Carp parvalbumin binds to and directly interacts with the sarcoplasmic reticulum for Ca2+ translocation.
Interaction between two relaxing factors, the sarcoplasmic reticulum and parvalbumin, in carp fast skeletal muscle was investigated. Immunoblotting using an anti-parvalbumin antibody revealed that parvalbumin bound to the light sarcoplasmic reticulum isolated from carp fast skeletal muscle in the presence of Ca2+. Parvalbumin enhanced Ca2+ uptake activity of the light sarcoplasmic reticulum. Furthermore, using a photoreactive cross-linker, we detected a protein in the light sarcoplasmic reticulum which bound to parvalbumin in a Ca(2+)-dependent manner. These results suggest that parvalbumin may directly interact with the sarcoplasmic reticulum in contraction-relaxation cycle of carp fast skeletal muscle.
Ushio
H
H
Laboratory of Marine Biochemistry, Faculty of Agriculture, University of Tokyo, Japan.
Watabe
S
S
D000818:Animals; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism*; D002347:Carps; D003432:Cross-Linking Reagents; D009119:Muscle Contraction; D010320:Parvalbumins / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D003432:Cross-Linking Reagents; D010320:Parvalbumins; D002118:Calcium