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-Tocopherol1
2
Departments of
*
Nutrition and Dietetics and
Clinical Biochemistry, King’s College, London, UK
2To whom correspondence should be addressed.
 |
ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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-tocopherol (ATC) supplementation. We have also shown evidence of
increased oxidative stress and reduced protein synthesis rates in
alcohol-exposed muscle. Serum levels of ATC fall and rates of
muscle protein synthesis are reduced in patients with alcoholic
myopathy. We therefore tested the hypothesis that treatment with ATC
could ameliorate the ethanol-induced changes in muscle protein
synthesis, a contributory event in the pathogenesis of alcoholic muscle
disease. Studies were carried out on gastrocnemius (Type II
fiber-predominant and usually considered representative of the
musculature as a whole), soleus (Type I fiber-predominant) and
plantaris (Type II fiber-predominant) muscles. For comparative
purposes, we also investigated the liver. Young male Wistar rats (90 g
body weight) were injected intraperitoneally (i.p.) daily with ATC (30
mg/kg body weight) in Intralipid fat emulsion (0.1 mL/100 g body, i.p.)
for 5 d. Controls were similarly injected with the Intralipid
vehicle alone. After ATC supplementation, rats were given ethanol (75
mmol/kg body weight, i.p., 2.5 h) or saline (0.15 mol/L NaCl,
i.p.). Fractional rates of tissue protein synthesis (i.e., the
percentage of the tissue protein pool renewed each day,
ks, %/d) and RNA activities [i.e., the
amount of protein synthesis each day per unit RNA,
kRNA, mg protein/d/mg RNA)] were then
measured. Supplementation increased ATC concentrations in plasma,
gastrocnemius and liver. There was no effect of ATC supplementation
alone on ks in any of the tissues. ATC
supplementation in the absence of alcohol increased
kRNA in the plantaris muscle. In
nonsupplemented groups, acute ethanol treatment reduced skeletal muscle
(soleus, plantaris and gastrocnemius) ks.
Hepatic ks was not altered by ethanol,
although ATC concentrations in this tissue increased due to ethanol.
However, none of the changes in muscle ks or
kRNA due to ethanol were significantly
affected by ATC supplementation. In conclusion, ATC supplementation
does not appear beneficial in ameliorating acute alcohol toxicity in
skeletal muscle as defined by reductions in protein synthesis.
KEY WORDS: • -tocopherol • muscle • liver • protein synthesis • rats • alcohol
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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), gastrointestinal tract (Seitz and Poschl 1997
), skeletal muscle (Xu et al. 1996
), heart
(Fernandez Sola et al. 1997
) and brain (Zimakin and Deitrich 1997
). A reduction in the rate of protein
synthesis is a central feature of acute ethanol toxicity affecting all
of the aforementioned tissues [see, for example Bonner et al. (2000)
, Marway et al. (1997)
, Preedy and Peters (1988)
, Proctor et al. (1993)
and
Siddiq et al. (1997)
]. These reductions are reported to
be related to changes in the activation of translation initiation
factors involved in the binding of met-tRNA to the 40S ribosomal
subunit, i.e., eukaryotic initiation factor 2B
(eIF2B)3and the initiation factors that are involved in the binding of mRNA to
the 43S preinitiation complex eIF4E (Lang et al. 1999
).
Muscle and liver respond differently with respect to these subcellular
changes (Lang et al. 1999
). In skeletal muscle,
reductions in protein synthesis may be an initiating factor in the
pathogenesis of the disease entity alcoholic myopathy (Preedy et al. 1990
, Reilly et al. 1995
). However, cellular
factors for initiating the reductions in tissue protein synthesis in
alcohol toxicity are unknown, although consideration must be given to
the excessive generation of reactive oxygen species (ROS), leading to
enhanced lipid peroxidation and/or membrane damage (Adachi et al. 2000b
; Preedy et al. 1998a and 1998b
). We
found that two cholesterol-derived hydroperoxides,
7-hydroperoxycholest-5-en-3ß-ol (7-OOH) and
7ß-hydroperoxycholest-5-en-3ß-ol (7ß-OOH), were significantly
elevated in both soleus and plantaris muscle of rats 24 h after
acute ethanol treatment (75 mmol/kg body as used in this study). This
reflects greater oxidative stress in the pathology of muscle of rats
treated acutely with ethanol and, together with the observations of
perturbations in membrane lipids in response to ethanol, has important
implications for the pathogenesis of alcohol-induced muscle
disorders. Although increased hydroperoxides were shown to be elevated
at 24 h (Adachi et al. 2000b
), we have also shown
significant increases in plantaris 2.5 h after ethanol treatment
(Adachi et al. 2000a
). A number of studies have
implicated oxidant and antioxidant factors in the pathogenesis of other
alcohol-related disorders such as alcoholic pancreatic (Van Gossum et al. 1996
) and liver diseases (Chen et al. 1995
).
