Kawasaki T, Kasai M
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
Biochem Biophys Res Commun. 1994 Mar 30;199(3):1120-7. doi: 10.1006/bbrc.1994.1347.
Gating properties of the Ca2+ channel in sarcoplasmic reticulum (SR) were monitored by measuring the choline permeation of the heavy fraction of SR (HSR) vesicles by the light scattering method. Increase of choline permeation by micromolar Ca2+, which refers to Ca2+ response, was lost when HSR vesicles were incubated overnight with EDTA or EGTA. In parallel, calsequestrin was released from the vesicles. This loss of Ca2+ response could not be inhibited by millimolar Mg2+, but was partially inhibited by submolar KCl. Since it took 3-5 hours to lose the Ca2+ response, calsequestrin may be released from the inside of the vesicles. When HSR vesicles were incorporated into lipid bilayer, open probability of the Ca2+ channel increased when calsequestrin was added to the trans side in the presence of millimolar Ca2+. These results suggest that calsequestrin acts as a regulator of Ca2+ channel in SR membrane.
通过光散射法测量肌浆网(SR)重组分(HSR)囊泡的胆碱通透性,监测SR中Ca2+通道的门控特性。当HSR囊泡与EDTA或EGTA孵育过夜时,微摩尔浓度的Ca2+引起的胆碱通透性增加(即Ca2+反应)消失。同时,钙结合蛋白从囊泡中释放出来。这种Ca2+反应的丧失不能被毫摩尔浓度的Mg2+抑制,但被亚摩尔浓度的KCl部分抑制。由于需要3至5小时才会丧失Ca2+反应,钙结合蛋白可能从囊泡内部释放出来。当HSR囊泡整合到脂质双层中时,在毫摩尔浓度的Ca2+存在下,向反侧加入钙结合蛋白时,Ca2+通道的开放概率增加。这些结果表明,钙结合蛋白作为SR膜中Ca2+通道的调节剂发挥作用。