E. Fehrenbach et al., Transcriptional and translational regulation of heat shock proteins in leukocytes of endurance runners, J APP PHYSL, 89(2), 2000, pp. 704-710
Heat shock proteins (HSP) represent cell-protective and antioxidant systems
that may be induced by reactive oxygen species, cytokines, and hyperthermi
a. In the present study, we evaluated the influence of heavy endurance exer
cise and training on HSP27 and HSP70 in peripheral leukocytes of 12 athlete
s (before and at 0, 3, and 24 h after a half-marathon) and 12 untrained con
trols on protein and mRNA levels by flow cytometry and RT/PCR, respectively
. HSP transcripts increased significantly immediately after acute exertion
accompanied by elevated levels of corresponding proteins. HSP protein expre
ssion remained high until 24 h postexercise. Significant increases of plasm
a interleukin-8, myeloperoxidase, and creatine kinase occurred after exerci
se. Basal HSP expression was usually lower in trained compared with untrain
ed subjects. Applying in vitro heat shock to resting blood samples of all s
ubjects significantly stimulated HSP mRNA, showing higher increases in trai
ned individuals. The exercise-induced alterations indicate that immunocompe
tent cells became activated. In addition to heat stress, other exercise-ass
ociated stress agents (oxidants, cytokines) may have also participated in s
timulation of RSP expression in leukocytes. The expression pattern of HSP d
ue to training status may be attributed to adaptive mechanisms.