The Activation of Stress-induced Heat Shock Protein 27 and the Relationship of Physical Therapy

스트레스-유도 열충격단백질 27(Heat Shock Protein 27)의 활성과 물리치료의 상관성

  • Kim, Mi-Sun (Department of Physical Therapy, the Graduate School, Doctoral Course, Yong In University) ;
  • Lee, Sung-Ho (Department of Physical Therapy, the Graduate School of Rehabilitation and Health Science, Master Course, Yong In University) ;
  • Kim, Il-Hyun (Department of Physical Therapy, the Graduate School of Rehabilitation and Health Science, Master Course, Yong In University) ;
  • Hwang, Byong-Yong (Department of Physical Therapy, Yongin University) ;
  • Kim, Jung-Hwan (Department of Physical Therapy, Yongin University)
  • 김미선 (용인대학교 대학원) ;
  • 이성호 (용인대학교 재활보건과학대학원) ;
  • 김일현 (용인대학교 재활보건과학대학원) ;
  • 황병용 (용인대학교 물리치료학과) ;
  • 김중환 (용인대학교 물리치료학과)
  • Published : 2008.03.25

Abstract

Purpose: Heat shock proteins (HSPs) are a group of proteins that are activated when cells are exposed to a variety of environmental stresses, such as infection, inflammation, exposure to toxins, starvation, hypoxia, brain injury, or water deprivation. The activation of HSPs by environmental stress plays a key role in signal transduction, including cytoprotection, molecular chaperone, anti-apoptotic effect, and anti-aging effects. However, the precise mechanism for the action of small HSPs, such as HSP27 and mitogen-activated protein kinases (MAPKs: extracellular-regulated protein kinase 1/2 (ERK1/2), p38MAPK, stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), is not completely understood, particularly in application of cell stimulators including platelet-derived growth factor (PDGF), angiotensin II (AngII), tumor necrosis factor $\alpha$ (TNF$\alpha$), and $H_2O_2$. This study examined the relationship between stimulators-induced enzymatic activity of HSP27 and MAPKs from rat smooth and skeletal muscles. Methods: 2-dimensional electrophoresis (2DE) and matrix assisted laser desorption ionizationtime-of-flight/time-of-flight (MALDI-TOF/TOF) analysis were used to identify HSP27 from the intact vascular smooth and skeletal muscles. Three isoforms of HSP27 were detected on silver-stained gels of the whole protein extracts from the rat aortic smooth and skeletal muscle strips. Results: The expression of PDGF, AngII, TNF$\alpha$, and $H_2O_2$-induced activation of HSP27, p38MAPK, ERK1/2, and SAPK/JNK was higher in the smooth muscle cells than the control. SB203580 (30${\mu}$M), a p38MAPK inhibitor, increased the level of HSP27 phosphorylation induced by stimulators in smooth muscle cells. Furthermore, the age-related and starvation-induced activation of HSP27 was higher in skeletal muscle cells (L6 myoblast cell lines) and muscle strips than the control. Conclusion: These results suggest, in part, that the activity of HSP27 and MAPKs affect stressors, such as PDGF, AngII, TNF$\alpha$, $H_2O_2$, and starvation in rat smooth and skeletal muscles. However, more systemic research will be needed into physical therapy, including thermotherapy, electrotherapy, radiotherapy and others.

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