Decrease in heart peptide initiation during head-down tilt may be modulated by HSP-70.
Decrease in heart peptide initiation during head-down tilt may be modulated by HSP-70.
复制标题
低头倾斜期间心脏肽起始的减少可能受到 HSP-70 的调节。
DOI:
10.1152/ajpcell.1995.268.6.c1375
复制
发表时间:
1995
期刊:
影响因子:
--
通讯作者:
Thomason,DB
中科院分区:
文献类型:
--
作者:
Menon,V;Yang,J;Ku,Z;Thomason,DB
This study examines the mechanism of the rapid decrease in cardiac muscle protein synthesis during rodent hindlimb non-weight bearing. Polysomes isolated from rat hearts 8 h after suspension show less RNA in the polysome pool and a shift in polysome size toward fewer ribosomes per mRNA; 18 h after suspension, the size shift persists, but the amount of RNA in the polysome pool returns to control values. These data are consistent with a decrease in the rate of initiation of protein synthesis. At both 8 and 12 h of suspension, the cardiac polysomes show a 78 and 93% increase association with the nascent polypeptide chaperone protein 70-kDa heat-shock cognate/heat-shock protein (HSC/HSP-70), respectively, that persists after 7 days of non-weight bearing. Because the dissociation of HSC/HSP-70 from unfolded protein can be modulated by ATP, we measured the adenosine nucleotide pools and found a 53% decrease in ATP levels after 18 h of suspension. We propose a mechanism in which a shift of HSC/HSP-70 to the nascent polypeptide indirectly inhibits protein synthesis initiation.