The cell as a biomaterial

For materials scientists, the cell is evidently a biomaterial – rich with polymers, surface forces, solvent-solute interactions, liquid-crystalline structures, etc. Yet, the language of the materials scientist is as foreign to the biological world as French is to Chinese. Little of the materials scientists' perspective has been brought to bear on the question of biological function. This review aims to begin bridging the gap between the two disciplines–to show that a materials-oriented approach has power to bring fresh insights into an otherwise impenetrably complex maze. In this approach the cell is treated as a polymer gel. If the cell is a gel, then a logical approach to the understanding of cell function is through an understanding of gel function. Great strides have been made recently in understanding the principles of polymer-gel dynamics. It has become clear that a central mechanism is the phase-transition – a major structural change prompted by a subtle change of environment. Phase-transitions are capable of doing work and such work could be responsible for much of the work of the cell. Here, we pursue this approach. We set up a polymer-gel-based foundation for cell behavior, and explore the extent to which this foundation explains how the cell achieves its everyday tasks.

[1]  A. Oplatka Critical review of the swinging crossbridge theory and of the cardinal active role of water in muscle contraction. , 1997, Critical reviews in biochemistry and molecular biology.

[2]  Håkan Wennerström,et al.  Role of hydration and water structure in biological and colloidal interactions , 1996, Nature.

[3]  S. Carpenter,et al.  Vacuolation of Muscle Fibers Near Sarcolemmal Breaks Represents T-Tubule Dilatation Secondary to Enhanced Sodium Pump Activity , 1988, Journal of neuropathology and experimental neurology.

[4]  J. Pelta,et al.  Gel-sol transition can describe the proteolysis of extracellular matrix gels. , 2000, Biochimica et biophysica acta.

[5]  H. Huxley A personal view of muscle and motility mechanisms. , 1996, Annual review of physiology.

[6]  A. Frey-wyssling Submicroscopic Morphology of Protoplasm , 1953 .

[7]  H. Huxley,et al.  Changes in the Cross-Striations of Muscle during Contraction and Stretch and their Structural Interpretation , 1954, Nature.

[8]  H. Huxley,et al.  Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: myofilament lengths. , 1994, Biophysical journal.

[9]  D. Jones,et al.  Dynamic mechanical analysis of polymeric systems of pharmaceutical and biomedical significance. , 1999, International journal of pharmaceutics.

[10]  James A. Spudich,et al.  How molecular motors work , 1994, Nature.

[11]  R. M. Simmons,et al.  Elasticity and unfolding of single molecules of the giant muscle protein titin , 1997, Nature.

[12]  G. Pollack Phase transitions and the molecular mechanism of contraction. , 1996, Biophysical chemistry.

[13]  J. A. Gimm,et al.  Quantitative study of molecular transport due to electroporation: uptake of bovine serum albumin by erythrocyte ghosts. , 1994, Biophysical journal.

[14]  Forces Between Surfaces in Liquids , 1988, Science.

[15]  H. Chiao,et al.  Contraction-induced cell wounding and release of fibroblast growth factor in heart. , 1995, Circulation research.

[16]  E. Katayama Quick-freeze deep-etch electron microscopy of the actin-heavy meromyosin complex during the in vitro motility assay. , 1998, Journal of molecular biology.

[17]  P. Janmey,et al.  Actin filament networks. , 2001, Results and problems in cell differentiation.

[18]  T. Holstein,et al.  An ultrahigh-speed analysis of exocytosis: nematocyst discharge. , 1984, Science.

[19]  K Matsuno,et al.  Propagation of a signal coordinating force generation along an actin filament in actomyosin complexes. , 1998, Biophysical chemistry.

[20]  V. Parsegian,et al.  Intracellular osmotic action , 2000, Cellular and Molecular Life Sciences CMLS.

[21]  P. Janmey,et al.  Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. , 1996, Journal of molecular biology.

[22]  J. M. Fernández,et al.  Reversible condensation of mast cell secretory products in vitro. , 1991, Biophysical journal.