Numerous studies have also implicated the generation of ROS and/or
enhanced lipid peroxidation in the pathogenesis of reduced tissue
protein synthesis The shellfish toxin okadaic acid reduces protein
synthesis in cultures of vero cells, by a mechanism involving increased
lipid peroxidation (Matias et al. 1999
). Similarly, an
increase in intestinal lipid peroxidation in Salmonella
typhimurium infection perturbs amino acid transport, thereby
leading to a reduction in enterocyte protein synthesis (Mehta et al. 1998
). In metabolically degenerated neuronal tissue in
vitro and liver tissue slices, there are also decreases in protein
synthesis in response to enhanced lipid peroxidation (Fraga et al. 1989
, Uto et al. 1995
). These reductions in
protein synthesis can be prevented by -tocopherol (ATC)
(Fraga et al. 1989
, Matias et al. 1999
,
Uto et al. 1995
).
From the above, we suggest that ATC supplementation may also have an ameliorative effect on ethanol-induced reductions in skeletal muscle protein synthesis. We tested this hypothesis by investigating changes in tissue ATC concentration and indices of protein metabolism in response to acute ethanol treatment in vivo, with or without ATC supplementation. Comparative reference was also made to the response of the liver because of its central role in both ethanol and ATC metabolism.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Male Wistar rats were obtained from Charles River (Margate, Kent, UK)
and consumed ad libitum a commercial pelleted diet containing crude
protein, 17.9%; crude fiber 3.6%; carbohydrate, 57%; 13.3 MJ/kg (CRM
diet, Special Diets Services, Essex, UK). They were housed in cages in
an air-conditioned (20–25°C), humidified (40–60%) animal house
with a 12-h light:dark cycle starting at 0800 h. Sterile
-(+/-)-tocopherol (950 g/L) for injections was obtained from Sigma
Chemical (Lewes, Sussex, UK) and Intralipid intravenous fat emulsion
from Kabi Pharmacia (Tring, Buckinghamshire, UK). Pyrogallol,
HPLC-grade ammonium acetate and HPLC-grade methanol were from
Merck/BDH (Poole, Dorset, UK). All other materials and chemicals were
from either Sigma Chemical or Merck/BDH.
ATC supplementation and ethanol dosage.
Four groups of rats (60–70 g body weight) were weight-ranked into
groups of equivalent mean body weights and allocated for treatment with
either vehicle (Intralipid) or ATC (supplemented) and saline or ethanol
as listed below. They were then fed and housed as described above for
an initial 3-d period until they reached a body weight of 
90 g. Rats
were then divided into four groups of equal mean body weight as a 2
x 2 factorial as follows: Group 1, vehicle-treated (5 d),
saline-injected (2.5 h); Group 2, vehicle-treated (5 d),
ethanol-injected (2.5 h); Group 3, ATC-supplemented (5 d),
saline-injected (2.5 h); and Group 4, ATC-supplemented (5 d),
ethanol-injected (2.5 h). The use of this ethanol treatment
protocol has been reviewed previously (Preedy et al. 1996
).
ATC suspensions were prepared by ultrasonic homogenization of
-(+/-)-tocopherol in 20% (v/v) Intralipid fat emulsion (mass/L;
fractionated soybean oil, 200 g; fractionated egg phospholipids,
12 g; glycerol, 225 g; energy content, 8400 kJ; and
osmolality, 350 mosm/kg) to a concentration of 300 g/L using a sterile
Polytron (Phillip Harris, London, UK) homogenizer probe. Rats were
injected intraperitoneally (i.p.) daily at 0900 h with either the
ATC preparation or Intralipid vehicle as indicated above, for a 5-d
period in the proportion of 0.1 mL/100 g body, after which time they
weighed 150 g. This regimen ensured a daily dose of 30 mg ATC/kg
body weight, in addition to the small amount of mixed tocopherols
present in the Intralipid vehicle (mass/L Intralipid: 0.024 g
RRR--tocopherol, 0.184 g
RRR-
-tocopherol and 0.088 g
RRR-
-tocopherol) which totaled 0.296 g. Although
control (i.e., vehicle-injected) rats also received the small amount of
mixed tocopherols in the Intralipid vehicle, the dose of ATC received
represented 1% of that administered to the ATC-supplemented
rats. In addition, the biological activities of -tocopherol and
-tocopherol in protection against ROS are far less important than
that of ATC (Chow 1985
). After supplementation, rats
were allowed a 1-d clearance period before i.p. ethanol or saline
treatment. This was to ensure that uptake of i.p. injected saline or
ethanol was not impeded by residual Intralipid or ATC.
