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First published online January 25, 2005
Journal of Experimental Biology 208, 549-560 (2005)
Published by The Company of Biologists 2005
doi: 10.1242/jeb.01425

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Flight muscle properties and aerodynamic performance of Drosophila expressing a flightin transgene

Byron Barton¹, Gretchen Ayer¹, Nicole Heymann³, David W. Maughan², Fritz-Olaf Lehmann³ and Jim O. Vigoreaux^1,2,*

¹ Department of Biology, University of Vermont, Burlington, VT 05405, USA
² Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA
³ Biofuture Research Group, Department of Neurobiology, University of Ulm, Albert-Einstein-Allee 11, 89081 Ulm, Germany

View larger version (4K): [in a new window]   Fig. 1. The Act88F-fln transgene used in this study. The Actin88F promoter is pale grey, flightin exons are the dark grey boxes, and introns and the 3'UTR are represented as empty boxes. Bar, 100 bp.

View larger version (120K): [in a new window]   Fig. 2. Electron microscopy of flight muscle from fln0, wild-type and transgenic flies. All pictures are from 2–5-day-old adult IFM. (A,B), fln0; (C,D), wild-type; (E,F), P{fln+}0.2; (G,H), P{fln+}2.2; (I and J), P{fln+}0.2. A, C, E, G, I are longitudinal sections; B, D, F, H, and J are cross sections. Note that the highly disrupted sarcomere structure in fln0 (in A,B) is no longer evident in the rescued line. However, there are fewer thick filaments per myofibril cross-sectional area. G and H, flies expressing four copies of fln+ have normal IFM. I and J, are examples of occasional defects seen in P{fln+}0.2 flies. Bar, 0.5 µm.

View larger version (13K): [in a new window]   Fig. 3. Western blot of flightin levels throughout pupal stages of development. (A) P{fln+}0.2 (B) wild type. Pupa were staged by visual inspection using standard criteria (Bainbridge and Bownes, 1981). Accumulation of flightin in wild type begins at stage P8 (Vigoreaux et al., 1993), approx 2–8 h after accumulation in P{fln+}0.2-rescued flies.

View larger version (22K): [in a new window]   Fig. 4. Western blot analysis of 2DE reveal normal temporal phosphorylation of flightin in transgenic line. (A,C,E) wild type; (B,D,F) P{fln+}0.2. A and B, P15 pupa; C and D, <1 h post-eclosion; E and F, 2–4-day-old adult. For all blots, the basic end is to the left. 2D gel analysis was followed by immunoblot analysis using anti-flightin polyclonal antibody. N1 and N2 are the non-phosphorylated isoelectic variants while P1 through P9 are phosphorylated variants (see Vigoreaux and Perry, 1994). For each of the developmental stages, P{fln+}0.2 transgenic flies have a nearly identical phosphorylation pattern when compared to the wild type.

View larger version (35K): [in a new window]   Fig. 5. Quantification of flightin in normal and transgenic IFM. (A) Western blot of 12% SDS-PAGE probed with an anti-flightin specific antibody. Lane 1, fln0; lane 2, molecular weight marker; lane 3, wild type; lane 4, P{fln+}2.2; lane 5, P{fln+}0.2; lane 6, w; P{w+Mhc+}wm2. (B) Relative intensity of the flightin bands in A. (*P<0.05 vs wt, N=3). Each lane was loaded with 0.15 µg of protein.

View larger version (39K): [in a new window]   Fig. 6. Mechanical parameters of maximally Ca2+ (pCa 5.0) activated IFM fibers. (A) Elastic moduli as a function of frequency, (B) viscous moduli as a function of frequency, and (C) is power produced as a function of frequency. Values are mean ± S.E.M. for wild type, P{fln+}0.2 and P{fln+}2.2. There is no significant difference among the three Drosophila lines for any of the parameters.

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