Purpose: Studies that have attributed gains in lean body mass to dietary supplementation during resistance exercise (RE) training have not reported these changes alongside adaptations at the cellular and subcellular levels. Therefore, the purpose of this study was to examine the effects of two popular supplements--whey protein (WP) and creatine monohydrate (CrM) (both separately and in combination)--on body composition, muscle strength, fiber-specific hypertrophy (i.e., type I, IIa, IIx), and contractile protein accrual during RE training.
Methods: In a double-blind randomized protocol, resistance-trained males were matched for strength and placed into one of four groups: creatine/carbohydrate (CrCHO), creatine/whey protein (CrWP), WP only, or carbohydrate only (CHO) (1.5 g x kg(-1) body weight per day). All assessments were completed the week before and after an 11-wk structured, supervised RE program. Assessments included strength (1RM, three exercises), body composition (DEXA), and vastus lateralis muscle biopsies for determination of muscle fiber type (I, IIa, IIx), cross-sectional area (CSA), contractile protein, and creatine (Cr) content.
Results: Supplementation with CrCHO, WP, and CrWP resulted in significantly greater (P < 0.05) 1RM strength improvements (three of three assessments) and muscle hypertrophy compared with CHO. Up to 76% of the strength improvements in the squat could be attributed to hypertrophy of muscle involved in this exercise. However, the hypertrophy responses within these groups varied at the three levels assessed (i.e., changes in lean mass, fiber-specific hypertrophy, and contractile protein content).
Conclusions: Although WP and/or CrM seem to promote greater strength gains and muscle morphology during RE training, the hypertrophy responses within the groups varied. These differences in skeletal muscle morphology may have important implications for various populations and, therefore, warrant further investigation.
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http://dx.doi.org/10.1249/01.mss.0000247002.32589.ef | DOI Listing |
Metab Brain Dis
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Hepato-Neuro Laboratory, Centre Hospitalier de l'Université de Montréal (CRCHUM), Université de Montréal, 900, Rue Saint-Denis - Pavillon R, R08.422, Montréal (Québec), H2X 0A9, Canada.
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Department of Physics and Astronomy, University of Denver, Denver, CO, USA.
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Laboratorio de Neuroinflamacion i2-06, Hospital Nacional de Paraplejicos, Finca La Peraleda s/n, Toledo, 45071, Spain.
Spinal cord injury (SCI) causes abnormal liver function, the development of metabolic dysfunction-associated steatotic liver disease features and metabolic impairment in patients. Experimental models also demonstrate acute and chronic changes in the liver that may, in turn, affect SCI recovery. These changes have collectively been proposed to contribute to the development of a SCI-induced metabolic dysfunction-associated steatohepatitis (MASH).
View Article and Find Full Text PDFCell Death Dis
January 2025
Department of Anatomical, Histological, Forensic Sciences and Orthopedics, Sapienza University of Rome, 00161, Rome, Italy.
Sarcoglycanopathies are heterogeneous proximo-distal diseases presenting severe muscle alterations. Although there are 6 different sarcoglycan isoforms, sarcoglycanopathies are caused exclusively by mutations in genes coding for one of the four sarcoglycan transmembrane proteins (alpha, beta, gamma and delta) forming the sarcoglycan complex (SGC) in skeletal and cardiac muscle. Little is known about the different roles of the SGC beyond the dystrophin glycoprotein complex (DGC) structural role.
View Article and Find Full Text PDFNat Commun
January 2025
Department of Pharmacology and Therapeutics, University of Florida, Gainesville, FL, USA.
Assembly of actin-based stereocilia is critical for cochlear hair cells to detect sound. To tune their mechanosensivity, stereocilia form bundles composed of graded rows of ascending height, necessitating the precise control of actin polymerization. Myosin 15 (MYO15A) drives hair bundle development by delivering critical proteins to growing stereocilia that regulate actin polymerization via an unknown mechanism.
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