Identification of resilin in the leg of cockroach, Periplaneta americana: confirmation by a simple method using pH dependence of UV fluorescence

Neff, David; Frazier, S. F.; Quimby, Laura; Wang, Ruu-Tong; Zill, Sasha N.

doi:10.1016/s1467-8039(00)00014-1

Cited by 95 publications

(95 citation statements)

References 24 publications

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“…The binding of the antibody at sites in Drosophila where resilin-bearing structures have been previously reported in other insects such as pads at the wing bases (Andersen and Weis-Fogh, 1964;Neff et al, 2000) and the socket region of sensilla (Thurm, 1964;Chevalier, 1969) provides confirmatory evidence that CG15920 is a resilin-encoding gene of Drosophila. The antibody binds at sites in insects other than Drosophila where resilin-bearing structures have been reported.…”

Section: Anti-rec1 Resilin Binds To Resilin Across a Variety Of Insectssupporting

confidence: 68%

“…Two canonical sites of resilin-rich pads are the pleural arch of the flea ) and the tendon connecting dragonfly flight muscle to the thoracic hypodermis (Weis-Fogh, 1960). Both sites bind the anti-Rec1 antibody and both sites show the strong blue autofluorescence characteristic of resilin (Neff et al, 2000). No binding of the anti-Rec1 antibody to adjacent cuticles that do not show the strong auto-fluorescence was evident, indicating a correlation between the autofluorescence characteristic of resilin and antibody binding to those sites.…”

Section: Anti-rec1 Resilin Binds To Resilin Across a Variety Of Insectsmentioning

confidence: 98%

“…In fleas, click beetles, and froghoppers, resilin plays a role in storing energy via prolonged muscular action and releasing this energy very rapidly when needed (Sannasi, 1969;Burrows et al, 2008). Resilin-bearing cuticle also acts to counteract movement caused by muscles, such as in the opening mechanism of the spiracle in locusts (Miller, 1960), the sound-producing tymbals in cicadas (Young and Bennet-Clark, 1995), and the joints connecting segments in the legs of the cockroach, Periplaneta americana (Neff et al, 2000). The development of biomimetic resilin-like compounds (Elvin et al, 2005;Qin et al, 2009) and their possible applications (Kopecek, 2007) means that the methods by which insects utilise resilin will come under more intense scrutiny.…”

Section: Introductionmentioning

confidence: 99%

“…Methods include fluorescence emission under ultraviolet light, known as auto-fluorescence, pH dependence of the auto-fluorescence, and positive staining with toluidine blue and methylene blue. These techniques have been shown to be the most efficient ways to detect the presence of resilin in insects and crustaceans (Weis-Fogh, 1960;Neff et al, 2000) but doubt can remain, as it is rare for all methods to be applied. While Drosophila pro-resilin was the first insect resilin gene to be completely sequenced, to date there has been no direct confirmation that resilin is indeed expressed as a cuticular protein in Drosophila as inferred from the chitin-binding domain (R&R Consensus) (Andersen, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Expression of the rubber‐like protein, resilin, in developing and functional insect cuticle determined using a Drosophila anti‐rec 1 resilin antibody

Wong

Pearson

Elvin

et al. 2012

Developmental Dynamics

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Background: The natural elastomeric protein, insect resilin, is the most efficient elastic material known, used to store energy for jumping and flight in a variety of insects. Here, an antibody to recombinant Drosophila melanogaster pro-resilin is used to examine resilin expression in Drosophila and a wider range of insects. Results: Immunostaining of Drosophila embryos reveals anti-resilin reactivity in epidermal patches that exhibit a dynamic spatial and temporal expression through late embryogenesis. Resilin is also detected in stretch receptors in the embryo. In developing adult Drosophila, resilin pads are described at the base of wings and at the base of flexible sensory hairs in pupae. Resilin is also detected in embryos of the tephritid fruitfly, Bactrocera tryoni, and two well-known concentrations of insect resilin: the flight muscle tendon of the dragonfly and the pleural arch of the flea. Conclusions: The antiRec1 antibody antibody developed using Drosophila pro-resilin as antigen is cross-reactive and is useful for detection of resilin in diverse insects. For the first time, resilin expression has been detected during embryogenesis, revealing segmental patches of resilin in the developing epidermis of Drosophila. Developmental Dynamics 241:333-339,

