The addition of an amylopectin/chromium complex to branched-chain amino acids enhances muscle protein synthesis in rat skeletal muscle

Figures & data

Fig. 1 The effect of supplementation with an amylopectin/chromium complex and branched-chain amino acids on the fractional rate of protein synthesis (FSR). Values represent the means and standard errors of three different analyses. Significant between-group differences are represented with different letters (p < 0.05)

Table 1 The effect of an amylopectin/chromium complex and branched-chain amino acids on serum amino acids levels

Fig. 2 The effect of supplementation with an amylopectin/chromium complex and branched-chain amino acids on serum insulin levels. Values represent the means and standard errors of three different analyses. Significant between-group differences are represented with different letters (p < 0.05)

Fig. 3 The effect of supplementation with an amylopectin/chromium complex and branched-chain amino acids on protein levels of the mammalian target of rapamycin (mTOR), ribosomal protein S6 kinase beta-1 (S6K1) and eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1). mTOR (a), S6K1 (b) and 4E-BP1 (c) in rat tissues, detected by Western blot analysis. Data are the percent of the exercise (set to 100%). Values represent the means and standard errors of three different analyses. Actin expression was used to ensure equal protein loading. Significant between-group differences are represented with different letters (p < 0.05)

Table 2 Pearson’s correlation coefficients (r) correlations among FSR, insulin, mTOR, pS6K1, and 4E-BP1

Availability of data and materials

The data and materials for this manuscript are not scheduled to be made publicly available due to the proprietary nature of the investigated materials. Contractually, the data is owned by Nutrition 21, LLC, not any of the authors.