Evaluation of pea/rice and amylopectin/chromium as an alternative protein source to improve muscle protein synthesis in rats

Eur J Nutr. 2023 Aug;62(5):2293-2302. doi: 10.1007/s00394-023-03150-8. Epub 2023 Apr 25.

Abstract

Background: A preclinical study reported that the combination of an amylopectin/chromium complex (ACr) of branched-chain amino acids (BCAA) significantly enhanced muscle protein synthesis (MPS). This study was conducted to determine the effects of the addition of ACr complex to a pea/rice (PR) protein on MPS, insulin, muslin levels, and the mTOR pathway in exercised rats.

Methods: Twenty-four rats were divided into three groups: (i) exercise (Ex); (ii) Ex + PR 1:1 blend (0.465 g/kg BW); (iii) Ex + PR + ACr (0.155 g/kg BW). On the day of single-dose administration, after the animals were exercised at 26/m/min for 2 h, the supplement was given by oral gavage. The rats were injected with a bolus dose (250 mg/kg BW, 25 g/L) of deuterium-labeled phenylalanine to determine the protein fractional synthesis rate (FSR) one h after consuming the study product.

Results: The combination of PR and ACr enhanced MPS by 42.55% compared to the Ex group, while Ex + PR alone increased MPS by 30.2% over the Ex group (p < 0.0001) in exercised rats. Ex + PR plus ACr significantly enhanced phosphorylation of mTOR and S6K1 (p < 0.0001), and 4E-BP1 (p < 0.001) compared to the Ex (p < 0.0001). PR to ACr also significantly increased insulin and musclin levels (p < 0.0001) in exercised rats. Additionally, compared to Ex + PR alone, Ex + PR + ACr enhanced mTOR (p < 0.0001) and S6K1 (p < 0.0001) levels.

Conclusion: These data suggested that PR + ACr may provide an alternative to animal proteins for remodeling and repairing muscle by stimulating MPS and mTOR signaling pathways in post-exercised rats. More preclinical and clinical human studies on combining pea/rice and amylopectin/chromium complex are required.

Keywords: Amylopectin/chromium; Essential amino acids; Insulin sensitivity; Musclin; Pea/rice protein blend.

MeSH terms

  • Amylopectin / metabolism
  • Amylopectin / pharmacology
  • Animals
  • Chromium
  • Humans
  • Insulins* / metabolism
  • Insulins* / pharmacology
  • Muscle Proteins
  • Muscle, Skeletal / metabolism
  • Oryza*
  • Phosphorylation
  • Pisum sativum
  • Rats
  • TOR Serine-Threonine Kinases / metabolism

Substances

  • Muscle Proteins
  • Amylopectin
  • Chromium
  • TOR Serine-Threonine Kinases
  • Insulins