A quantitative description of the extension and retraction of surface protrusions in spreading 3T3 mouse fibroblasts.

Albrecht‐Buehler, Guenter; Lancaster, Robert M.

doi:10.1083/jcb.71.2.370

Cited by 54 publications

(30 citation statements)

References 26 publications

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“…Also a quantitative assay for the motility phenomena in spreading animal cells in culture, which are associated with large surface extensions, i.e., lamellipodia and filopodia (microspikes), has been described (Albrecht-Buehler and Lancaster 1976). Freshly suspended cells, plated on top of a gold particle-coated coverslip, produce various surface protrusions and remove the particles within a ring around each cell.…”

Section: Locomotion Assaymentioning

confidence: 99%

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Cytoskeleton changes and impaired motility of monocytes at modelled low gravity

et al. 2006

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Summary. Investigations performed in space have shown that gravity changes affect important cellular mechanisms like proliferation, differentiation, genetic expression, cytoskeletal architecture, and motility in lymphocytes, monocytes, and other mammalian cells. In particular, a dramatic depression of the mitogenic in vitro activation of human peripheral blood lymphocytes was observed at low gravity. The hypothesis of the present work is that a reduced interaction between T lymphocytes and monocytes, essential for the second signalling pathway, might be one of the reasons for the observed depression of the in vitro activation of human lymphocytes. Cell motility and with it a continuous rearrangement of the cytoskeletal network within the cell is essential for cell-tocell contacts. Whereas nonactivated lymphocytes in suspension are highly motile at low gravity, no data are available so far on the motility of adherent monocytes. It thus can be argued that impaired monocyte locomotion and cytoskeletal changes could be responsible for a reduced interaction of monocytes with T lymphocytes. In this study, the locomotion ability of J-111 cells, an adherent monocyte cell line, attached to colloidal gold particles on coverslips and exposed to modelled low gravity in the random positioning machine was found to be severely reduced compared with that of controls and the structures of actin, tubulin, and vinculin were affected.

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Section: Locomotion Assaymentioning

confidence: 99%

“…In approaching the problem of quantifying the motile behaviour of monocytes in modelled low gravity (or the phenomena of the motile actions of surface protrusions) we plated J-111 cells onto chamber slides coated with colloidal gold (Sigma) according to Albrecht-Buehler and Lancaster (1976).…”

Section: Locomotion Assaymentioning

confidence: 99%

Cytoskeleton changes and impaired motility of monocytes at modelled low gravity

et al. 2006

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“…Tissue culture dishes (Nunc Inc.) were coated with colloidal gold as described previously (3,4). Briefly, 9 ml of 14.5 mM AuCl4H and 30 ml of 36.5 mM Na2CO3 were added to 55 ml of H20, and the solution was heated in a glass beaker.…”

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confidence: 99%

Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility.

et al. 1993

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Evidence is accumulating that rho p21, a ras p21-related small GTP-binding protein (G protein), regulates the actomyosin system. The actomyosin system is known to be essential for cell motility. In the present study, we examined the action of rho p21, its inhibitory GDP/GTP exchange protein (named rho GDI), its stimulatory GDP/GTP exchange protein (named smg GDS), and Clostridium botulinum ADP-ribosyltransferase C3, known to selectively ADP-ribosylate rho p21 and to impair its function, in cell motility (chemokinesis) of Swiss 3T3 cells. We quantitated the capacity of cell motility by measuring cell tracks by phagokinesis. Microinjection of the GTP'yS-bound active form of rhoA p21 or smg GDS into Swiss 3T3 cells did not affect cell motility, but microinjection of rho GDI into the cells did inhibit cell motility. This rho GDI action was prevented by comicroinjection of rho GDI with the GTPyS-bound form of rhoA p21 but not with the same form of rhoA p21 lacking the C-terminal three amino acids which was not posttranslationally modified with lipids. The rho GDI action was not prevented by Ki-rasva l2 p21 or any of the GTP'yS-bound form of other small GTP-binding proteins including racl p21, G25K, and smg p21B. Among these small G proteins, rhoA p21, racl p21, and G25K are known to be substrates for rho GDI. The rho GDI action was not prevented by comicroinjection of rho GDI with smg GDS. Microinjection of C3 into Swiss 3T3 cells also inhibited cell motility. These results indicate that the rho GDI-rho p21 system regulates cell motility, presumably through the actomyosin system.Cell motility is essential for inflammatory reactions, tissue repair, and immune-system interactions in normal cells (for a review, see reference 48). Moreover, cell motility is essential for malignant cancer cells to infiltrate surrounding tissues and for smooth muscle cells in the media to migrate to the intima at the atherosclerotic lesion of vascular vessels (17; for a review, see reference 42). Evidence is accumulating that various kinds of cytoskeletal proteins and interacting proteins between cells and their substrates or neighboring cells regulate cell motility (48). Among these proteins, actomyosin is suggested to be one of the most important molecules in cell motility, on the basis of the observations that cell motility is sensitive to the actin-binding compounds cytochalasin D and phalloidin, which prevent polymerization and depolymerization of actin filaments, respectively (36, 46; for reviews, see references 13 and 28), and that an antibody against myosin affects cell motility (21). However, it is not clear how this actomyosin system is regulated to cause cell motility.Evidence is accumulating that small G proteins regulate various cell functions including cell growth, cell differentiation, gene expression, vesicle transport, cell morphological change, smooth muscle contraction, and superoxide generation in phagocytes (1, 20, 27; for reviews, see references 5, 6, 8, 18, and 51). Of the many small G proteins, the rho p21 family, c...

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“…F-actin, the filamentous polymer of globular G-actin, is involved in a variety of cellular functions, such as extension of microspikes from tissue culture cells (1), contraction ofthe contractile ring during cell division (2), and extension or retraction of pseudopods in amoeboid movement (3). Actin filaments also serve as mechanical support in structures; these include stress fibers in various cells (4), microvilli of intestinal brush border cells (5,6), and stereocilia of hair cells in the inner ear (7).…”

mentioning

confidence: 99%

Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles.

Miyata

Hotani

1992

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

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Spherical giant liposomes that had encapsulated skeletal-muscle G-actin were made by swelling a dried lipid mixture of dimyristoyl phosphatidyicholine/cardiolipin, 1:1 (wt/wt), in a solution of G-actin/CaCl2 at OC. Polymerization of the encapsulated G-actin into actin filaments was achieved by raising the temperature to 30C. We observed the subsequent shape changes of the liposomes by dark-field and differential interference-contrast light microscopy. After ;40 min, which was required for completion of actin polymerization, two shapes of liposome were evident: dumbbell and disk. Elongation of the dumbbell-shaped liposomes was concomitant with actin polymerization. Polarization microscopy showed that actin filaments formed thick bundles in the liposomes and that these filaments lay contiguous to the periphery of the liposome. Localization of actin filaments in the liposomes was confirmed by observation of rhodamine phalloidin-conjugated actin filaments by fluorescence microscopy. Both dumbbelland disk-shaped liposomes were rigid and kept their shapes as far as actin filaments were stabilized. In contrast, liposomes containing bovine serum albumin were fragile, and their shapes continually fluctuated from Brownian motion, indicating that the actin bundles served as mechanical support for the liposome shapes.

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A quantitative description of the extension and retraction of surface protrusions in spreading 3T3 mouse fibroblasts.

Cited by 54 publications

References 26 publications

Cytoskeleton changes and impaired motility of monocytes at modelled low gravity

Cytoskeleton changes and impaired motility of monocytes at modelled low gravity

Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility.

Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles.

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