Effects of removal and reconstitution of myosin regulatory light chain andtroponin C on the Ca2+-sensitive ATPase activity of myofibrils from scallop striated muscle
F. Shiraishi et al., Effects of removal and reconstitution of myosin regulatory light chain andtroponin C on the Ca2+-sensitive ATPase activity of myofibrils from scallop striated muscle, J BIOCHEM, 126(6), 1999, pp. 1020-1024
In order to examine the involvement of troponin-linked Ca2+-regulation, in
addition to well-known myosin-linked Ca2+-regulation, in the contraction of
molluscan striated muscle, myofibrils from Ezo-giant scallop striated musc
le were desensitized to Ca2+ by removing both myosin regulatory light chain
and troponin C by treatment with a strong divalent cation chelator, CDTA,
The ATPase level in the desensitized myofibrils was about half the maximum
level in intact myofibrils regardless of the Ca2+-concentration at 25 and 1
5 degrees C. In the absence of Ca2+, the ATPase of the desensitized myofibr
ils was suppressed by myosin regulatory light chain but not affected by tro
ponin C at either temperature, The ATPase was activated at higher Ca2+-conc
entrations by both myosin regulatory light chain and troponin C, but the ac
tivating effects of these two proteins were affected differently by tempera
ture. The activation of ATPase by myosin regulatory light chain was much gr
eater than that by troponin C at 25 degrees C, whereas the activation by tr
oponin C was much greater than that by myosin regulatory light chain at 15
degrees C. The maximum activation was only obtained in the presence of both
myosin regulatory light chain and troponin C at these temperatures, These
findings strongly suggest that the contraction of scallop striated muscle i
s regulated through both myosin-linked and troponin-linked Ca2+-regulation,
and that the troponin-linked Ca2+-regulation is more significant at lower
temperature.