HSP70 AND OTHER POSSIBLE HEAT-SHOCK OR OXIDATIVE STRESS PROTEINS ARE INDUCED IN SKELETAL-MUSCLE, HEART, AND LIVER DURING EXERCISE
HSP70 AND OTHER POSSIBLE HEAT-SHOCK OR OXIDATIVE STRESS PROTEINS ARE INDUCED IN SKELETAL-MUSCLE, HEART, AND LIVER DURING EXERCISE
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DOI：
10.1016/0891-5849(91)90119-n
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发表时间：
1991-01-01
影响因子：
7.4
通讯作者：
DAVIES, KJA
中科院分区：
文献类型：
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作者：
SALO, DC;DONOVAN, CM;DAVIES, KJA
运动会导致热休克（肌肉温度高达 45 摄氏度，核心温度高达 44 摄氏度）和氧化应激（产生 O2- 和 H2O2），运动训练可促进线粒体生物发生（肌肉线粒体增加 2-3 倍）。 通过运动，骨骼肌、心脏和肝脏中至少 15 种可能的热休克或氧化应激蛋白（包括一种分子量为 70 kDa 的蛋白）的浓度增加。 比目鱼肌、跖肌和趾长伸肌 (EDL) 在体外对热休克和氧化应激表现出不同的蛋白质合成反应（[H-3]亮氨酸掺入），但两种应激共有 5 种蛋白质（特别是 70 kDa 蛋白质和 106 kDa 蛋白质）。 接下来使用 [P-32] 标记的 HSP70 cDNA 探针通过 Northern 转移分析 HSP70 mRNA 水平。 运动、热休克和氧化应激会增加骨骼肌和心肌中 HSP70 mRNA 的水平。 骨骼肌 HSP70 mRNA 水平在运动后 30-60 分钟达到峰值，并在运动后 6 小时缓慢下降至对照水平。 在心肌中观察到两种不同的 HSP70 mRNA 种类； 2.3 kb mRNA 在运动后 2-3 小时内恢复到控制水平，3.5 kb mRNA 种类在运动后约 6 小时内保持升高浓度。 HSP70 的诱导似乎是对运动的热休克和氧化应激的生理反应。 运动高温实际上可能会引起氧化应激，因为我们还发现肌肉线粒体随着温度的升高而逐渐解偶联并增加氧气的产生。 据报道，HSP70 可将多肽从细胞核转运至线粒体，并在线粒体中整合成完整的线粒体蛋白。 因此，HSP70 可能是运动诱导线粒体生物发生分子机制中的重要环节。
Exercise causes heat shock (muscle temperatures of up to 45-degrees-C, core temperatures of up to 44-degrees-C) and oxidative stress (generation of O2- and H2O2), and exercise training promotes mitochondrial biogenesis (2-3-fold increases in muscle mitochondria). The concentrations of at least 15 possible heat shock or oxidative stress proteins (including one with a molecular weight of 70 kDa) were increased, in skeletal muscle, heart, and liver, by exercise. Soleus, plantaris, and extensor digitorum longus (EDL) muscles exhibited differential protein synthetic responses ([H-3]leucine incorporation) to heat shock and oxidative stress in vitro but five proteins (particularly a 70 kDa protein and a 106 kDa protein) were common to both stresses. HSP70 mRNA levels were next analyzed by Northern transfer, using a [P-32]-labeled HSP70 cDNA probe. HSP70 mRNA levels were increased, in skeletal and cardiac muscle, by exercise and by both heat shock and oxidative stress. Skeletal muscle HSP70 mRNA levels peaked 30-60 min following exercise, and appeared to decline slowly towards control levels by 6 h postexercise. Two distinct HSP70 mRNA species were observed in cardiac muscle; a 2.3 kb mRNA which returned to control levels within 2-3 h postexercise, and a 3.5 kb mRNA species which remained at elevated concentrations for some 6 h postexercise. The induction of HSP70 appears to be a physiological response to the heat shock and oxidative stress of exercise. Exercise hyperthermia may actually cause oxidative stress since we also found that muscle mitochondria undergo progressive uncoupling and increased O2- generation with increasing temperatures. HSP70 has been reported to transport polypeptides from the nucleus to mitochondria where they are incorporated into complete mitochondrial proteins. HSP70 may, thus, be a vital link in the molecular mechanism of exercise-induced mitochondrial biogenesis.