Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis

Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis
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DOI:
10.1113/jphysiol.2009.179325
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发表时间:
2010-01-15
影响因子:
5.5
通讯作者:
Kjaer, Michael
Kjaer, Michael
中科院分区:
医学1区
文献类型:
--
作者:
Doessing, Simon;Heinemeier, Katja M.;Kjaer, Michael

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在骨骼肌和肌腱中,细胞外基质赋予重要的拉伸性能,并且对于损伤后的组织再生至关重要。肌肉骨骼组织适应性受机械负荷的影响,机械负荷调节生长因子的可用性,包括生长激素(GH)和胰岛素样生长因子-I(IGF-I),这可能是至关重要的。为了检验生长激素促进肌肉肌腱组织中基质胶原合成的假设,我们研究了健康年轻个体给予33-50 μ g kg(-1)d(-1)重组人生长激素(rhGH)14天的效果。rhGH组血清GH、血清IGF-I及肌腱和肌肉中IGF-I mRNA表达均升高。肌腱I型胶原mRNA表达和肌腱胶原蛋白合成分别增加3.9倍和1.3倍(P < 0.01和P = 0.02),肌肉I型胶原mRNA表达和肌肉胶原蛋白合成分别增加2.3倍和5.8倍(P < 0.01和P = 0.06)。肌原纤维蛋白合成不受GH和IGF-I升高的影响。适度的运动并没有增强GH操作的效果。因此,增加生长激素的可用性刺激基质胶原蛋白的合成在骨骼肌和肌腱,但没有任何影响肌原纤维蛋白的合成。结果表明,生长激素是更重要的是在加强基质组织比肌肉细胞肥大成人肌肉肌腱组织。
In skeletal muscle and tendon the extracellular matrix confers important tensile properties and is crucially important for tissue regeneration after injury. Musculoskeletal tissue adaptation is influenced by mechanical loading, which modulates the availability of growth factors, including growth hormone (GH) and insulin-like growth factor-I (IGF-I), which may be of key importance. To test the hypothesis that GH promotes matrix collagen synthesis in musculotendinous tissue, we investigated the effects of 14 day administration of 33-50 mu g kg(-1) day(-1) recombinant human GH (rhGH) in healthy young individuals. rhGH administration caused an increase in serum GH, serum IGF-I, and IGF-I mRNA expression in tendon and muscle. Tendon collagen I mRNA expression and tendon collagen protein synthesis increased by 3.9-fold and 1.3-fold, respectively (P < 0.01 and P = 0.02), and muscle collagen I mRNA expression and muscle collagen protein synthesis increased by 2.3-fold and 5.8-fold, respectively (P < 0.01 and P = 0.06). Myofibrillar protein synthesis was unaffected by elevation of GH and IGF-I. Moderate exercise did not enhance the effects of GH manipulation. Thus, increased GH availability stimulates matrix collagen synthesis in skeletal muscle and tendon, but without any effect upon myofibrillar protein synthesis. The results suggest that GH is more important in strengthening the matrix tissue than for muscle cell hypertrophy in adult human musculotendinous tissue.