Translocation of HSP27 and MKBP in ischemic heart.
HSP27 and MKBP translocate from the cytosolic to myofibril fraction in ischemic rat heart as demonstrated by immunoblotting. Immunohistochemistry analysis showed that ischemia enhances the Z line labeling of HSP27 and MKBP. Two dimensional gel electrophoresis showed that ischemia increases the hyperphosphorylated form of HSP27. These data suggest that HSP27 and MKBP may be involved in the Z line protection against postischemic reperfusion injury.
Yoshida
K
K
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Japan. kyoshida@m.u-tokyo.ac.jp
Aki
T
T
Harada
K
K
Shama
K M
KM
Kamoda
Y
Y
Suzuki
A
A
Ohno
S
S
D000199:Actins / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism*; D015151:Immunoblotting; D007150:Immunohistochemistry; D008297:Male; D017202:Myocardial Ischemia / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism; D009210:Myofibrils / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism*; D018384:Oxidative Stress; D051381:Rats; D017208:Rats, Wistar; D013997:Time Factors
D000199:Actins; D002352:Carrier Proteins; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; C486700:Hspb2 protein, rat; D009363:Neoplasm Proteins