1999 Volume 126 Issue 4 Pages 643-649
To elucidate the function of pICln, its localization in subcellular organellae was investigated. A specific polyclonal anti-pICln antibody detected the soluble 38-kDa pICln exclusively in the cytosols of rat heart, lung, liver, spleen, skeletal muscle, testis, and brain, but not rat kidney. pICln-associated proteins in skeletal muscle were also analyzed. Native-gradient PAGE showed a single 340-kDa protein band reactive to anti-pICln antibody. This band also stained with anti-actin antibody. Two-dimensional PAGE and immunoprecipitation analysis indicated that all of the pICln was present in association with actin of a constant length: the molecular ratio of pICln to actin was roughly 1:7. In addition, all actin in the cytosol fractions was found in association with pICln. These results suggest the possibility that skeletal muscle pICln controls the length of cytosolic F-actin.
