Journal of Nutrition Animal Diets/Enrichment Products...

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Abstract Freely available
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hunter, R. J.
Right arrow Articles by Preedy, V. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hunter, R. J.
Right arrow Articles by Preedy, V. R.

© 2003 The American Society for Nutritional Sciences J. Nutr. 133:1154-1157, April 2003

Nutrient Interactions and Toxicity
Research Communication

Alcohol Affects the Skeletal Muscle Proteins, Titin and Nebulin in Male and Female Rats

R. J. Hunter2, C. Neagoe*, H. A. Järveläinen{dagger}, C. R. Martin{ddagger}, K. O. Lindros{dagger}, W. A. Linke* and V. R. Preedy

Department of Nutrition and Dietetics, King’s College, London, UK, * University of Heidelberg, Institute of Physiology and Pathophysiology, Heidelberg, Germany, {dagger} Alcohol Research Unit, National Public Health Institute, Helsinki, Finland and {ddagger} Department of Health Sciences, Alcuin College, University of York, Heslington, York, UK

2To whom correspondence should be addressed. E-mail: ross.hunter{at}kcl.ac.uk


   ABSTRACT
TOP
 ABSTRACT
MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 LITERATURE CITED
 
Alcoholic myopathy is characterized by decreased protein synthesis and contents resulting in atrophy of muscle fibers. We investigated the effect of alcohol on the cytoskeletal muscle proteins, nebulin and titin. Because women are more susceptible than men to the toxic effects of alcohol, male and female rats were included. Four groups were investigated: alcoholic males, pair-fed males, alcoholic females, pair-fed females. Alcohol consumption per unit body weight was 12.9 g/kg·d, with no difference between males and females. After 10 wk, male and female rats fed alcohol had lower gastrocnemius and plantaris protein and RNA contents (P < 0.001), with no effect on soleus, indicating myopathy of type II fibers. The gastrocnemius was fractionated to measure myofibrillary protein contents. Low percentage SDS-gel electrophoresis was performed to determine myosin heavy chain (MHC), nebulin and titin contents. Alcohol reduced gastrocnemius myofibrillary protein and MHC contents, and the plantaris RNA/protein ratio (P < 0.01). The titin/MHC and nebulin/MHC ratios were unaffected, suggesting a concomitant reduction in titin and nebulin. The decreases in titin and nebulin contents may affect muscle function. An interaction between gender and alcohol was noted for the plantaris RNA/protein ratio (P < 0.025), suggesting a reduced capacity for muscle protein synthesis in females.

KEY WORDS: • alcohol • titin • nebulin • protein • muscle

Skeletal muscle myopathy attributed to alcoholism occurs in between one third and two thirds of all chronic alcohol abusers, and is a major cause of morbidity (1 ,2 ). Alcoholic myopathy is characterized, in both humans and rats, by a reduction in skeletal muscle protein synthesis, total RNA and protein content, and more specifically, the myofibrillary protein contents (3 –8 ). These changes are confined to muscles rich in type II muscle fibers such as plantaris and gastrocnemius, with soleus (type I fiber predominant) being relatively unaffected (5 ). Light microscopy with staining for type II fibers confirms that these changes are fiber type specific (9 ).

The muscular weakness accompanying alcoholic myopathy may therefore be ascribed to a reduction in the contractile apparatus and/or disruption of the contractile process. However, aside from the actual contractile proteins, there are many other proteins intimately involved in the contractile process. Titin (connectin) is a giant filamentous protein that spans from the Z disc to the M line, thereby forming a third filament system of the sarcomere, contributing to passive force development of relaxed muscle fibers, and maintaining the structural integrity of the myofibril during contraction (10 ). The A band section of titin provides regular binding sites for other sarcomeric proteins, and so may contribute to sarcomere assembly (11 ,12 ). The I band section consists of immunoglobulin-like domains, and the PEVK segment, both of which contribute to the extensibility and passive force development of relaxed skeletal muscle fibers when stretched (10 ). The titin molecule also contains phosphorylation sites, a serine/threonine kinase domain and binding sites for muscle-specific calpain proteases, indicating that it may also play a role in myofibrillar signal transduction pathways (11 ). Nebulin is an inextensible filamentous giant protein associated with the Z disc, thought to act as a molecular ruler to specify the length of the actin thin filament (13 ). Nebulin may also act as scaffolding to which actin monomers must join during sarcomere assembly, therefore playing a role in myofibrillary synthesis (14 ).

