Fujii J, Maruyama K, Tada M, MacLennan D H
Banting and Best Department of Medical Research, Charles H. Best Institute, University of Toronto, Ontario, Canada.
FEBS Lett. 1990 Oct 29;273(1-2):232-4. doi: 10.1016/0014-5793(90)81092-3.
Full length cDNAs encoding both slow-twitch/cardiac (SERCA2) and fast-twitch skeletal muscle (SERCA1) Ca2(+)-ATPases were expressed by transient transfection of COS-1 cells. Studies of the Ca2(+)-dependency of Ca2(+)-transport in microsomes isolated from these cells showed that both isoforms had an affinity for Ca2+ of about 0.2 microM. The Ca2(+)-affinity of SERCA2 was lowered when phospholamban was co-expressed with it, demonstrating that the two proteins interact in this expression system. These studies support the view that phospholamban inhibition accounts for the low Ca2(+)-affinity and low activity of SERCA2 in cardiac muscle sarcoplasmic reticulum.