Zusammenfassung
Motilität ist eine an nahezu alien Zellen beobachtbare Funktion. Der Begriff umfaßt sämtliche zellulären Bewegungsformen, angefangen bei der intrazellulären Zytoplasmaströmung, die durch Transport von Organellen an Aktinfilamenten oder an Mikrotubuli entsteht, über die Fortbewegung von Einzellern durch Formänderungen der ganzen Zelle (amöboide Bewegung) oder von Zellfortsätzen (Zilien und Flagellen) bis hin zur Fortbewegung vielzelliger Organismen mit Hilfe von Muskeln, die am Skelettsystem angreifen. Auch Volumen- und Formänderungen von Hohlorganen gehören dazu.
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Literatur
Weiterführende Lehr- und Handbücher
Bagshaw C (1993) Muscle contraction, 2nd edn. Chapman & Hall, London
Bloom W, Fawcett DW (1968) A textbook of histology, 11th edn. Saunders, Philadelphia
Carlson FD, Wilkie DR (1974) Muscle physiology. Prentice-Hall, Englewood Cliffs
Darnell J, Lodish H, Baltimore D (1990) Molecular cell biology. Scientific American Books, New York
Eckert R, Randall D, Augustine G (1993) Tierphysiologie. Thieme, Stuttgart
Grell KG (1973) Protozoology. Springer, Berlin
Huxley AF (1980) Reflections on muscle. Liverpool Univ Press, Liverpool
Jerusalem F, Zierz S (1991) Muskelerkrankungen. Thieme, Stuttgart
Rüegg JC (1992) Calcium in muscle contraction. Springer, Berlin
Squire JM (1981) The structural basis of muscular contraction. Plenum, New York
Einzel- und Übersichtsarbeiten
Baba SA, Hiramoto Y (1970) A quantitative analysis of ciliary movement by means of high speed microcinematography. J Exp Biol 52:645–690
Brenner B (1988) Effects of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci USA 85:3265–3269
Brenner B (1990) Muscle mechanics and biochemical kinetics. In: Squire JM (ed) Molecular mechanisms of muscular contraction. Macmillan, London, pp 77–149
Brenner B, Yu LC, Chalovich JM (1991) Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon: implications for the pathway to force generation. Proc Natl Acad Sci USA 88:5739–5743
Brenner B, Yu LC (1993) Structural changes in the actomyosin cross-bridges associated with force generation. Proc Natl Acad Sci USA 90:5252–5256
Cooke R (1986) The mechanism of muscle contraction. CRC Crit Rev Biochem 21:53–118
Finer JT, Simmons RM, Spudich JA (1994) Single myosin molecule mechanics: piconewton forces and nanometer steps. Nature 368:113–118
Gordon AM, Huxley AF, Julian FJ (1966) The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J Physiol (Lond) 184:170–192
Haselgrove JC (1973) X-ray evidence for the conformational changes in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harb Symp Quant Biol 37:341–352
Hirokawa N, Pfister KK, Yorifuji H, Wagner MC, Brady ST, Bloom GS (1989) Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56:867–878
Huxley AF, Niedergerke R (1954) Interference microscopy of living muscle fibres. Nature 173:971–973
Huxley AF, Simmons RM (1971) Proposed mechanism for force generation in striated muscle. Nature 233:533–538
Huxley HE (1969) The mechanism of muscular contraction. Science 164:1356–1366
Huxley HE (1973) Structural changes in the actin-and myosin-containing filaments during contraction. Cold Spring Harb Symp Quant Biol 37:361–376
Huxley HE, Hanson J (1954) Changes in the crossstriations of muscle during contraction and stretch and their structural interpretation. Nature 173:973–976
Jahn TL, Votta J J (1972) Locomotion of protozoa. Annu Rev Fluid Mech 4:93–116
Lymn RW, Taylor EW (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10:4617–4624
Melzer W, Herrmann-Frank A, Lüttgau HC (1995) The role of Ca2+ ions in excitation-contraction coupling of skeletal muscle fibres. Biochim Biophys Acta 1241:59–116
Metzger JM, Moss RL (1990) Calcium-sensitive crossbridge transmission in mammalian fast and slow muscle fibers. Science 247:1088–1090
Parry DAD, Squire JM (1973) Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles. J Mol Biol 75:33–55
Peachey LD (1965) The sarcoplasmic reticulum and transverse tubules of the frog’s sartorius. J Cell Biol 25:209–231
Pette D, Vrbová G (1992) Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev Physiol Biochem Pharmacol 120:115–202
Podolsky RJ, Teicholz LE (1970) The relation between calcium and contraction kinetics in skinned muscle fibres. J Physiol (Lond) 211:19–35
Pollard TD, Doberstein SK, Zot HG (1991) Myosin-1. Annu Rev Physiol 53:653–681
Pringle JWS (1967) The contractile mechanism of insect fibrillar muscle. Prog Biophys 17:1–60
Rayment I, Holden HM, Whittaker M, Yohn CB, Lorenz M, Holmes KC, Milligan RA (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58–65
Rayment I, Rypniewski WR, Schmidt-Blase K, Smith R, Tomchick DR, Benning MM, Winkelman DA, Wesenberg G, Holden HM (1993) Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261:50–58
Schröder RR, Manstein DJ, Jahn W, Holden H, Rayment I, Holmes KC, Spudich JA (1993) Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin SI. Nature 364:171–174
Shroer TA, Sheetz MP (1991) Functions of microtubule-based motors. Annu Rev Physiol 53:629–652
Smith CA, Rayment I (1996) X-ray structure of the Magnesium (II) · ADP · Vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35:5404–5417
Tamm SL, Horridge GA (1970) The relation between the orientation of the central fibrils and the direction of beat in cilia of Opalina. Proc R Soc Lond [Biol] 175:219–233
Tsien RY (1989) Fluorescent probes of cell signalling. Annu Rev Neurosci 12:227–253
Vallee RB, Wall JS, Paschal BM, Sheptner HS (1988) Microtubule-associated protein 1C from brain is a twoheaded cytosolic dynein. Nature 332:561–563
Wakabayashi K, Tokunaga M, Kohno I, Sugimoto Y, Hamanaka T, Takezawa Y, Wakabayashi T, Amemiya Y (1992) Small-angle synchrotron X-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP. Science 258:443–447
Warner FD, Satir P (1974) The structural basis of ciliary bend formation. J Cell Biol 63:35–63
Wessells NK (1971) How living cells change shape. Sci Am 225:76–82
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Rüdel, R., Brenner, B. (2001). Muskeln und Motilität. In: Dudel, J., Menzel, R., Schmidt, R.F. (eds) Neurowissenschaft. Springer-Lehrbuch. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56497-0_6
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DOI: https://doi.org/10.1007/978-3-642-56497-0_6
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