PMID: 558196Apr 1, 1977Paper

Muscle actin filaments bind pituitary secretory granules in vitro

The Journal of Cell Biology
R E OstlundD M Kipnis

Abstract

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.

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Citations

Jan 1, 1978·Journal of Supramolecular Structure·C M CohenD Branton
Jul 9, 1990·Molecular and Cellular Endocrinology·R Ravindra, C E Grosvenor
Oct 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·S S BrownM S Wicha
Mar 1, 1985·The Journal of Cell Biology·C A Stratford, S S Brown
Mar 1, 1980·The Journal of Cell Biology·S W Craig, C L Lancashire
Feb 1, 1983·Australian and New Zealand Journal of Medicine·B G RobinsonB J Morris
Jan 1, 1979·Archives of Biochemistry and Biophysics·S LohmanderA Hinek
Dec 28, 2018·Endocrine-related Cancer·G MantovaniE Peverelli
Oct 1, 1982·Molecular and Cellular Biology·C Greer, R Schekman

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