Chang J, Knowlton A A, Wasser J S
Department of Veterinary Physiology and Pharmacology, College of Veterinary Medicine, Texas A&M University, College Station, 77843, Texas, USA.
Am J Physiol Regul Integr Comp Physiol. 2000 Jan;278(1):R209-14. doi: 10.1152/ajpregu.2000.278.1.R209.
Heat shock proteins (HSPs) may play a cardioprotective role during hypoxia or ischemia. We hypothesized that cardiac tissue from hypoxia-tolerant animals might have high levels of specific HSPs. We measured myocardial HSP60 and HSP72/73 in painted and softshell turtles during normoxia and anoxia (12 h) and after recovery (12 or 24 h). We also measured myocardial HSPs in normoxic rats and rabbits. During normoxia, hearts from the most highly anoxia-tolerant species, the painted turtle, expressed the highest levels of HSP60 (22.6+/-2.0 mg/g total protein) followed by softshells (11.5+/-0.8 mg/g), rabbits (6.8+/-0.9 mg/g), and rats (4.5+/-0.5 mg/g). HSP72/73 levels, however, were not significantly different. HSP60 levels in hearts from both painted and softshell turtles did not deviate significantly from control values after either 12 h of anoxia or 12 or 24 h of recovery. The pattern of changes observed in HSP72/73 was quite different in the two turtle species. In painted turtles anoxia induced a significant increase in myocardial HSP72/73 (from 2.8+/-0.1 mg/g normoxic to 3.9+/-0.2 mg/g anoxic, P<0.05). By 12 h of recovery, HSP72/73 had returned to control levels (2.7+/-0.1 mg/g) and remained there through 24 h (2.6+/-0.2 mg/g). In softshell turtles, HSP72/73 decreased significantly after 12 h of anoxia (from 2.4+/-0.4 mg/g normoxic to 1.3+/-0.2 mg/g anoxic, P<0.05). HSP72/73 levels were still slightly below control after 12 h of recovery (2.1+/-0.1 mg/g) and then rose to significantly above control after 24 h of recovery (4.1+/-0.7 mg/g, P<0.05). We also conclude that anoxia-tolerant and anoxia-sensitive turtles exhibit different patterns of myocardial HSP changes during anoxia and recovery. Whether these changes correlate with their relative degrees of anoxia tolerance remains to be determined.
热休克蛋白(HSPs)在缺氧或缺血期间可能发挥心脏保护作用。我们推测,耐缺氧动物的心脏组织可能具有高水平的特定热休克蛋白。我们测量了锦龟和软壳龟在常氧和缺氧(12小时)以及恢复(12或24小时)期间心肌中的HSP60和HSP72/73。我们还测量了常氧大鼠和兔子心肌中的热休克蛋白。在常氧期间,耐缺氧能力最强的物种锦龟的心脏中,HSP60表达水平最高(22.6±2.0毫克/克总蛋白),其次是软壳龟(11.5±0.8毫克/克)、兔子(6.8±0.9毫克/克)和大鼠(4.5±0.5毫克/克)。然而,HSP72/73水平没有显著差异。在缺氧12小时或恢复12或24小时后,锦龟和软壳龟心脏中的HSP60水平与对照值相比没有显著偏差。在两种龟类中观察到的HSP72/73变化模式有很大不同。在锦龟中,缺氧导致心肌HSP72/73显著增加(从常氧时的2.8±0.1毫克/克增加到缺氧时的3.9±0.2毫克/克,P<0.05)。到恢复12小时时,HSP72/73已恢复到对照水平(2.7±0.1毫克/克),并在24小时内保持在该水平(2.6±0.2毫克/克)。在软壳龟中,缺氧12小时后HSP72/73显著降低(从常氧时的2.4±0.4毫克/克降至缺氧时的1.3±0.2毫克/克,P<0.05)。恢复12小时后,HSP72/73水平仍略低于对照(2.1±0.1毫克/克),然后在恢复24小时后显著高于对照(4.1±0.7毫克/克,P<0.05)。我们还得出结论,耐缺氧和对缺氧敏感的龟在缺氧和恢复期间表现出不同的心肌热休克蛋白变化模式。这些变化是否与其相对的耐缺氧程度相关仍有待确定。