Photoinduced <i>in situ</i> formation of various F‐actin assemblies with a photoresponsive polycation

Misu, Manami; Furukawa, Hidemitsu; Kwon, Hyeokshin; Shikinaka, Kazuhiro; Kakugo, Akira; Satoh, Toshifumi; Osada, Yoshihito; Gong, Jian Ping

doi:10.1002/jbm.a.31990

Cited by 6 publications

(3 citation statements)

References 18 publications

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“…To date, many studies on the actin organization have been reported to elucidate the cellular mechanism. However, limited attempts have been made to investigate the effect of spatial distribution of binding proteins or polycations on the actin organization . As a future study, we will investigate the effect of spatial distribution of polycations on the morphological transformation of the actin-encapsulated liposome by applying local UV irradiation.…”

Section: Resultsmentioning

confidence: 99%

Morphogenesis of Liposomes Caused by Polycation-Induced Actin Assembly Formation

et al. 2008

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We investigated the effects of polycation-mediated actin assembly on the morphological transformation of the lipid vesicle membrane by spatiotemporally controlling actin assembly. By triggering the radical polymerization of the cationic monomer using UV irradiation, we achieved a varied photoinduced assembly of actin in bulk solution. Furthermore, we designed liposomes containing actin and cationic monomers. In these actin-encapsulated liposomes, various actin assemblies were formed by UV irradiation similar to that observed in bulk solution. Moreover, morphogenesis of actin-encapsulated liposomes was observed in liposomes encapsulated with G-actin but not with F-actin. This result indicates that a dynamic polymerization of G-actin is important for vesicle protrusion.

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Section: Resultsmentioning

confidence: 99%

Morphogenesis of Liposomes Caused by Polycation-Induced Actin Assembly Formation

et al. 2008

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“…This appears to be mediated through an inhibition of p47 phox translocation leading to a reduction in NADPH oxidase activity and to a diminution in neutrophil degranulation. Upon stimulation, neutrophils undergo a series of structural and functional rearrangements to enable the killing of ingested microbes, which is made possible by the conversion of G-actin to F-actin in order to facilitate the internal rearrangements (Misu et al, 2009). This work demonstrates that fumagillin may act by retarding the conversion of G to F actin and as a consequence this could hinder the other structural alterations associated with neutrophil activation.…”

Section: Utmentioning

confidence: 87%

Inhibition of neutrophil function following exposure to the Aspergillus fumigatus toxin fumagillin

Fallon

Reeves

Kavanagh

2010

Journal of Medical Microbiology

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The filamentous fungus Aspergillus fumigatus produces a variety of enzymes and toxins that may facilitate fungal colonization of tissue and evasion of the host immune response. One such toxin, fumagillin, was investigated for its ability to inhibit the action of neutrophils, which are a central component of the innate immune response to microbial infection. Neutrophils exposed to 2 mg fumagillin ml "1 for 25 min showed a significantly reduced ability to kill yeast cells (P,0.02), to phagocytose conidia of A. fumigatus (P,0.023) and to consume oxygen (P,0.032). The ability of neutrophils to generate superoxide is dependent upon the action of a functional NADPH oxidase complex which is composed of cytosolic (p40 phox , p47 phox , p67 phox , Rac2) and membrane (gp91 phox) proteins. Exposure of neutrophils to fumagillin inhibited the formation of the NADPH oxidase complex by blocking the translocation of p47 phox from the cytosolic to the membrane fraction (P50.02). In addition to the production of superoxide, neutrophils also undergo degranulation, which leads to the release of proteolytic enzymes that contribute to the microbicidal activity of the cell. Fumagillin-treated neutrophils showed reduced degranulation as evidenced by lower myeloperoxidase activity (P,0.019). Fumagillin-treated cells demonstrated reduced levels of F-actin, thus indicating that retarding the formation of F-actin may contribute to the inhibition of the structural rearrangements required in the activated neutrophil. This work indicates that fumagillin may contribute to reducing the local immune response by altering the activity of neutrophils and thus facilitate the continued persistence and growth of A. fumigatus in the host.

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“…A temporal control on the self‐assembly process of a motor protein system has been achieved through a novel in situ method, by combining a ‘top down’ and ‘bottom up’ approach. For this, a synthetic photoresponsive polycation has been developed, which provided a means for spatiotemporal control over polymer/actin complex formation 77. The photoresponsive polycation was mainly comprised of a water soluble cationic monomer and also contained a small amount of monomer of a triphenylmethane leucohydroxide derivative, a well known photochromic molecule that can be cationized in aqueous solution by UV irradiation, thereby causing an increase in the total charge on the photoresponsive polycation.…”

Section: Self‐organization and The Bottom‐up Approachmentioning

confidence: 99%

How to Integrate Biological Motors towards Bio‐Actuators Fueled by ATP

Kabir¹,

Kakugo²,

Gong³

et al. 2011

Macromolecular Bioscience

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Biological motors, driven by the conversion of chemical energy into mechanical energy, are much more efficient than man-made machines. The development of such efficient biomimetic motor systems in vitro is currently a vital need. However, great difficulty lies in how to integrate the sophisticated functions of the constituent components to obtain a performance as in the case of natural living systems. Based on 'active' and 'passive' self-organization principles, it has been demonstrated that the functions of motor protein systems can be integrated to obtain complex hierarchical structures that can work as actuators. Most of the works discussed here concern two-dimensional behavior, and recent works aim to explore the three-dimensional features of such artificial bio-mechanical systems.

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Photoinduced in situ formation of various F‐actin assemblies with a photoresponsive polycation

Cited by 6 publications

References 18 publications

Morphogenesis of Liposomes Caused by Polycation-Induced Actin Assembly Formation

Morphogenesis of Liposomes Caused by Polycation-Induced Actin Assembly Formation

Inhibition of neutrophil function following exposure to the Aspergillus fumigatus toxin fumagillin

How to Integrate Biological Motors towards Bio‐Actuators Fueled by ATP

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