Inhibition of normal and transformed fibroblast aggregation by skeletal muscle F‐actin

Oplatka, Avraham; Borejdo, Julian; Gadasi, Hana; Mühlrád, András

doi:10.1016/0014-5793(76)80108-1

Cited by 2 publications

(1 citation statement)

References 14 publications

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“…The association of actinlike filaments with lipid structures has also been shown in several ways. For example, actin has been identified in erythrocyte membranes (28), and actinlike filaments have been shown to be associated with mammalian (2,4,28,16) and amoeba (22) plasma membranes as well as with intestinal brush border membranes (14). The nature of the secretory granule-actin binding appears to be lipophilic.…”

Section: Discussionmentioning

confidence: 99%

Muscle actin filaments bind pituitary secretory granules in vitro.

Ostlund¹,

Leung²,

Kipnis³

1977

The Journal of Cell Biology

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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 granuleactin 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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Section: Discussionmentioning

confidence: 99%