The content of heat shock protein 47 (HSP47), a collagen-specific stress protein, changes with gravitational conditions in skeletal muscle.
It is well known that unloading of skeletal muscle with spaceflight or tail suspension leads rat soleus muscle atrophy. Previously, we reported that one of small heat shock protein (sHSP), alpha B-crystallin shows an early dramatic decrease in atrophied rat soleus muscle (Atomi et al, 1991). In this report, we focused to study the gravitational responses of another HSP, which may be reactive to the gravity. HSP47, a collagen-specific stress protein, has been postulated to be a collagen-specific molecular chaperone localized in the ER (Nagata et al, 1992). Western blot analysis revealed that HSP47 in slow skeletal muscle decreases at 5 days after tail suspension (TS) and increased at 5 days recovery after 10 days of TS as compared with the control level. Hypothetically, HSP47 in slow soleus muscle increases at 5 days after hypergravity (HG) induced by the centrifugation. The content of HSP47 in soleus muscle was strongly affected by gravity conditions.
Oguro
Asami
A
Department of Life Sciences, The Graduate School of Arts & Sciences, The University of Tokyo.
Sakurai
Takashi
T
Otawa
Mayumi
M
Okuno
Makoto
M
Atomi
Yoriko
Y
D000818:Animals; D050958:HSP47 Heat-Shock Proteins / Q000378:metabolism*; D019417:Hindlimb Suspension; D018471:Hypergravity; D008297:Male; D018657:Muscle Fibers, Slow-Twitch / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar; D018474:Weightlessness Simulation
D050958:HSP47 Heat-Shock Proteins