Intracellular distribution of a 32-KDa calcium-dependent phospholipid-binding protein from human placenta.
A 32-KDa calcium dependent phospholipid-binding protein was purified to homogeneity from human placenta by affinity adsorption to polyacrylamide-immobilized phosphatidylserine followed by elution with 5 mM EGTA and ion exchange chromatography. Immunochemical studies using the polyclonal antibody against the 32-KDa protein revealed that this protein was present around the nucleus in the cytoplasm but not clearly associated with cell organelles and cytoskeletons. In KB cells treated with insulin, 32-KDa protein was localized in the ruffling membranes in addition to the cytoplasm. Purified 32-KDa protein was shown to coprecipitate with skeletal muscle actin under polymerizing conditions. These findings suggest that the 32-KDa protein interacts with networks of actin filaments in cells.
Giga-Hama
Y
Y
Research Center, Asahi Glass Company, Ltd., Yokohama, Japan.
Yohda
M
M
Kumagai
H
H
D000199:Actins / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D015153:Blotting, Western; D002118:Calcium / Q000494:pharmacology*; D002352:Carrier Proteins / Q000032:analysis* / Q000302:isolation & purification; D002467:Cell Nucleus / Q000032:analysis*; D002852:Chromatography, Ion Exchange; D003593:Cytoplasm / Q000032:analysis*; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D007328:Insulin / Q000494:pharmacology; D008297:Male; D008970:Molecular Weight; D010743:Phospholipids / Q000378:metabolism*; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000032:analysis* / Q000302:isolation & purification; D011817:Rabbits
D000199:Actins; D000596:Amino Acids; D002352:Carrier Proteins; D007328:Insulin; D010743:Phospholipids; D011257:Pregnancy Proteins; D002118:Calcium