Ethanol-dosed rats were injected with a single bolus of ethanol [75
mmol/kg body weight as 1.0 mL/kg body, i.p., (Preedy et al. 1996
)]. Saline-injected controls were similarly injected
with isovolumetric 0.15 mol/L NaCl (sterile). Treatment of
saline-injected rats was identical to that of ethanol-injected
rats.
At 140 min after ethanol or saline injection, rats were injected
intravenously with a "flooding dose" of
[4-3H]-phenylalanine and killed by decapitation 10 min
later as described previously (Garlick et al. 1980
).
Tissue samples were taken for analysis of protein and RNA composition,
ATC and fractional rates of protein synthesis
(ks) as detailed below. Blood was collected
in heparin- or fluoride-coated tubes for analysis of plasma ATC and
ethanol, respectively. All tissue samples were stored at -70°C until
processing; plasma was stored at -20°C (analytes) or -70°C
(ethanol) before analysis.
Assays performed.
Tissue ATC was extracted and assayed by reverse-phase HPLC
(Heap 1994
). Briefly, 1.5-mL aliquots of tissue
homogenate (or 0.5 mL plasma) in water were mixed with pyrogallol (1.5
g/L in ethanol, 2.0 mL) and saponified at 70°C for 30 min with 0.45
mL of 10 mol/L KOH. Hexane (4 mL) was used as the extractant and was
evaporated under nitrogen. The residues were then redissolved in 0.1 mL
methanol. Aliquots of this extract were assayed on a MOS-2
glass-fiber column (Jones Chromatography, Hengoed, Wales)
in a mobile phase of 5% of 1 mol/L ammonium acetate/95% (v/v)
methanol by fluorescent spectrophotometry using excitation and emission
wavelengths of 294 and 320 nm, respectively [Hitachi F 1050 model
fluorescent spectrophotometry; Hitachi, Tokyo, Japan (Heap 1994
)]. Total RNA and protein were measured as previously
described (Siddiq et al. 1993
).
"Flooding dose" determination of fractional synthesis rates in vivo.
The fractional rate of protein synthesis
(ks, defined as the percentage of tissue
protein renewed each day, i.e., %/d) was measured as described
previously (Garlick et al. 1980
) for phenylalanine.
Briefly, L-[4-3H]-phenylalanine (150 mmol/L;
specific radioactivity 18.5 MBq/mol, 1 mL/100 g body weight) was
injected into rats via a lateral tail vein. Exactly 10 min after
injection of isotope, rats were killed by decapitation and tissues were
quickly removed, blotted dry, weighed and frozen in liquid nitrogen.
All tissue samples were stored at -70°C until processing for
specific radioactivities of phenylalanine in intracellular tissue free
(Si) and protein-bound
(Sb) amino acid pools. The fractional rate
ks was calculated as follows:
ks = (Sb
x 100)/(Si x t),
%/d. Where t (in units of days) was the period
between injection of isotope and freezing of the tissue in liquid
nitrogen, during which the label was incorporated (Garlick et al. 1980
). The RNA activity (kRNA, a
dynamic measure of the activity of cellular RNA in protein synthesis,
defined as the amount of protein synthesized per unit of RNA) was
derived by division of ks by protein
"synthetic capacity" (Cs, mg RNA/g
protein).
Statistics.
All data are expressed as means ± SEM (n = 4–8). Differences between means were assessed by two-way ANOVA. Significant difference was indicated at P < 0.05.
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RESULTS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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-ATC supplementation. ATC-supplementation
significantly increased plasma concentrations of ATC (P
< 0.001; Table 1
). There were also large increases in ATC concentrations in
gastrocnemius muscle (P < 0.025) and liver
(P < 0.001).