This study was designed to quantify changes in the cytoskeletal proteins nebulin and titin attributed to alcohol. We used the new high fat, alcohol feeding regimen, previously shown to cause histological liver lesions exceeding those caused by traditional high carbohydrate diets (15 ). Clinically, women are more susceptible than men to alcoholic myopathy, cardiomyopathy and liver disease (16 ,17 ), so we investigated whether there was any interaction between the effects of alcohol and gender on skeletal muscle biochemistry, to see whether a biochemical basis for this clinical observation could be found.


   MATERIALS AND METHODS
TOP
 ABSTRACT
 MATERIALS AND METHODS
RESULTS
 DISCUSSION
 LITERATURE CITED
 
Treatment of animals.

All rats were treated in accordance with the ethical guidelines provided by the university at which the study was conducted. Wistar rats (Mollegaard, Ejby, Denmark) were individually housed in stainless steel wire cages. There were four groups: 1) male rats consumed the alcohol containing diet ad libitum, 2) male rats pair-fed the control diet, 3) female rats consumed the alcohol containing diet ad libitum, 4) female rats pair-fed the control diet. In alcohol feeding studies, the control rats should always be pair-fed to the alcohol group to control for the anorexia and reduced food consumption of rats fed alcohol (3 –8 ). The mean daily intake of the rats fed alcohol was recorded, and weight-matched controls were pair-fed the same amount of the control diet the subsequent day.

The high fat/low carbohydrate liquid feeding regimen was used as described previously (15 ). This involved modification of the Lieber–DeCarli diet (LD101 and LD101A; Purina Mills, Richmond, IN) described previously (18 ). A 50% level of energy was provided by the LD101A diet (LD101 in controls), and corn oil was added to increase the fat content from 35 to 44%, with a corresponding decrease in the content of carbohydrate from 11 to 5.5% (or from 47 to 40% in controls). The percentage of energy supplied as ethanol was 34.5% (compared to 36% in the Lieber–DeCarli diet). Casein, vitamins and minerals (technical grade; Sigma, St. Louis, MO) were added to equal the composition of the Lieber–DeCarli diet. In addition, carboxymethylcellulose (CMC, 4 g/L; Metsa Specialty Chemicals Oy, Aanekoski, Finland) was added as a stabilizer to increase viscosity. The metabolically inert CMC is widely used as a thickener in a variety of dairy and other food industry products. There was no difference between the male and female rats in the daily consumption of alcohol per unit body weight (12.9 g/kg), with consistent elevation of diurnal blood ethanol levels (40.3 ± 14.9 mmol/L) that did not differ between genders (15 ).

Body weights are not presented because it has been previously shown that in glucose fed control and alcohol fed rats, body weights can change markedly over a day because of episodic engorgement of the liquid diets, so that body weights are not meaningful (19 ). Alcohol has been previously shown to reduce muscle weight (6 ,20 ).

After 10 wk, soleus, plantaris and gastrocnemius were removed, weighed and frozen in liquid nitrogen. Muscles were homogenized and assayed for protein and RNA. The myofibrillary protein fraction was isolated from gastrocnemius muscle by differential solubility and high speed centrifugation as described previously (21 ). Gastrocnemius protein was then analyzed for titin, nebulin and myosin heavy chain (MHC).

Tissue processing.

All steps, including homogenization, were carried out at 0–4°C, and all centrifugations were at 2000 x g for 10 min, unless otherwise stated. Muscles were homogenized in ice-cold water, and portions of homogenate containing 200–400 mg tissue were either immediately precipitated with perchloric acid to a final concentration of 0.2 mmol/L or used for protein fractionation (described later).

Mixed protein and RNA.

After the first precipitation, the acid supernatant was discarded after centrifugation and the protein pellet was then washed twice with perchloric acid (0.2 mmol/L). The pellet was then subjected to alkali digestion in NaOH (0.3 mol/L) before protein estimation by the Biuret reaction (22 ). The protein was then reprecipitated, and RNA was measured in the supernatant (3 –5 ).