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Section: Anti-rec1 Resilin Binds To Resilin Across a Variety Of Insectssupporting

confidence: 68%

Section: Anti-rec1 Resilin Binds To Resilin Across a Variety Of Insectsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Expression of the rubber‐like protein, resilin, in developing and functional insect cuticle determined using a Drosophila anti‐rec 1 resilin antibody

Wong

Pearson

Elvin

et al. 2012

Developmental Dynamics

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“…These wavelength bands correspond to the absorbance and emission peaks of resilin (Andersen and Weis-Fogh, 1964). An identifiable feature of the fluorescence of resilin is its sensitivity to pH (Andersen, 1963;Neff et al, 2001). Accordingly, the bathing saline was altered to pH2 with 2moll -1 hydrochloric acid, and pH12 with 2moll -1 sodium hydroxide.…”

Section: Methodsmentioning

confidence: 99%

A buckling region in locust hindlegs contains resilin and absorbs energy when jumping or kicking goes wrong

Bayley

Sutton

Burrows

2012

Journal of Experimental Biology

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SUMMARYIf a hindleg of a locust slips during jumping, or misses its target during kicking, energy generated by the two extensor tibiae muscles is no longer expended in raising the body or striking a target. How, then, is the energy in a jump (4100-4800J) or kick (1700J) dissipated? A specialised buckling region found in the proximal hind-tibia where the bending moment is high, but not present in the other legs, buckled and allowed the distal part of the tibia to extend. In jumps when a hindleg slipped, it bent by a mean of 23±14deg at a velocity of 13.4±9.5degms , we showed that one hindleg could store about 870J on bending, of which 210J was dissipated back to the leg on release. A band of blue fluorescence was revealed at the buckling region under UV illumination that had the two key signatures of the elastic protein resilin. A group of campaniform sensilla 300m proximal to the buckling region responded to imposed buckling movements. The features of the buckling region show that it can act as a shock absorber as proposed previously when jumping and kicking movements go wrong. Supplementary material available online at

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Chitin and Chitosan from Animal Sources

Peter

2002

Biopolymers Online

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Introduction Historical Outline Structure of Chitin and Chitosan Conformation in Solution Crystal Structures Occurrence Physiological Function Detection of Chitin in Animals and Analysis of Chitin and Chitosan Detection of Chitin in Biological Samples Determination of F A Mass Spectrometry of Chitin and Chitosan Oligosaccharides Macromolecular Characterization of Chitin and Chitosan Biosynthesis of Chitin in Animals Synthesis of Substrates for the Polymerizing Enzyme Enzymology of Chitin Synthase Genetic Basis of Chitin Synthesis Regulation of Chitin Synthesis Biodegradation Enzymology of Chitin Degradation Chitinase Genes Regulation of Degradation Production of Chitin and Chitosan Isolation of Chitin and Chitosan from Shellfish Waste Preparation of Low Molecular‐weight Chitin, Chitosan, and of Chitooligosaccharides Current World Market and Economics Companies Producing the Polymer Properties of Chitin and Chitosan Physico‐chemical Properties Materials Produced from Chitin or Chitosan Chemistry of Chitin and Chitosan Biological Properties Applications of Chitin and Chitosan Technical Applications Medicine and Healthcare Pharmaceutical Applications Cosmetics Agriculture Food Current Problems and Limits Outlook and Perspectives Relevant Patents for Isolation, Production and Applications of Chitin and Chitosan Acknowledgements

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Identification of resilin in the leg of cockroach, Periplaneta americana: confirmation by a simple method using pH dependence of UV fluorescence

Cited by 95 publications

References 24 publications

Expression of the rubber‐like protein, resilin, in developing and functional insect cuticle determined using a Drosophila anti‐rec 1 resilin antibody

Expression of the rubber‐like protein, resilin, in developing and functional insect cuticle determined using a Drosophila anti‐rec 1 resilin antibody

A buckling region in locust hindlegs contains resilin and absorbs energy when jumping or kicking goes wrong

Chitin and Chitosan from Animal Sources

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