Research shows that higher dietary protein of up to 1.2 g/kg_bodyweight/day may help prevent sarcopenia and maintain musculoskeletal health in older individuals. Achieving higher daily dietary protein levels is challenging, particularly for older adults with declining appetites and underlying health conditions. The negative impact of these limitations on aging muscle may be circumvented through the consumption of high-quality sources of protein and/or supplementation. Currently, there is a debate regarding whether source of protein differentially affects musculoskeletal health in older adults. Whey and soy protein have been used as the most common high-quality proteins in recent literature. However, there is growing consumer demand for additional plant-sourced dietary protein options. For example, pea protein is rapidly gaining popularity among consumers, despite little to no research regarding its long-term impact on muscle health. Therefore, the objectives of this review are to: (1) review current literature from the past decade evaluating whether specific source(s) of dietary protein provide maximum benefit to muscle health in older adults; and (2) highlight the need for future research specific to underrepresented plant protein sources, such as pea protein, to then provide clearer messaging surrounding plant-sourced versus animal-sourced protein and their effects on the aging musculoskeletal system.

Background: Individual skeletal muscles have evolved to perform specific tasks based on their molecular composition. In general, muscle fibers are characterized as either fast-twitch or slow-twitch based on their myosin heavy chain isoform profiles. This approach made sense in the early days of muscle studies when SDS-PAGE was the primary tool for mapping fiber type. However, Next Generation Sequencing tools permit analysis of the entire muscle transcriptome in a single sample, which allows for more precise characterization of differences among fiber types, including distinguishing between different isoforms of specific proteins. We demonstrate the power of this approach by comparing the differential gene expression patterns of extensor digitorum longus (EDL), psoas, and soleus from mice using high throughput RNA sequencing. Results: EDL and psoas are typically classified as fast-twitch muscles based on their myosin expression pattern, while soleus is considered a slow-twitch muscle. The majority of the transcriptomic variability aligns with the fast-twitch and slow-twitch characterization. However, psoas and EDL exhibit unique expression patterns associated with the genes coding for extracellular matrix, myofibril, transcription, translation, striated muscle adaptation, mitochondrion distribution, and metabolism. Furthermore, significant expression differences between psoas and EDL were observed in genes coding for myosin light chain, troponin, tropomyosin isoforms, and several genes encoding the constituents of the Z-disk. Conclusions: The observations highlight the intricate molecular nature of skeletal muscles and demonstrate the importance of utilizing transcriptomic information as a tool for skeletal muscle characterization.

Context: : Injury-prediction models have identified trunk muscle function as an identifiable factor for future injury. A history of low back pain (HxLBP) may also place athletes at increased risk for future low back pain. Reduced muscle thickness of the lumbar multifidus (LM) and transversus abdominis (TrA) has been reported among populations with clinical low back pain via ultrasound imaging in multiple positions. However, the roles of the LM and TrA in a more functional cohort and for injury prediction are still unknown.Objectives: : To (1) assess the reliability of LM and TrA ultrasound measures, (2) compare changes in muscle thickness across positions between persons reporting or not reporting HxLBP, and (3) determine the ability to distinguish between groups.Design: : Cross-sectional study.Setting: : Research laboratory.Patients or Other Participants: : Participants were 34 people who did not report HxLBP (age = 22 ± 7 years, body mass index = 23.7 ± 2.7) and 25 people who reported HxLBP (age = 25 ± 10 years, body mass index = 24.0 ± 3.2).Main Outcome Measure(s): : Muscle thickness and changes in muscle thickness of the LM and TrA as shown on ultrasound imaging.Results: : Intraclass correlation coefficients ranged from 0.641 to 0.943 for all thickness measures and from 0 to 0.693 for all averaged thickness modulations bilaterally. Participants who reported HxLBP had voluntarily reduced TrA thickness modulations compared with those not reporting HxLBP (P = .03), and the testing position influenced TrA thickness modulations (P < .01). No differences were observed for LM thickness modulations between groups or positions (P > .05). A tabletop cutoff value of 1.32 had a sensitivity of 0.640 and a specificity of 0.706, whereas a seated cutoff value of 1.18 had a sensitivity of 0.600 and a specificity of 0.647.Conclusions: : In participants reporting HxLBP, TrA thickness modulations were lower and both tabletop and seated thickness modulations were able to distinguish reported HxLBP status. These findings suggest that TrA muscle function may be altered by HxLBP.

While protein refolding has been studied for over 50 years since the pioneering work of Christian Anfinsen, there have been a limited number of studies correlating results between chemical, thermal, and mechanical unfolding. The limited knowledge of the relationship between these processes makes it challenging to compare results between studies if different refolding methods were applied. Our current work compares the energetic barriers and folding rates derived from chemical, thermal, and mechanical experiments using an immunoglobulin-like domain from the muscle protein titin as a model system. This domain, I83, has high solubility and low stability relative to other Ig domains in titin, though its stability can be modulated by calcium. Our experiments demonstrated that the free energy of refolding was equivalent with all three techniques, but the refolding rates exhibited differences, with mechanical refolding having slightly faster rates. This suggests that results from equilibrium-based measurements can be compared directly but care should be given comparing refolding kinetics derived from refolding experiments that used different unfolding methods.