Protein fractionation.

Homogenates from the above procedures (containing 200 mg tissue) were immediately transferred to 20 mL of low ionic strength buffer, pH 7.0 [imidazole, 10 mmol; KCl, 60 mmol; EGTA, 0.5 mmol; MgCl2, 4.0 mmol; sodium azide, 1.0 mmol; and dithiothreitol, 1.0 mmol/L plus 0.5% (v/v) Triton X-100] (22 ). After centrifugation at 33,000 x g, the supernatant was discarded. The protein pellet was then disrupted in a ground-glass homogenizer with 10 mL of high ionic strength [potassium dihydrogen orthophosphate, 100 mmol; dipotassium hydrogen orthophosphate, 50 mmol; KCl, 300 mmol; EDTA, 1.0 mmol; and ATP, 5.0 mmol/L, pH 6.3 (22 )]. After centrifugation at 33,000 x g, supernatants containing solubilized "myofibrillar" proteins were decanted. The protein fractions were then processed as described above. Measurement of myofibrillary protein is quantitative, with a fractional recovery of ~100% (3 ,21 ).

SDS-gel electrophoresis.

Low percentage SDS–polyacrylamide gel electrophoresis (SDS–PAGE) was employed to investigate high-molecular-weight proteins in rat gastrocnemius muscles. Procedures were carried out essentially as described previously (23 ). Briefly, agarose-strengthened 2.8% polyacrylamide gels with a Laemmli buffer system (24 ) were prepared to detect titin, nebulin and myosin. Equal amounts of solubilized tissue were loaded in each lane, and the protein contents were then measured spectrophotometrically, by use of a protein assay, to ensure equal loading between lanes (Bio-Rad protein assay; Bio-Rad Laboratories GmbH, Munich, Germany). Approximately 100 µg of protein was loaded in each lane, but greater emphasis was placed on equal loading of the lanes. Protein bands were visualized with Coomassie brilliant blue R. Titin and nebulin were previously sequenced for rabbit soleus muscle (molecular weights of 3700 and 800 kDa, respectively), so rabbit soleus was used as a standard to verify that the bands obtained were in fact titin and nebulin (24 ). Gel images were scanned at a resolution of 600 dpi. Protein bands on scanned gels were analyzed for their optical volume (integrated optical density), using TotalLab software (Phoretix, Newcastle-upon-Tyne, UK). This ensured that gels were assessed objectively, given that ratios were used to express titin and nebulin relative to MHC. Data were expressed as ratios to account for variation between gels. Density ratios between proteins of interest were calculated after constructing calibration curves for myosin, nebulin and titin. The optical volume/mg of total protein was then calculated.

Statistics.

Data are expressed as means ± SEM, n = 7–10. Data were compared using two-way ANOVA, with differences of P < 0.05 considered significant.


   RESULTS
TOP
 ABSTRACT
 MATERIALS AND METHODS
 RESULTS
DISCUSSION
 LITERATURE CITED
 
Alcohol decreased the gastrocnemius and plantaris protein and RNA contents in both males and females (Table 1 ). The gastrocnemius myofibrillary protein fraction (Table 1) and MHC (Table 2 ) were also reduced. Soleus RNA and protein contents of soleus, a type I fiber–predominant muscle, were unaffected by alcohol (Table 1) , indicating that the high fat, alcohol diet induced a type II fiber myopathy. Alcohol reduced the plantaris RNA/protein ratio by 5% in males and 13% in females (Table 3 ), with a significant interaction between alcohol and gender (P < 0.025). This ratio was unaffected in soleus and gastrocnemius muscles.


View this table:
[in this window]
[in a new window]
  		TABLE 1 Muscle RNA and protein contents in male and female Wistar rats fed control and ethanol-containing diets for 10 wk12

 

View this table:
[in this window]
[in a new window]
  		TABLE 2 Myosin heavy chain (MHC) content ratios of MHC to titin or nebulin in gastrocnemius muscle of male and female Wistar rats fed control and ethanol-containing diets for 10 wk12

 

View this table:
[in this window]
[in a new window]
  		TABLE 3 Muscle RNA/protein ratios in male and female Wistar rats fed control and ethanol-containing diets for 10 wk12

 
Because alcohol decreased gastrocnemius MHC but not the titin/MHC and nebulin/MHC ratios, it also reduced the levels of titin and nebulin (Table 2) . Representative gels showing the clear resolution of MHC, titin and nebulin are shown in Figure 1 .



