In-vitro effect of phalloidin on a plasma membrane preparation from rat liver

Govindan, V. M.; Faulstich, Heinz; Wieland, Th.; Agostini, Bruno; Hasselbach, Wilhelm

doi:10.1007/bf00609837

Cited by 69 publications

(12 citation statements)

References 13 publications

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“…The above results confirm the conclusion that filaments observed after phalloidin treatment in the isolated plasma membrane fraction in vivo or in vitro [2] consist of actin which must be situated close to the membrane or could even be an integral protein of the plasma membrane of hepatocytes. Its total identity with muscle actin of the same species remains to be elucidated by amino acid analysis and fingerprint mapping.…”

Section: Resultssupporting

confidence: 87%

“…Phalloidin, a toxic bicyclic heptapeptide from poisonous Amanita mushrooms [1 ] leads to a markedly enhanced appearance of microfilaments in membrane preparations from livers of rats poisoned in vivo as well as in vitro [2]. Morphologically and by their reaction with heavy meromyosin under formation of arrowhead-like structures, the filaments are indistinguishable from actin filaments of rabbit muscle [3,4].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Isolation and identification of an actin from rat liver

Govindan¹,

Wieland²

1975

FEBS Letters

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Section: Resultssupporting

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Isolation and identification of an actin from rat liver

Govindan¹,

Wieland²

1975

FEBS Letters

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“…The use of phalloidin was previously limited, because most tissue culture cell lines are resistant to the drug applied in the medium (see Results). The possibility of a permeation barrier for a majority of cell types was expected, because phalloidin poisoning of animals showed that the liver was the specific target of the drug and pathological changes in other tissues were not observed (17,18). Does phalloidin act specifically on cytoplasmic actin when microinjected into cells?…”

Section: Discussionmentioning

confidence: 99%

Phalloidin-induced actin polymerization in the cytoplasm of cultured cells interferes with cell locomotion and growth

Wehland

Osborn

Weber

1977

Proc. Natl. Acad. Sci. U.S.A.

185

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Phalloidin, the toxic drug from the mushroom Amanita phalloides, was injected into the cytoplasm of tissue culture cells and the changes in intracellular actin distribution were followed by immunofluorescence microscopy with actin antibody. At low concentrations, phalloidin recruits the nonor less highly polymerized forms of cytoplasmic actin into stable "islands" of aggregated actin polymers and does not interfere with the preexisting thick bundles of microfilaments (stress fibers). Differential focusing shows that these islands of phalloidin-induced actin polymers occur at a level in the cytoplasm that is above the submembranous bundles of microfilaments present on the adhesive side of the cells. The pattern of cytoplasmic microtubules remains unaffected by the injection of phalloidin; however, filamin, a protein usually associated with actin in the cytoplasm, is also recruited into the islands. At higher phalloidin concentrations, contraction of the cell is observed. These results are discussed in the light of previous biochemical studies by Wieland and Faulstich and their coworkers [for a review see Wieland, T. (1977) Naturwissenschaften 64, 303-3091 on the in vitro interaction of phalloidin with muscle actin, which have documented that phalloidin reacts stoichiometrically with actin, promotes actin polymerization, and stabilizes actin polymers.In addition, we show that microinjection of phalloidin interferes in a concentration-dependent manner with cell locomotion and cell growth. These results indicate that a well-balanced controlled reversible equilibrium between different polymerization states of actin may be a necessary requirement for cell locomotion and may also influence other cellular functions such as growth.Actin is the major structural protein of the cytoplasm of eukaryotic cells. The structural organization and polymerization of cytoplasmic actin is still poorly understood (for a review see ref. 1). Although in muscle cells actin is exclusively organized in nearly crystalline ordered arrays of thin filaments, the actin organization in nonmuscle cells can be rather diverse. Actin is the major protein of the thick bundles of microfilaments (stress fibers) typical for a variety of fibroblastic, epithelial, and other cells (2-4), but less ordered actin polymerization occurs in the ruffling edge of these cells, and many other cell types show only thin microfilamentous structures (2, 3, 5, 6). In addition, the mechanisms that govern the polymerization and depolymerization of these various types of cellular actin structures are still unclear and it is currently difficult to assess how much of the cellular actin is present in an unpolymerized form (G actin) and how much is present in different types of polymers (F actin), including the individual microfilaments and the stress fibers.Recently phalloidin, a cyclic peptide of the mushroom Amanita phalloides, was introduced as an actin-specific drug in vitro. Wieland, Faulstich, and their coworkers have carefully documented in several studies tha...

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“…However, in phalloidin-treated hepatocytes an accumulation of microfilamentous networks was detectable at the base of each protrusion (23,26). Liver treated in vivo showed a striking increase of actin filaments in hepatocytes, mainly around bile canaliculi with a parallel accumulation of cytoplasmic actin (27,28).…”

Section: Discussionmentioning

confidence: 99%