There were no significant differences in protein or RNA contents in any
of the tissues due to ATC treatment (data not presented). ATC
supplementation per se did not affect fractional rates of protein
synthesis (ks) in any of the tissues
examined (Table 2
). The RNA activity (kRNA) in the
plantaris but not in other tissues increased significantly
(P < 0.02; Table3
) in response to ATC supplementation. The meaning of the increase in
plantaris kRNA is unclear because
ks values (Table 2)
and protein and
RNA contents (not shown) were not significantly raised, but this may
represent a Type II fiber–specific response because this effect was
not observed in the soleus, a Type I fiber–predominant muscle.
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The i.p. ethanol treatment produced high plasma ethanol concentrations
(for example, 275 ± 12 mg/100 mL; 60 mmol/L), similar to
clinically determined values arising during alcoholic binge drinking in
humans, i.e., 61 mmol/L (Donovan et al. 1999
).
ATC concentration was not significantly affected in either plasma or
muscle due to ethanol treatment (Table 1)
. However, acute ethanol
treatment significantly increased liver ATC concentrations
(P < 0.05; Table 1
). Ethanol treatment reduced
ks in all skeletal muscles studied
(P < 0.001), but the fractional synthesis rates in the
liver were unaffected (Table 2)
. Ethanol decreased the
kRNA in all muscles studied
(P < 0.001; Table 3
).
|
No significant interactions were observed between ATC and ethanol on
RNA and protein contents (data not shown), ATC concentrations (Table 1)
, ks (Table 2)
or
kRNA (Table 3)
in any of the tissues
studied.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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). There are four
areas of evidence to support the hypothesis that -tocopherol
supplementation may be beneficial in ameliorating alcohol-induced
biochemical lesions in muscle. The first pertains to studies (with the
same treatment protocol as that used in this study, i.e., 75 mmol/kg
body) that show increased oxidative stress as evidenced by elevations
in skeletal muscle cholesterol-derived hydroperoxides, 7-OOH and
7ß-OOH (Adachi et al. 2000a and 2000b
). This is
suggestive of perturbations in membrane lipids in response to ethanol,
which may have important implications for the pathogenesis of
alcohol-induced muscle disorders. The second pertains to clinical
studies showing reduced levels of serum tocopherol in UK alcoholics
with skeletal muscle myopathy compared to patients without myopathy
(Ward and Peters 1992
). Third, alcoholic patients have
reduced rates of muscle protein synthesis as measured by stable isotope
incorporation studies (Pacy et al. 1991
). Finally, a
number of studies have implicated oxidant and antioxidant factors in
the pathogenesis of reduced protein synthesis, which can be ameliorated
by -tocopherol (Fraga et al. 1989
, Matias et al. 1999
, Uto et al. 1995
). From the above, we
proposed that ATC supplementation may also have an ameliorative effect
on ethanol-induced reductions in skeletal muscle protein synthesis
especially because ATC protects against a variety of
alcohol-induced pathologies (Mitchell et al. 1999
,
Nanji et al. 1996
). We tested this hypothesis by measuring tissue ATC concentrations and indices of protein metabolism in response to acute ethanol treatment in vivo, with or without prior ATC-supplementation. Comparative reference was also made to the response of the liver because of its central role in both ethanol and ATC metabolism.
Ethanol administration over extended periods causes marked
anorexia. The acute ethanol treatment protocol used in this study
circumvents this effect, allowing the appraisal of pathologic tissue
changes due solely to high levels of circulating ethanol. Reductions in
skeletal muscle (gastrocnemius, soleus and plantaris) protein synthesis
due to acute ethanol administration were observed, confirming previous
studies (Preedy et al. 1990, 1998a and 1998b
).
Acute dosing experiments reporting a relative lack of effect of ethanol
on hepatic protein synthesis in vivo (Donohue et al. 1987
) are also confirmed by the present results.
In this study, we focused on in vivo protein synthesis measurements
using the "flooding dose" method with phenylalanine (Garlick et al. 1980
). This has been reported to be the only feasible
method for measuring protein synthesis in intact animals (Davis et al. 1999
). None of the observed alterations in
ks or
kRNA in the present study were due to
changes in the specific radioactivity of the precursor as reflected by
measurement of Si (P
> 0.05; data not presented). Recent studies have shown that with
the "flooding dose" technique with phenylalanine, there is
excellent agreement with actual measurement of aminoacyl tRNA specific
radioactivities and free phenylalanine specific radioactivities in vivo
(Davis et al. 1999
). This does not appear to be
influenced by hormonal or nutritional perturbations (Davis et al. 1999
).