[23]  G. Bittner,et al.  Extent and mechanism of sealing in transected giant axons of squid and earthworms , 1994, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[24]  G H Pollack,et al.  The cross-bridge theory. , 1983, Physiological reviews.

[25]  Toshio Yanagida,et al.  A single myosin head moves along an actin filament with regular steps of 5.3 nanometres , 1999, Nature.

[26]  G H Pollack,et al.  Actin-filament motion in the in vitro motility assay has a periodic component. , 1997, Cell motility and the cytoskeleton.

[27]  J. Howard,et al.  Molecular motors: structural adaptations to cellular functions , 1997, Nature.

[28]  C. D. dos Remedios,et al.  Actin and the actomyosin interface: a review. , 1995, Biochimica et biophysica acta.

[29]  T. Kouyama,et al.  Domain motion in actin observed by fluorescence resonance energy transfer. , 1994, Biochemistry.

[30]  Yoshihito Osada,et al.  Stimuli-responsive polymer gels and their application to chemomechanical systems , 1993 .

[31]  E. Sackmann,et al.  Direct imaging of reptation for semiflexible actin filaments , 1994, Nature.

[32]  G H Pollack,et al.  Rescue of in vitro actin motility halted at high ionic strength by reduction of ATP to submicromolar levels. , 1996, Biochimica et biophysica acta.

[33]  M. Rief,et al.  Reversible unfolding of individual titin immunoglobulin domains by AFM. , 1997, Science.

[34]  G. Ling A revolution in the physiology of the living cell , 1992 .

[35]  S. Jarvis,et al.  Local Solvation Shell Measurement in Water Using a Carbon Nanotube Probe , 2000 .

[36]  Gerald H. Pollack,et al.  Cells, Gels and the Engines of Life: A New Unifying Approach to Cell Function , 2001 .

[37]  Toshio Yanagida,et al.  Direct observation of motion of single F-actin filaments in the presence of myosin , 1984, Nature.

[38]  R. Cooke,et al.  Actomyosin interaction in striated muscle. , 1997, Physiological reviews.

[39]  G. Ling,et al.  What retains water in living cells? , 1976, Science.

[40]  F. Oosawa,et al.  Polarized fluorescence from epsilon-ADP incorporated into F-actin in a myosin-free single fiber: conformation of F-actin and changes induced in it by heavy meromyosin. , 1978, Journal of molecular biology.

[41]  S M Block,et al.  Fifty Ways to Love Your Lever: Myosin Motors , 1996, Cell.

[42]  Malcolm Irving,et al.  Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle , 1995, Nature.

[43]  E. Vogler,et al.  Structure and reactivity of water at biomaterial surfaces. , 1998, Advances in colloid and interface science.

[44]  R. Pashley,et al.  Surface forces in adsorbed multilayers of water on quartz , 1979 .

[45]  J. Israelachvili,et al.  Direct measurement of structural forces between two surfaces in a nonpolar liquid , 1981 .

[46]  K Matsuno,et al.  Communicative interaction of myosins along an actin filament in the presence of ATP. , 1996, Biophysical chemistry.

[47]  L. Chernomordik,et al.  Electrically induced DNA uptake by cells is a fast process involving DNA electrophoresis. , 1991, Biophysical journal.

[48]  G. Pollack,et al.  Quantal length changes in single contracting sarcomeres , 1999, Journal of Muscle Research & Cell Motility.

[49]  A. Maniotis,et al.  Microsurgical removal of centrosomes blocks cell reproduction and centriole generation in BSC-1 cells , 1991, Cell.

[50]  A. Huxley,et al.  Structural Changes in Muscle During Contraction: Interference Microscopy of Living Muscle Fibres , 1954, Nature.

[51]  P. Verdugo,et al.  Molecular mechanism of product release in mucin secretion , 1988 .

[52]  G. Ling THE PHYSICAL STATE OF WATER IN LIVING CELL AND MODEL SYSTEMS * , 1965, Annals of the New York Academy of Sciences.