Heavy meromyosin binding to microfilaments involved in cell and morphogenetic movements

Spooner, Brian S.; Ash, John F.; Wrenn, Joan T.; Frater, R.; Wesells, Norman K.

doi:10.1016/s0040-8166(73)80004-7

Cited by 88 publications

(19 citation statements)

References 23 publications

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“…Alternatively, if all the actin is present as double-helical filaments, then each cell would contain a total length of about 40cm. A more realistic picture is that about half of the actin is present in an unpolymerized form at about 2mg/ml (D. Bray & C. Thomas, unpublished work), and the remaining filamentous actin is distributed largely in bundles beneath the cell cortex and within filopodia (Goldman & Knipe, 1973;Perdue, 1973;Spooner et al, 1973).…”

Section: Discussionmentioning

confidence: 99%

“…Ishikawa et al (1969) showed that cells treated with heavy meromyosin contained thin filaments with regular arrowhead projections along their lengths resembling those formed between filaments of muscle actin and heavy meromyosin (Huxley, 1963). This observation has now been made in many different types of fibroblastic cell (Goldman & Knipe, 1973;Perdue, 1973;Spooner et al, 1973). Biochemical evidence was obtained by Yang & Perdue (1972), who obtained from chick embyro fibroblasts a protein which has the same electrophoretic mobility, morphology and ability to interact with myosin as muscle actin.…”

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confidence: 87%

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The actin content of fibroblasts

Bray¹,

Thomas²

1975

Biochemical Journal

107

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Cultures of chick skin fibroblasts were dissolved in solutions of sodium dodecyl sulphate, and their entire protein content was examined by gel electrophoresis. The most abundant species migrated in the same position as muscle actin. It gave a similar pattern of iodinated peptides after reaction with radioactive sodium iodide and digestion with proteinases, and contained comparable amounts of N-methylhistidine. Its amount was estimated by quantitative densitometry of stained gels with bovine serum albumin as an internal standard, and by radioactive assay ofcultures that had been grown in the presence of [35S]methionine. The values obtained ranged from 7 to 14% of the total cellular protein, with an average of 8.5 %. A protein band in the position of muscle myosin was also present and accounted for about 2.5 % of the total protein. Both this and the actin band increased in relative amount with the age of the cultures.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 87%

The actin content of fibroblasts

Bray¹,

Thomas²

1975

Biochemical Journal

107

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“…Under optimal conditions, these bundles can be visualized as "stress fibers" in extensively flattened living cells (1,8,12,16). Other microfilament configurations have also been described and are termed microfilament meshworks ( 3 , 8 ) and microfilament networks (14-15, [17][18][19]. Electron microscopic studies of suspended cells and cells in the process of attachment to and spreading on solid substrates have led to the suggestion that microfilament meshworks and microfilament bundles may be interconvertible and that the formation and loss of cell-cell and cell-substrate contacts signals these interconversions (3,8,12).…”

Section: Introductionmentioning

confidence: 99%

Localization and organization of microfilaments and related proteins in normal and virus‐transformed cells

1976

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The localization and organization of actin-like microfilaments in normal, SV-40 and adenovirus transformed cells are determined by the coordinated use of light optical, electron optical and biochemical techniques. In adenovirus-type 5 transformed hamster embryo cells, microfilament meshworks appear to be the predominant organizational form of cellular action, while in normal hamster cells, microfilament bundles are prevalent. Differences between 3T3 and SV-40 transformed 3T3 cells are less apparent and may be related to the packing and intracellular distribution of microfilament bundles. Attempts at relating these ultrastructural changes in transformed cells to the images obtained following reaction with fluorescein-labelled myosin fragments and indirect immunofluorescence with smooth muscle myosin antibody are discussed. In several instances the fluorescence microscope images to not correspond to the ultrastructural observations. The results are discussed in terms of the possible relationships between alterations in cytoplasmic contractile elements and the abnormal behavior of transformed cells.

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“…These movements seem to be related to a membraneassociated microfilament system (14,27,28,36,38) that has frequently been shown to contain actin (2,22,24,29,30). Many morphological studies showing disruption of thin filament arrays (3,6,7,18,31,32,39,40) and a few studies with purified actin (16,21,33,34) or myosin (footnote 2 and reference 26) suggest that cytochalasins can interact directly with proteins of the microfilament system.…”

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confidence: 99%

Cytochalasin B inhibits actin-related gelation of HeLa cell extracts.

Weihing¹

1976

The Journal of Cell Biology

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When the 100,000 g supernatant fraction (extract) of HeLa cells lysed in a buffer containing sucrose, ATP, DTE, EGTA, imidazole, and Triton X-100 is incubated at 25 degrees C, it gels, and actin and a HMWP are progressively enriched in the extract and in gel isolated from extract. CB (greater than or equal to 0.25 muM) inhibits gelation and specifically lowers the concentrations of actin and the HMWP in the fraction which sediments at 100,000 g after incubation. These results indicate that actin and HMWP are partly disaggregated by cytochalasin treatment, and thus that their aggregation is related gelation. Inasmuch as previous results showed that actin is present and HMWP is enriched in the plasma membrane fraction of HeLa cells, the results also point to a possible relation between plasma membrane-associated gel and in vivo effects of CB.

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Heavy meromyosin binding to microfilaments involved in cell and morphogenetic movements

Cited by 88 publications

References 23 publications

The actin content of fibroblasts

The actin content of fibroblasts

Localization and organization of microfilaments and related proteins in normal and virus‐transformed cells

Cytochalasin B inhibits actin-related gelation of HeLa cell extracts.

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