A number of processes have been proposed as causative mechanisms in
alcohol-induced muscle damage, including excessive generation of
ROS or impaired antioxidant systems (Reilly et al. 1995
). Increased generation of ROS has been reported after
acute ethanol administration [see, for example Preedy et al. (1999)
and Reinke et al. (1997)
]. Increased
skeletal muscle production of ROS has been suggested to arise from
intramuscular xanthine oxidase activities causing raised lipid
peroxidation of fatty acid moieties within the cellular and subcellular
membranes (Reinke and McCay, 1996
). The involvement of
ROS in the pathogenesis of alcohol-related disorders has previously
been assessed by attempts to reverse or ameliorate pathologic changes
using antioxidant therapies. Beneficial effects of ATC supplementation
on the extent of chronic ethanol-induced hepatic injury have been
observed (Nanji et al. 1996
). However, there are
comparatively few studies on the protective effects of antioxidants on
skeletal muscle. In skeletal muscle, the efficacy of ATC
supplementation in ameliorating ROS-mediated protein oxidation has
been shown after exercise (Meydani et al. 1993
),
glucocorticoid-induced myopathy (Ohtsuka et al. 1998
) and immobilization atrophy (Appell et al. 1997
). In ischemia or ischemia-reperfusion injury,
-tocopherol can ameliorate the reductions in muscle ATP, neutrophil
infiltration and increased lipid peroxidation; some of the beneficial
effects of -tocopherol may be related to its ability to impede the
expression of adhesion molecules such as ICAM-1 (Punz et al. 1998
). However, in our studies, ATC supplementation did not
significantly attenuate the ethanol-induced reductions in protein
synthesis. The reason for this relative lack of effect is unknown but
may pertain to the complex etiology of protein synthetic perturbations.
We used a 5-d protocol of ATC supplementation, which was sufficient to
raise circulating, liver and muscle levels of ATC. Such acute regimens
have proved efficacious in past studies on ROS-associated tissue or
metabolic damage in animals (Bauersachs et al. 1993
).
For example, a single dose given before the onset of ischemia can be
effective in ameliorating reductions in muscle ATP (Punz et al. 1998
) or reduce malondialdehyde after hypoxia
(Varskeviciene et al. 1984
).
It is possible that the failure to observe a protective effect of ATC was due to a protocol that allowed 1-d clearance before ethanol administration. However, we do not think this is likely because muscle, liver and plasma ATC concentrations were still raised 1 d after the last dose.
The presence of raised oxidative challenge (i.e., increased ROS) after
ethanol administration is now well documented, as is the role of ATC as
an important antioxidant for membrane lipid moieties (Reinke and McCay 1996
). It is possible that the oxidative stress induced
by ethanol may have been insufficient to cause changes in membrane
oxidation or that muscle has a higher antioxidant capacity. This can be
refuted because ethanol induces oxidative damage to muscle membrane
lipids, an effect that is not seen in liver (Adachi et al. 2000a
). However, it is important to realize that not all muscle
pathologies or indices of muscle damage can be ameliorated by ATC
supplementation. For example, raising muscle ATC concentrations by
dietary supplementation produced observable improvements in muscle
antioxidant capacity without improvement in indices of cellular injury
induced by eccentric exercise (Siciliano et al. 1997
) or
myotonic dystrophy (Orndahl et al. 1994
). It seems then
that alcohol-induced muscle damage, as reflected by changes in
tissue protein synthesis, may fall into this "nonresponsive"
category. The inability of skeletal muscle to respond to ATC may
reflect the fact that other processes may be involved in
ethanol-induced reductions in protein synthesis. Candidate
mechanisms include the formation of acetaldehyde-protein adducts,
which will render inoperative cytoskeletal or other proteins involved
in translation, by a process involving covalent binding (Niemela 1999
).
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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3 Abbreviations used: 7-OOH,
7-hydroperoxycholest-5-en-3ß-ol; ATC, -tocopherol; 7ß-OOH,
7ß-hydroperoxycholest-5-en-3ß-ol; eIF, eukaryotic initiation
factors; i.p., intraperitoneal; ks,
fractional rate of protein synthesis; kRNA,
RNA activity; ROS, reactive oxidative species;
Sb, specific radioactivity of
protein-bound amino acid; Si, specific
radioactivity of free amino acid in intracellular pools;
Sp, specific radioactivity of free plasma
amino acid.
Manuscript received April 19, 2000. Initial review completed May 19, 2000. Revision accepted August 22, 2000.
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-tocopherol–supplemented rats injected with saline or
ethanol12