View larger version (47K):
[in this window]
[in a new window]
  		FIGURE 1 A 2.8% SDS–polyacrylamide gel showing separation of titin, nebulin and MHC bands for gastrocnemius muscle of control male and female rats. To verify the identity of the bands labeled titin and nebulin, rabbit soleus was run as a standard because titin and nebulin have both been sequenced in this muscle.

 

   DISCUSSION
TOP
 ABSTRACT
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
LITERATURE CITED
 
Alcoholic myopathy is characterized by lean tissue wasting, with a reduction in total RNA and protein contents, and specific proteins such as desmin, actin, troponins I and T, and the MHC isoforms (3 –8 ). However, other noncontractile proteins are intimately related to the contractile process such as the sarcomeric cytoskeletal proteins, titin and nebulin. We tested the hypothesis that nebulin and titin would also be affected by ethanol consumption.

The effect of alcohol on skeletal muscle biochemistry.

The ethanol feeding regimen used resulted in a myopathy of type II fibers, as evidenced by the reduced protein contents in gastrocnemius and plantaris muscles (type II fiber rich), with no effect on soleus (type I fiber predominant). This is well documented in other alcohol feeding studies (6 ). The myofibrillary protein contents and MHC specifically were also reduced, indicating that the contractile proteins in particular were affected by alcohol, as has been demonstrated in conventional alcohol feeding studies (8 ). A reduction in tissue synthetic potential was also demonstrated by the decreased RNA/protein ratio in the plantaris muscle.

The effect of alcohol on titin and nebulin.

Titin contributes to the passive force development of relaxed muscle fibers, maintains the structural integrity of the myofibril during contraction and may also be involved in sarcomere assembly and turnover (10 ). Titin has been implicated in several disease processes such as limb girdle muscular dystrophy type 2a and cardiac failure (25 ,26 ). Nebulin binds tightly to actin and may control the length of actin filaments (13 ). Genetic mutations in the nebulin gene are associated with nemaline myopathy (27 ,28 ). Therefore, titin and nebulin play important roles in normal muscle physiology and in disease.

Titin and nebulin contents were expressed relative to MHC. The titin/MHC and nebulin/MHC ratios were unaffected by alcohol, which indicates that titin and nebulin are reduced proportionately to the decrease in MHC. This reduction in titin and nebulin may decrease the stability of the sarcomere and myofibrils at rest and during contraction, which may impair muscle tension generation and function.

The effect of gender.

Because women are clinically more susceptible than men to the pathological effects of alcohol (16 ,17 ), male and female groups were included to explore any effect of gender on alcohol-induced perturbations in skeletal muscle biochemistry. The RNA/protein ratio in plantaris muscle showed an alcohol/gender interaction, with a greater reduction in females. The RNA/protein ratio is a measure of the tissues capacity for protein synthesis (29 ). The protein content is a static measure that gives little insight into rates of synthesis and proteolysis. The decreased protein content in alcoholic myopathy is attributed to reduced rates of protein synthesis. This is thought to be under both translational and transcriptional control, with a reduction in ribosomal RNA, attributed at least in part to increased RNase activity (30 ). The interaction between gender and alcohol for this variable may indicate differences between the sexes in the effects of alcohol on RNase activity.

This is the first study to explore changes in skeletal muscle expression of titin and nebulin in alcoholic myopathy. Titin and nebulin were reduced in proportion to the reduction in MHC. The decrease in titin and nebulin contents may affect muscle function. The data also showed for the first time that female rats are more susceptible than males to the adverse effects of alcohol on skeletal muscle biochemistry.


   FOOTNOTES
 
1 This work was funded by a grant from the Pathological Society of Great Britain and Ireland. Back

3 Abbreviations used: CMC, carboxymethylcellulose; MHC, myosin heavy chain. Back

Manuscript received 4 July 2002. Initial review completed 24 July 2002. Revision accepted 1 October 2002.


