Schweitzer Allyson M, Koehle Michael S, Fliss Matthew D, Mitchell Cameron J
School of Kinesiology, University of British Columbia, Vancouver, British Columbia, Canada.
Am J Physiol Cell Physiol. 2025 Jul 1;329(1):C68-C81. doi: 10.1152/ajpcell.00992.2024. Epub 2025 Jun 2.
Alterations to the extracellular matrix of skeletal muscle are implicated in age-related declines in muscle quality. Reduced collagen breakdown and collagen accumulation between muscle fibers are suggested to reduce the force-generating capacity of the muscle and impede adaptation to mechanical loading. The current study investigated total intramuscular collagen content in healthy, physical fitness-matched young and older skeletal muscle and how regulators of collagen breakdown respond to an acute bout of resistance exercise. No differences in intramuscular collagen content between young (5.4% ± 2.1) and older muscle (5.1% ± 3.1, = 0.779) were found. Seventy-two hours after resistance exercise, matrix metalloproteinase (MMP) and tissue inhibitors of metalloproteinase (TIMP) gene expression (, = 0.003; , ≤ 0.001; , = 0.008; , ≤ 0.001), protein content (MMP14 proenzyme, = 0.016), and protein activity (MMP2, = 0.009; MMP9, = 0.014) were elevated in both young and older muscle. An age-by-time interaction was demonstrated 72 h postexercise, with older adults demonstrating more MMP14 enzyme content at this timepoint than young adults ( = 0.02). Main effects of age were demonstrated for ( = < 0.001), ( = 0.008), and ( ≤ 0.001) gene expression. No significant differences were observed between baseline and 6 h postexercise in either age group. Acute resistance exercise potently stimulates upregulation of markers of collagen breakdown in healthy young and older skeletal muscle. Further research is warranted to determine the precise roles of MMPs and TIMPs in skeletal muscle's response to mechanical loading. Gene expression, protein content, and protein activity of regulators of collagen breakdown (MMPs and TIMPs) were elevated 72 but not 6 h after an acute bout of resistance exercise in healthy young and older human skeletal muscle, with similar baseline intramuscular collagen content. Young and older adults were healthy and matched for physical fitness, indicating that intramuscular collagen accumulation may be driven by factors other than aging per se.
骨骼肌细胞外基质的改变与肌肉质量的年龄相关下降有关。肌肉纤维间胶原蛋白分解减少和胶原蛋白积累被认为会降低肌肉产生力量的能力,并阻碍对机械负荷的适应。本研究调查了健康的、体能匹配的年轻和老年骨骼肌的肌肉内总胶原蛋白含量,以及胶原蛋白分解调节因子对急性抗阻运动的反应。未发现年轻肌肉(5.4%±2.1)和老年肌肉(5.1%±3.1,P = 0.779)的肌肉内胶原蛋白含量存在差异。抗阻运动72小时后,年轻和老年肌肉中的基质金属蛋白酶(MMP)和金属蛋白酶组织抑制剂(TIMP)基因表达(P,P = 0.003;P,P≤0.001;P,P = 0.008;P,P≤0.001)、蛋白质含量(MMP14酶原,P = 0.016)和蛋白质活性(MMP2,P = 0.009;MMP9,P = 0.014)均升高。运动后72小时出现年龄与时间的交互作用,此时老年人的MMP14酶含量高于年轻人(P = 0.02)。年龄对P(P = <0.001)、P(P = 0.008)和P(P≤0.001)基因表达有主效应。两个年龄组在基线和运动后6小时均未观察到显著差异。急性抗阻运动有力地刺激了健康年轻和老年骨骼肌中胶原蛋白分解标志物的上调。有必要进一步研究以确定MMP和TIMP在骨骼肌对机械负荷反应中的精确作用。在健康的年轻和老年人体骨骼肌中,急性抗阻运动72小时后,而非6小时后,胶原蛋白分解调节因子(MMP和TIMP)的基因表达、蛋白质含量和蛋白质活性升高,肌肉内胶原蛋白基线含量相似。年轻和老年人健康且体能匹配,这表明肌肉内胶原蛋白积累可能由衰老本身以外的因素驱动。