I. Park, C. M. Grant, M. J. Davies, and I. W. Dawes The Cytoplasmic Cu,Zn Superoxide Dismutase of Saccharomyces cerevisiae Is Required for Resistance to Freeze-Thaw Stress. GENERATION OF FREE RADICALS DURING FREEZING AND THAWING J. Biol. Chem., September 4, 1998; 273(36): 22921 - 22928. [Abstract] [Full Text] [PDF]
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M. M. Whittaker and J. W. Whittaker A Glutamate Bridge Is Essential for Dimer Stability and Metal Selectivity in Manganese Superoxide Dismutase J. Biol. Chem., August 28, 1998; 273(35): 22188 - 22193. [Abstract] [Full Text] [PDF]
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R. J. Singh, H. Karoui, M. R. Gunther, J. S. Beckman, R. P. Mason, and B. Kalyanaraman Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H2O2 PNAS, June 9, 1998; 95(12): 6675 - 6680. [Abstract] [Full Text] [PDF]
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S. K. Manna, H. J. Zhang, T. Yan, L. W. Oberley, and B. B. Aggarwal Overexpression of Manganese Superoxide Dismutase Suppresses Tumor Necrosis Factor-induced Apoptosis and Activation of Nuclear Transcription Factor-kappa B and Activated Protein-1 J. Biol. Chem., May 22, 1998; 273(21): 13245 - 13254. [Abstract] [Full Text] [PDF]
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L. Benov and I. Fridovich Growth in Iron-enriched Medium Partially Compensates Escherichia coli for the Lack of Manganese and Iron Superoxide Dismutase J. Biol. Chem., April 24, 1998; 273(17): 10313 - 10316. [Abstract] [Full Text] [PDF]
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Y. Li, H. Zhu, P. Kuppusamy, V. Roubaud, J. L. Zweier, and M. A. Trush Validation of Lucigenin (Bis-N-methylacridinium) as a Chemilumigenic Probe for Detecting Superoxide Anion Radical Production by Enzymatic and Cellular Systems J. Biol. Chem., January 23, 1998; 273(4): 2015 - 2023. [Abstract] [Full Text] [PDF]
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W. Wang, S. Wang, L. Yan, P. Madara, A. Del Pilar Cintron, R. A. Wesley, and R. L. Danner Superoxide Production and Reactive Oxygen Species Signaling by Endothelial Nitric-oxide Synthase J. Biol. Chem., May 26, 2000; 275(22): 16899 - 16903. [Abstract] [Full Text] [PDF]
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Z. Zhang, K. Apse, J. Pang, and R. C. Stanton High Glucose Inhibits Glucose-6-phosphate Dehydrogenase via cAMP in Aortic Endothelial Cells J. Biol. Chem., December 15, 2000; 275(51): 40042 - 40047. [Abstract] [Full Text] [PDF]
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M. D. Wheeler, M. Nakagami, B. U. Bradford, T. Uesugi, R. P. Mason, H. D. Connor, A. Dikalova, M. Kadiiska, and R. G. Thurman Overexpression of Manganese Superoxide Dismutase Prevents Alcohol-induced Liver Injury in the Rat J. Biol. Chem., September 21, 2001; 276(39): 36664 - 36672. [Abstract] [Full Text] [PDF]
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A. J. Vidal-Puig, D. Grujic, C.-Y. Zhang, T. Hagen, O. Boss, Y. Ido, A. Szczepanik, J. Wade, V. Mootha, R. Cortright, et al. Energy Metabolism in Uncoupling Protein 3 Gene Knockout Mice J. Biol. Chem., May 19, 2000; 275(21): 16258 - 16266. [Abstract] [Full Text] [PDF]
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S. P. Didion and F. M. Faraci Effects of NADH and NADPH on superoxide levels and cerebral vascular tone Am J Physiol Heart Circ Physiol, February 1, 2002; 282(2): H688 - H695. [Abstract] [Full Text] [PDF]
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