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PMID: 558196 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Muscle actin filaments bind pituitary secretory granules in vitro.

The Journal of cell biology ·Vol. 73 ·No. 1 ·1977-04-00 ·Pages 78-87

Ostlund RE, Leung JT, Kipnis DM

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.

MeSH Terms
Actins/metabolism,pharmacology Centrifugation, Density Gradient Cytoplasm/metabolism Cytoplasmic Granules/metabolism Cytoskeleton/metabolism Dithiothreitol/pharmacology Kinetics Liposomes/metabolism Membranes/metabolism Mitochondria/metabolism Pituitary Gland/ultrastructure Pituitary Gland, Anterior/ultrastructure Trypsin/pharmacology
Chemicals
Actins Liposomes Trypsin Dithiothreitol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ostlund R E
Leung J T
Kipnis D M
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24 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.73.1.78
Published
1977-04-00
Pages
78-87
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2109906
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.73.1.78 PMC Full Text View journal details
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