   LITERATURE CITED
TOP
 ABSTRACT
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 LITERATURE CITED
 

1. Martin, F., Ward, K., Slavin, G., Levi, J. & Peters, T. J. (1985) Alcoholic skeletal myopathy, a clinical and pathological study. Q. J. Med. 55:233-251.

2. Urbano Marquez, A., Estruch, R., Navarro Lopez, F., Grau, J. M., Mont, L. & Rubin, E. (1989) The effects of alcoholism on skeletal and cardiac muscle. N. Engl. J. Med. 320:409-415.[Abstract]

3. Preedy, V. R. & Peters, T. J. (1988) Acute effects of ethanol on protein synthesis in different muscles and muscle protein fractions of the rat. Clin. Sci. 74:461-466.[Medline]

4. Preedy, V. R. & Peters, T. J. (1988) The effect of chronic ethanol feeding on body and plasma composition and rates of skeletal muscle protein turnover in the rat. Alcohol 23:217-224.

5. Preedy, V. R. & Peters, T. J. (1988) The effect of chronic ethanol ingestion on protein metabolism in type-I and type-II-fiber-rich skeletal muscles of the rat. Biochem. J. 254:631-639.[Medline]

6. Preedy, V. R., Duane, P. & Peters, T. J. (1988) Biological effects of chronic ethanol consumption: a reappraisal of the Lieber-DeCarli liquid-diet model with reference to skeletal muscle. Alcohol Alcohol 23:151-154.[Abstract/Free Full Text]

7. Marway, J. S., Preedy, V. R. & Peters, T. J. (1990) Experimental alcoholic skeletal muscle myopathy is characterised by a rapid and sustained decrease in muscle RNA content. Alcohol 25:401-406.

8. Reilly, M. E., McKoy, G., Mantle, D., Peters, T. J., Goldspink, G. & Preedy, V. R. (2000) Protein and mRNA levels of the myosin heavy chain isoforms 1ß, IIa, IIx, and IIb in Type I and Type II fiber-predominant rat skeletal muscles in response to chronic alcohol feeding. J. Muscle Res. Cell. Motil. 21:763-773.[Medline]

9. Slavin, G., Martin, F., Ward, P., Levi, J. & Peters, T. (1983) Chronic alcohol excess is associated with selective but reversible injury to type 2B muscle fibers. J. Clin. Pathol. 36:772-777.[Abstract/Free Full Text]

10. Linke, W. A. (2000) Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol. Histopathol. 15:799-811.[Medline]

11. Labeit, S., Kolmerer, B. & Linke, W. A. (1997) The giant protein titin. Emerging roles in physiology and pathophysiology. Circ. Res. 80:290-294.[Abstract/Free Full Text]

12. Gregorio, C. C., Granzier, H., Sorimachi, H. & Labeit, S. (1999) Muscle assembly: a titanic achievement?. Curr. Opin. Cell Biol. 11:18-25.[Medline]

13. McElhinny, A. S., Kolmerer, B., Fowler, V. M., Labeit, S. & Gregorio, C. C. (2001) The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments. J. Biol. Chem. 276:583-592.[Abstract/Free Full Text]

14. Nwe, T. M. & Shimada, Y. (2000) Inhibition of nebulin and connectin (titin) for assembly of actin filaments during myofibrillogenesis. Tissue Cell 32:223-227.[Medline]

15. Lindros, K. O. & Jarvelainen, H. A. (1998) A new oral low-carbohydrate alcohol liquid diet producing liver lesions: a preliminary account. Alcohol Alcohol 33:347-353.[Abstract/Free Full Text]

16. Urbano-Marquez, A., Estruch, R., Fernandez-Sola, J., Nicolas, J. M., Pare, J. C. & Rubin, E. (1995) The greater risk of alcoholic cardiomyopathy and myopathy in women compared with men. J. Am. Med. Assoc. 274:149-154.[Abstract]

17. Thurman, R. G. (2000) Sex-related liver injury due to alcohol involves activation of Kupffer cells by endotoxin. Can. J. Gastroenterol. 14D:129D-135D.

18. Kim, C., Leo, M. A., Lowe, N. & Lieber, C. S. (1988) Differential effects of retinoids and chronic ethanol consumption on membranes in rats. J. Nutr. 118:1097-1103.

