title: Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men.
abstract: This study was designed to compare the acute response of mixed muscle protein synthesis (MPS) to rapidly (i.e., whey hydrolysate and soy) and slowly (i.e., micellar casein) digested proteins both at rest and after resistance exercise. Three groups of healthy young men (n = 6 per group) performed a bout of unilateral leg resistance exercise followed by the consumption of a drink containing an equivalent content of essential amino acids (10 g) as either whey hydrolysate, micellar casein, or soy protein isolate. Mixed MPS was determined by a primed constant infusion of l-[ring-(13)C(6)]phenylalanine. Ingestion of whey protein resulted in a larger increase in blood essential amino acid, branched-chain amino acid, and leucine concentrations than either casein or soy (P < 0.05). Mixed MPS at rest (determined in the nonexercised leg) was higher with ingestion of faster proteins (whey = 0.091 +/- 0.015, soy = 0.078 +/- 0.014, casein = 0.047 +/- 0.008%/h); MPS after consumption of whey was approximately 93% greater than casein (P < 0.01) and approximately 18% greater than soy (P = 0.067). A similar result was observed after exercise (whey > soy > casein); MPS following whey consumption was approximately 122% greater than casein (P < 0.01) and 31% greater than soy (P < 0.05). MPS was also greater with soy consumption at rest (64%) and following resistance exercise (69%) compared with casein (both P < 0.01). We conclude that the feeding-induced simulation of MPS in young men is greater after whey hydrolysate or soy protein consumption than casein both at rest and after resistance exercise; moreover, despite both being fast proteins, whey hydrolysate stimulated MPS to a greater degree than soy after resistance exercise. These differences may be related to how quickly the proteins are digested (i.e., fast vs. slow) or possibly to small differences in leucine content of each protein.
authors: Department of Kinesiology-Exercise Metabolism Research Group, McMaster University, Hamilton, Ontario L8S 4K1, Canada.
authors: Jason E
authors: JE
authors: Tang
authors: Daniel R
authors: DR
authors: Moore
authors: Gregory W
authors: GW
authors: Kujbida
authors: Mark A
authors: MA
authors: Tarnopolsky
authors: Stuart M
authors: SM
authors: Phillips
mesh_terms: D000328:Adult; D000465:Algorithms; D000596:Amino Acids / Q000032:analysis / Q000378:metabolism; D002364:Caseins / Q000494:pharmacology*; D015444:Exercise / Q000502:physiology*; D008401:Gas Chromatography-Mass Spectrometry; D006801:Humans; D007328:Insulin / Q000097:blood; D008297:Male; D008894:Milk Proteins / Q000494:pharmacology*; D018482:Muscle, Skeletal / Q000187:drug effects / Q000378:metabolism*; D010649:Phenylalanine / Q000097:blood / Q000378:metabolism; D011492:Protein Hydrolysates / Q000494:pharmacology*; D030262:Soybean Proteins / Q000494:pharmacology*; D013268:Stimulation, Chemical; D014891:Weight Lifting / Q000502:physiology*; D000067816:Whey Proteins; D055815:Young Adult
chemical_list: D000596:Amino Acids; D002364:Caseins; D007328:Insulin; D008894:Milk Proteins; D011492:Protein Hydrolysates; D030262:Soybean Proteins; D000067816:Whey Proteins; D010649:Phenylalanine