The assessment of in vivo protein synthesis following chronic resistance exercise using 2 H 2 O

2008 ◽  
Vol 22 (S2) ◽  
pp. 91-91 ◽  
Author(s):  
Heath G. Gasier ◽  
Michael P Wiggs ◽  
Stephen F Previs ◽  
Steven E Riechman ◽  
James D Fluckey
2001 ◽  
Vol 20 (2) ◽  
pp. 181-182 ◽  
Author(s):  
A. JANUSZKIEWICZ ◽  
P. ESSÉN ◽  
M.A. McNURLAN ◽  
O. RINGDÉN ◽  
P.J. GARLICK ◽  
...  

2000 ◽  
Vol 88 (3) ◽  
pp. 1036-1042 ◽  
Author(s):  
Peter A. Farrell ◽  
Jazmir M. Hernandez ◽  
Mark J. Fedele ◽  
Thomas C. Vary ◽  
Scot R. Kimball ◽  
...  

Translational control of protein synthesis depends on numerous eukaryotic initiation factors (eIFs) and we have previously shown ( Am. J. Physiol. Endocrinol. Metab. 276: E721–E727, 1999) that increases in one factor, eIF2B, are associated with increases in rates of protein synthesis after resistance exercise in rats. In the present study we investigated whether the eIF4E family of initiation factors is also involved with an anabolic response to exercise. Male Sprague-Dawley rats either remained sedentary ( n = 6) or performed acute resistance exercise ( n = 6), and rates of protein synthesis were assessed in vivo 16 h after the last session of resistance exercise. eIF4E complexed to eIF4G (eIF4E ⋅ eIF4G), eIF4E binding protein 1 (4E-BP1) complexed to eIF4E, and phosphorylation state of eIF4E and 4E-BP1 (γ-form) were assessed in gastrocnemius. Rates of protein synthesis were higher in exercised rats compared with sedentary rats [205 ± 8 (SE) vs. 164 ± 5.5 nmol phenylalanine incorporated ⋅ g muscle−1 ⋅ h−1, respectively; P < 0.05]. Arterial plasma insulin concentrations were not different between the two groups. A trend ( P = 0.09) for an increase in eIF4E ⋅ eIF4G with exercise was noted; however, no statistically significant differences were observed in any of the components of the eIF4E family in response to resistance exercise. These new data, along with our previous report on eIF2B, suggest that the regulation of peptide chain initiation after exercise is more dependent on eIF2B than on the eIF4E system.


1984 ◽  
Vol 36 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Suzanne M. Harley ◽  
Harry Beevers

1999 ◽  
Vol 276 (4) ◽  
pp. E721-E727 ◽  
Author(s):  
Peter A. Farrell ◽  
Mark J. Fedele ◽  
Thomas C. Vary ◽  
Scot R. Kimball ◽  
Charles H. Lang ◽  
...  

These studies determined whether insulin-like growth factor-I (IGF-I) involvement in exercise-stimulated anabolic processes becomes more evident during hypoinsulinemia. Male Sprague-Dawley rats ( n = 6–12/group) were made diabetic (blood glucose ≅ 300 mg/dl) by partial pancreatectomy (PPX) or remained nondiabetic (glucose ≅ 144 mg/dl). Rats performed acute resistance exercise by repetitive standing on the hindlimbs with weighted backpacks (ex), or they remained sedentary (sed). Resistance exercise caused increases in rates of protein synthesis (nmol Phe incorporated ⋅ g muscle−1 ⋅ h−1, measured for gastrocnemius muscle in vivo 16 h after exercise) for both nondiabetic [sed = 154 ± 6 (SE) vs. ex = 189 ± 7] and diabetic rats (PPXsed = 152 ± 11 vs. PPXex = 202 ± 14, P < 0.05). Arterial plasma insulin concentrations in diabetic rats, ≅180 pM, were less than one-half those found in nondiabetic rats, ≅444 pM, ( P < 0.05). The activity of eukaryotic initiation factor 2B (eIF2B; pmol GDP exchanged/min) was higher ( P < 0.05) in ex rats (sed = 0.028 ± 0.006 vs. ex = 0.053 ± 0.015; PPXsed = 0.033 ± 0.013 vs. PPXex = 0.047 ± 0.009) regardless of diabetic status. Plasma IGF-I concentrations were higher in ex compared with sed diabetic rats ( P < 0.05). In contrast, plasma IGF-I was not different in nondiabetic ex or sed rats. Muscle IGF-I (ng/g wet wt) was similar in ex and sed nondiabetic rats, but in diabetic rats was 2- to 3-fold higher in ex ( P < 0.05) than in sed rats. In conclusion, moderate hypoinsulinemia that is sufficient to alter glucose homeostasis does not inhibit an increase in rates of protein synthesis after acute moderate-intensity resistance exercise. This preserved response may be due to a compensatory increase in muscle IGF-I content and a maintained ability to activate eIF2B.


Biochemistry ◽  
1990 ◽  
Vol 29 (18) ◽  
pp. 4263-4268 ◽  
Author(s):  
Ranjan Chattapadhyay ◽  
Heike Pelka ◽  
LaDonne H. Schulman

2010 ◽  
Vol 42 ◽  
pp. 64
Author(s):  
Jared M. Dickinson ◽  
Jonah D. Lee ◽  
Bridget E. Sullivan ◽  
Matthew P. Harber ◽  
Scott W. Trappe ◽  
...  

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