19. Preedy, V. R., Marway, J. S. & Peters, T. J. (1989) Changes in tissue weight and RNA using the Lieber-DeCarli feeding regime. Alcohol Alcohol 24:439-445.[Abstract/Free Full Text]

20. Preedy, V. R. & Peters, T. J. (1987) The young rat as a model for alcohol-induced skeletal muscle myopathy. Biochem. Soc. Trans. 15:1166.

21. Preedy, V. R. & Peters, T. J. (1989) Synthesis and subcellular protein fractions in the rat heart in vivo in response to chronic ethanol feeding. Cardiovasc. Res. 23:730-736.[Medline]

22. Hunter, R. J., Patel, V. B., Miell, J. P., Wong, H. J., Marway, J. S., Richardson, P. J. & Preedy, V. R. (2001) Diarrhea reduces the rates of cardiac protein synthesis in myofibrillar protein fractions in rats in vivo. J. Nutr. 131:1513-1519.[Abstract/Free Full Text]

23. Linke, W. A., Ivemeyer, M., Labeit, S., Hinssen, H., Rüegg, J. C. & Gautel, M. (1997) Actin-titin interaction in cardiac myofibrils: probing a physiological role. Biophys. J. 73:905-919.[Abstract/Free Full Text]

24. Neagoe, C., Kulke, M., del Monte, F., Gwathmey, J. K., de Tombe, P. P., Hajjar, R. J. & Linke, W. A. (2002) Titin isoform switch in ischemic human heart disease. Circulation 106:1333-1341.[Abstract/Free Full Text]

25. Hein, S., Kostin, S., Heling, A., Maeno, Y. & Schaper, J. (2000) The role of the cytoskeleton in heart failure. Cardiovasc. Res. 45:273-278.[Abstract/Free Full Text]

26. Sorimachi, H., Ono, Y. & Suzuki, K. (2000) Skeletal muscle-specific calpain, p94, and connectin/titin: their physiological functions and relationship to limb-girdle muscular dystrophy type 2A. Adv. Exp. Med. Biol. 481:383-395.[Medline]

27. Wallgren-Pettersson, C., Pelin, K., Hilpela, P., Donner, K., Porfirio, B., Graziano, C., Swoboda, K. J., Fardeau, M., Urtizberea, J. A., Muntoni, F., Sewry, C., Dubowitz, V., Iannaccone, S., Minetti, C., Pedemonte, M., Seri, M., Cusano, R., Lammens, M., Castagna-Sloane, A., Beggs, A. H., Laing, N. G. & de la Chapelle, A. (1999) Clinical and genetic heterogeneity in autosomal recessive nemaline myopathy. Neuromuscul. Disord. 9:564-572.[Medline]

28. Laing, N. G. (1999) Inherited disorders of sarcomeric proteins. Cur. Opin. Neurol. 12:513-518.[Medline]

29. Preedy, V. R., Why, H. J. F., Paice, A. G., Reilly, M. E., Ansell, H., Patel, V. B. & Richardson, P. J. (1995) Protein synthesis in the heart in vivo: its measurement and patho-physiological alterations. Int. J. Cardiol. 50:95-106.[Medline]

30. Reilly, M. E., Erylmaz, E. I., Amir, A., Peters, T. J. & Preedy, V. R. (1998) Skeletal muscle ribonuclease activities in chronically ethanol-treated rats. Alcohol Clin. Exp. Res. 22:876-883.[Medline]




This article has been cited by other articles:


Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
C. H. Lang, R. A. Frost, and T. C. Vary
Skeletal muscle protein synthesis and degradation exhibit sexual dimorphism after chronic alcohol consumption but not acute intoxication
Am J Physiol Endocrinol Metab, June 1, 2007; 292(6): E1497 - E1506.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
T. Nakahara, K. Hashimoto, M. Hirano, M. Koll, C. R. Martin, and V. R. Preedy
Acute and chronic effects of alcohol exposure on skeletal muscle c-myc, p53, and Bcl-2 mRNA expression
Am J Physiol Endocrinol Metab, December 1, 2003; 285(6): E1273 - E1281.
[Abstract] [Full Text] [PDF]

This Article
Right arrow Abstract Freely available
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hunter, R. J.
Right arrow Articles by Preedy, V. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hunter, R. J.
Right arrow Articles by Preedy, V. R.

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]