Laquerre S, Poulin R, Labrie F, Chafouleas J G
Research Centre, Laval University Medical Centre, Que., Canada.
Biochem Cell Biol. 1990 May;68(5):863-9. doi: 10.1139/o90-128.
Calmodulin-binding proteins (CaMBPs) were analyzed during estrogen-stimulated growth in the human breast cancer cell line ZR-75-1. A variety of Ca2(+)-dependent and -independent CaMBPs were observed to be present in these cells. Calmodulin (CaM) binding to a 51-kilodalton protein was shown to be Ca2(+)-dependent. Moreover, binding to this protein was reduced in the estrogen-treated cells. This effect occurred early during estrogen-stimulated cell growth and was maintained during exponential growth in the presence of estrogen. 125I-labeled CaM overlay procedure of two-dimensional polyacrylamide gels reveals that this 51-kilodalton protein is composed of at least two distinct isoforms with different isoelectric points. Subcellular localization demonstrates that this protein resides exclusively in the microsomal fraction.