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Combination of Soy Protein, Amylopectin, and Chromium Stimulates Muscle Protein Synthesis by Regulation of Ubiquitin–Proteasome Proteolysis Pathway after Exercise

  • Veysi Kayri
  • Cemal Orhan
  • Mehmet Tuzcu
  • Patrick Brice Deeh Defo
  • Hafize Telceken
  • Mehmet Irmak
  • Nurhan Sahin
  • Hakki Tastan
  • James R. Komorowski
  • Kazim Sahin
Article

Abstract

The present study was undertaken to investigate the effect of the combination of soy protein, amylopectin, and chromium (SAC) on muscle protein synthesis and signal transduction pathways involved in protein synthesis (mTOR pathways, IGF-1, and AktSer473) and proteolysis (FOXO1Ser256; MURF1, MAFbx) after exercise. Thirty-five Wistar rats were randomly divided into five groups: (1) control (C); (2) exercise (E); (3) exercise + soy protein (3.1 g/kg/day) (E + S); (4) exercise + soy protein + chromium (E + S + Cr); (5) exercise + soy protein + amylopectin + chromium (E + S + A + Cr). Post-exercise ingestion of SAC significantly increased the fractional rate of protein synthesis (FSR), insulin, glycogen, and amino acid levels with the highest effect observed in E + S + A + Cr group (P ˂ 0.05). However, SAC supplementation decreased the lactic acid concentration (P ˂ 0.05). A reduction in forkhead box protein O1 (FOXO1) and forkhead box protein O3 (FOXO3) (regulators of ubiquitin-related proteolysis) and muscle atrophy F-box (MAFbx) levels was noted after treatment with SAC (P < 0.05). Insulin-like growth factor 1(IGF-1) level was increased in the E + S, E + S + Cr, and E + S + A + Cr groups (P < 0.05). While the phosphorylation of 4E-BP1Thr37/46, AktSer473, mTORSer2448, and S6K1Thr389 levels increased after SAC supplementation, phosphorylated muscle ring finger 1 (MuRF-1, an E3-ubiquitin ligase gene) was found to be significantly lower compared with the E group (P ˂ 0.05). These results indicate that SAC supplementation improves FSR, insulin, and glycogen levels after exercise. SAC improves protein synthesis by inhibiting the ubiquitin–proteasome pathway and inducing anabolic metabolism.

Keywords

Soy protein Amylopectin Chromium Protein synthesis Ubiquitin–proteasome pathway 

Notes

Acknowledgments

This work was granted by Firat University Scientific Research Projects Unit (VF.16.20) and the Turkish Academy of Sciences (K.S.). The authors thank Nutrition21 (Purchase, NY, USA) for providing amylopectin + chromium and to Mr. Besir Er for his kind efforts during this study.

Authors’ Contributions

K.S. and J.R.K. participated in the study design and drafting the manuscript. C.O., M.T., and N.S. participated in the data collection and assays, data analysis, and drafting the manuscript. C.O. and D.D.P.B. participated in the data analysis and statistical analysis for the variables and drafting the manuscript. K.S. and J.R.K. participated in drafting the manuscript. All authors read and approved the final manuscript.

Compliance with Ethical Standards

Conflict of Interest

The authors declare that there are no conflicts of interest. J.R.K. is employed by Nutrition21, Purchase, NY, USA.

Compliance with Ethical Standards

All animal experimental procedures followed protocols approved by the Experimental Animal Ethics Committee of Firat University (Elazig, Turkey).

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  • Veysi Kayri
    • 1
  • Cemal Orhan
    • 1
  • Mehmet Tuzcu
    • 2
  • Patrick Brice Deeh Defo
    • 3
  • Hafize Telceken
    • 1
  • Mehmet Irmak
    • 1
  • Nurhan Sahin
    • 1
  • Hakki Tastan
    • 4
  • James R. Komorowski
    • 5
  • Kazim Sahin
    • 1
  1. 1.Department of Animal Nutrition, Faculty of Veterinary MedicineFirat UniversityElazigTurkey
  2. 2.Division of Biology, Faculty of ScienceFirat UniversityElazigTurkey
  3. 3.Department of Animal Biology, Faculty of ScienceUniversity of DschangDschangCameroon
  4. 4.Department of Biology, Faculty of ScienceGazi UniversityAnkaraTurkey
  5. 5.Scientific and Regulatory AffairsNutrition 21 IncPurchaseUSA

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