[Progress in research on heat shock proteins in cardiovascular system].
Diverse physiological stresses (e.g., heat shock, ischemia and hemodynamics) produce multiple changes in a cell that affect metabolic processes and cellular structures. In response, stress proteins are synthesized, and are thought to mediate cytoprotection through biological function as molecular chaperones. Accumulated evidence indicates that HSP70, HSP90, HSP47, HSP32 and HSP27 play an important role during cardiac ischemia, ischemia preconditioning, cardiac hypertrophy and vascular wall injury.
Zhou
Jing-Jun
JJ
Department of Physiology, Fourth Military Medical University, Xi'an 710032.
Zhu
Yun-Long
YL
Pei
Jian-Ming
JM
Gao
Zhan
Z
Zhu
Miao-Zhang
MZ
D000818:Animals; D002318:Cardiovascular Diseases / Q000378:metabolism* / Q000503:physiopathology; D002319:Cardiovascular System / Q000378:metabolism* / Q000503:physiopathology; D050958:HSP47 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D018841:HSP90 Heat-Shock Proteins / Q000502:physiology; D006360:Heat-Shock Proteins / Q000502:physiology*; D051381:Rats; D013552:Swine
D050958:HSP47 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C494662:Serpinh1 protein, rat