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REVIEW ARTICLES

Continuum thermomechanics and the clinical treatment of disease and injury

[+] Author and Article Information
JD Humphrey

Department of Biomedical Engineering, Texas A&M University, College Station, TX 77843-3120; jhumphrey@tamu.edu

Appl. Mech. Rev 56(2), 231-260 (Mar 04, 2003) (30 pages) doi:10.1115/1.1536177 History: Online March 04, 2003
Copyright © 2003 by ASME
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Figures

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Schema of a typical mammalian cell. In particular, note that a cell can be regarded both as a composite structure, consisting of a membrane and cytoplasm, and as having a composite cytoskeleton consisting of three primary types of structural proteins plus hundreds of accessory proteins. Because each protein can exhibit different biothermomechanical responses, detailed analyses of thermal damage and death are clearly complex (from Humphrey 4, with permission).
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Schema of the structure of fibrillar collagen, from the triple helix motif of the molecule, to the quarter-staggered arrangement that constitutes a fibril, to the level of the fiber. Note, too, that not only does the degree of undulation, orientation and cross-linking change from tissue-to-tissue, different tissues have different amounts and types of proteoglycans, which can thermally stabilize the collagen further. From 4, with permission.
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Light micrographs of skin: control (top) and thermally damaged (bottom). Note the heating-induced loss of order. Courtesy of Dr Sharon Thomsen, University of Texas at Austin.
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Force-time data from Kampmeier et al. 65 who performed HIT tests on excised corneal strips. Note that the original data have been re-scaled: force by the maximum value attained during the test and time via the characteristic time τm at which the force reached its maximum value. Note that the data that reveal an initial increasing force due to heating tend toward a master curve whereas those during the subsequent phase of a decreasing force do not; the former was thought to relate to the thermal damage process and the latter to a stress relaxation of the damaged material.
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Isothermal shrinkage data from Chen et al. (111; with permission) for a 1D isothermal isotonic shrinkage test on chordae tendineae subjected to two different isotonic loads (500 and 650 kPa). Symbols represent testing at the following temperatures: 75°C (crosses), 80°C (pluses), 85°C (astericks), and 90°C (circle-dots). Note that increasing temperature hastens the process whereas increasing stress during heating delays it.
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Data from 17 different (isothermal-isotonic) thermomechanical tests (T from 65 to 90°C and Piola-Kirchhoff stress P from 0 to 650 kPa) on chordae tendineae. Scaling each data set with its temperature and load dependent characteristic time τ2 collapsed all data to a single master curve. (From Chen et al. 111, with permission.)
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Shrinkage data from Weir 91, where l is the current length and l the length after maximum shrinkage, wherein the original data have been scaled by temperature- and load-dependent characteristic times τ1 (similar to Fig. 7).
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Shrinkage data from Wall et al. 109 again showing data scaled with temperature-dependent characteristic times τ1.
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Stress-strain data at 37°C before and after various degrees of prior thermal damage (revealed by the % equilibrium shrinkage ξe). (From Chen and Humphrey 129, with permission.)
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Time-dependent partial recovery (ie, reversal of shrinkage or partial renaturation) of chordae tendineae upon restoration of a 37°C bath following thermal damage. Symbols are the same as in Fig. 6. (From Chen et al. 111, with permission.)

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