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J Appl Physiol 81: 1522-1527, 1996;
8750-7587/96 $5.00
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Journal of Applied Physiology
Vol. 81, No. 4, pp. 1522-1527, October 1996
EXERCISE AND MUSCLE

Fractal analysis of cytoskeleton rearrangement in cardiac muscle during head-down tilt

Donald B. Thomason, Otis Anderson III, and Vandana Menon

Department of Physiology and Biophysics, University of Tennessee Health Science Center, Memphis, Tennessee 38163

Received 22 January 1996; accepted in final form 22 May 1996.

Thomason, Donald B., Otis Anderson III, and Vandana Menon. Fractal analysis of cytoskeleton rearrangement in cardiac muscle during head-down tilt. J. Appl. Physiol. 81(4): 1522-1527, 1996.---Head-down tilt by tail suspension of the rat produces a volume, but not pressure, load on the heart. One response of the heart is cytoskeleton rearrangement, a phenomenon commonly referred to as disruption. In these experiments, we used fractal analysis as a means to measure complexity of the microtubule structures at 8 and 18 h after imposition of head-down tilt. Microtubules in whole tissue cardiac myocytes were stained with fluorescein colchicine and were visualized by confocal microscopy. The fractal dimensions (D) of the structures were calculated by the dilation method, which involves successively dilating the outline perimeter of the microtubule structures and measuring the area enclosed. The head-down tilt resulted in a progressive decrease in D (decreased complexity) when measured at small dilations of the perimeter, but the maximum D (maximum complexity) of the microtubule structures did not change with treatment. Analysis of the fold change in complexity as a function of the dilation indicates an almost twofold decrease in microtubule complexity at small kernel dilations. This decrease in complexity is associated with a more Gaussian distribution of microtubule diameters, indicating a less structured microtubule cytoskeleton. We interpret these data as a microtubule rearrangement, rather than erosion, because total tubulin fluorescence was not different between groups. This conclusion is supported by F-actin fluorescence data indicating a dispersed structure without loss of actin.

microtubules; actin filaments; volume load; myocyte; colchicine; complexity


0161-7567/96 $5.00 Copyright © 1996 the American Physiological Society







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