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长期锻炼会增加HspBP1(一种70千道尔顿热休克蛋白的共伴侣蛋白)的浓度。

Long-term exercises increase the concentration of HspBP1, a co-chaperone of 70-KDa heat shock protein.

作者信息

Grebenyuk E S, Stupnikova T V, Sakharov D A, Shleptsova V A, Sashchenko L P, Tonevitsky E A

机构信息

Institute of Physical Culture and Sports, Moscow, Russia.

出版信息

Bull Exp Biol Med. 2010 Oct;149(5):640-4. doi: 10.1007/s10517-010-1013-1.

DOI:10.1007/s10517-010-1013-1
PMID:21165407
Abstract

Extracellular concentration of heat shock protein (Hsp) with a molecular weight of 70 kDa (Hsp70) rapidly increases in the serum in response to stress and returns to the basal level during recovery. Further regulation of its blood concentration is unclear. A possible regulator is HspBP1, a protein binding Hsp70. Binding to ATPase domain of Hsp70, HspBP1 inactivates it, thus acting as a factor of nucleotide exchange. Blood sera from athletes were examined at the beginning and end of the last mesocycle of the training period by two-staged immunoaffinity test system. The concentration of HspBP1 increased with decreasing Hsp70 concentration under conditions of long-term training. Presumably, the dynamics of Hsp70 and HspBP1 concentrations can serve as the test for evaluating the adaptation potential.

摘要

分子量为70千道尔顿的热休克蛋白(Hsp)70(Hsp70)的细胞外浓度在应激反应时会在血清中迅速升高,并在恢复过程中回到基础水平。其血液浓度的进一步调节尚不清楚。一种可能的调节因子是HspBP1,一种与Hsp70结合的蛋白质。HspBP1与Hsp70的ATP酶结构域结合,使其失活,从而作为核苷酸交换因子发挥作用。通过两步免疫亲和测试系统,在训练期最后一个中周期开始和结束时对运动员的血清进行了检测。在长期训练条件下,HspBP1的浓度随着Hsp70浓度的降低而升高。据推测,Hsp70和HspBP1浓度的动态变化可作为评估适应潜力的测试指标。

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