Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise
Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise
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DOI：
10.1113/jphysiol.2005.093690
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发表时间：
2005-09-15
影响因子：
5.5
通讯作者：
Rennie, MJ
中科院分区：
文献类型：
--
作者：
Miller, BF;Olesen, JL;Rennie, MJ
我们假设，剧烈的、非损伤性的运动会增加肌腱和骨骼肌中胶原蛋白的蛋白质合成率，但会低于肌肉肌原纤维和肌浆蛋白的合成率。两组（n = 8 和 6）健康年轻男性在进行 1 小时最大工作量 (W-max) 67% 的单腿踢腿运动后 72 小时内进行了研究。为了标记肌肉和肌腱中的组织蛋白，静脉内持续输注[1-C-13]亮氨酸或[1-C-13]缬氨酸和大量剂量的[N-15]或[C-13]脯氨酸，并通过气相色谱-质谱法评估目标蛋白中的标记。在运动后 6、24、42 或 48 和 72 小时对运动和休息的腿进行髌腱和股四头肌活检。所有蛋白质的合成分数在运动后6小时升高，并在运动后24小时迅速升至峰值（肌腱胶原蛋白（0.077% h(-1)）、肌肉胶原蛋白（0.054% h(-1)）、肌原纤维蛋白（0.121% h(-1)）和肌浆蛋白（0.134% h(-1)））。尽管肌腱胶原蛋白和肌原纤维蛋白合成率仍然升高，但 72 小时后，该比率下降至基础值。组织学评估中没有可见的肌肉组织损伤。组织微透析液和 IGF-I 和 IGF 结合蛋白（IGFBP-3 和 IGFBP-4）或 I 型前胶原 N 末端前肽的血清浓度均未从静息值发生变化。因此，人体肌腱和肌肉剧烈运动后胶原蛋白合成迅速增加。不同细胞类型中蛋白质合成速率变化的相似时间过程支持协调肌腱适应的想法。
We hypothesized that an acute bout of strenuous, non-damaging exercise would increase rates of protein synthesis of collagen in tendon and skeletal muscle but these would be less than those of muscle myofibrillar and sarcoplasmic proteins. Two groups (n = 8 and 6) of healthy young men were studied over 72 h after I h of one-legged kicking exercise at 67% of maximum workload (W-max). To label tissue proteins in muscle and tendon primed, constant infusions of [1-C-13]Ieucine or [1-C-13]valine and flooding doses of [N-15] or [C-13]proline were given intravenously, with estimation of labelling in target proteins by gas chromatography-mass spectrometry. Patellar tendon and quadriceps biopsies were taken in exercised and rested legs at 6, 24, 42 or 48 and 72 h after exercise. The fractional synthetic rates of all proteins were elevated at 6 h and rose rapidly to peak at 24 h post exercise (tendon collagen (0.077% h(-1)), muscle collagen (0.054% h(-1)), myofibrillar protein (0.121% h(-1)), and sarcoplasmic protein (0.134% h(-1))). The rates decreased toward basal values by 72 h although rates of tendon collagen and myofibrillar protein synthesis remained elevated. There was no tissue damage of muscle visible on histological evaluation. Neither tissue microdialysate nor serum concentrations of IGF-I and IGF binding proteins (IGFBP-3 and IGFBP-4) or procollagen type I N-terminal propeptide changed from resting values. Thus, there is a rapid increase in collagen synthesis after strenuous exercise in human tendon and muscle. The similar time course of changes of protein synthetic rates in different cell types supports the idea of coordinated musculotendinous adaptation.