Muscle actin filaments bind pituitary secretory granules in vitro.
Hog anterior pituitary secretory granules sediment at 3,000 g. When rat or rabbit skeletal muscle actin filaments are present with the granules, the sedimentation decreases markedly. Depolymerized actin or viscous solutions of Ficoll and collagen have no effect on granule sedimentation. With this assay, actin filaments bind secretory granules (consisting of the proteinaceous core plus limiting membrane), secretory granule membranes, mitochondria, artificial lecithin liposomes, and styrene-butadiene microspheres, but have little or no interaction with membrane-free secretory granule cores and albumin microspheres. A secretory granule-actin complex sedimentable between 3,000 g and 25,000 g can be isolated. Metal ions, nucleotides, salts, dithiothreitol, or pretreatment of the granules with trypsin do not destroy the binding, which appears to be a lipophilic interaction.
D000199:Actins / Q000378:metabolism* / Q000494:pharmacology; D002499:Centrifugation, Density Gradient; D003593:Cytoplasm / Q000378:metabolism*; D003594:Cytoplasmic Granules / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D007700:Kinetics; D008081:Liposomes / Q000378:metabolism; D008566:Membranes / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D010902:Pituitary Gland / Q000648:ultrastructure*; D010903:Pituitary Gland, Anterior / Q000648:ultrastructure*; D014357:Trypsin / Q000494:pharmacology
D000199:Actins; D008081:Liposomes; D014357:Trypsin; D004229:Dithiothreitol