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Literature Review

  • Nikos C. Apostolopoulos
Chapter

Abstract

In this chapter, stretching is defined with reference made to various stretching techniques. An understanding of how force (generated by stretching) affects soft and connective tissue is looked at both macroscopically (muscle, tendon, myotendon junction) and microscopically (sarcomere, myofibrillar proteins, ECM). By referring to these levels, an appreciation is gained of how the magnitude and rate of force generated during stretching affects the body as a whole. In order to elucidate this further, reference is made to inflammation and exercise, both non-damaging and damaging. With stretching considered as a load on tissue, a comprehensive overview is focused on damaging exercise, neutrophils, macrophages, and cytokines and their importance with regard to acute inflammation. The idea is proposed that stretching intensity be considered as a mechanotransduction mechanism. Mechanotransduction refers to the process by which the cells and tissues of the body respond to their environment, with the conversion of a mechanical energy into biochemical signals. Tensegrity is the main tenant of mechanotransduction, concerned with the essential maintenance of mechanical stability, which may be influenced by stretching intensity. Depending on the stretching intensity, this may or may not prompt an inflammatory response.

Keywords

Stretching Stretching magnitude Information Muscle Tendons Myotendon unit Sarcomere Sarcomeric proteins Intermediate filaments Cytokines ECM Calpains Neutrophils Macrophages Mechanotransduction Tensegrity 

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Further Readings

    A. Molecular Structure of Muscle

    1. Barczyk, M., Carracedo, S., & Gulberg, D. (2010). Integrins. Cell and Tissue Research, 339, 269–280.PubMedCrossRefGoogle Scholar
    2. Burkin, D. J., & Kaufman, S. J. (1999). The a7b1 integrin in muscle development and disease. Cell and Tissue Research, 296, 183–190.PubMedCrossRefGoogle Scholar
    3. Campbell, I. D., & Humphries, M. J. (2011). Integrin structure, activation, and interactions. Cold Spring Harbor Perspectives in Biology, 2011, 1–14.Google Scholar
    4. Clark, K. A., Mcelhinny, A. S., Beckerle, M. C., & Gregorio, C. C. (2002). Striated muscle cytoarchitecture: An intricate web of form and function. Annual Review of Cell and Developmental Biology, 18, 637–706.PubMedCrossRefGoogle Scholar
    5. Craig, R. W., & Padron, R. (2004). Molecular structure of the sarcomere. In A. C. Engel & C. Franzini-Armstrong (Eds.), Myology (3rd ed.). New York: McGraw-Hill.Google Scholar
    6. Geeves, M. A., & Holmes, K. C. (2005). The molecular mechanism of muscle contraction. Advances in Protein Chemistry, 71, 161–193.PubMedCrossRefGoogle Scholar
    7. Green, L. J., Mould, P., & Humphries, M. J. (1998). The integrin b subunit. The International Journal of Biochemistry & Cell Biology, 30, 179–184.CrossRefGoogle Scholar
    8. Holmberg, J., & Durbeej, M. (2013). Laminin-211 in skeletal muscle function. Cell Adhesion & Migration, 7, 111–121.CrossRefGoogle Scholar
    9. Kontrogianni-Konstantopoulos, A., Ackermann, M. A., Bowman, A. L., Yap, S. V., & Bloch, R. J. (2009). Muscle giants: Molecular scaffolds in sarcomeregenesis. Physiological Reviews, 89, 1217–1267.PubMedPubMedCentralCrossRefGoogle Scholar
    10. Mayer, U. (2003). Integrins: Redundant or important players in skeletal muscle. JBC, 278, 14587–14590.CrossRefGoogle Scholar
    11. Plow, E. F., Haas, T. A., Zhang, L., Loftus, J., & Smith, J. W. (2000). Ligand binding to integrins. JBC, 275, 21785–21788.CrossRefGoogle Scholar
    12. Squire, J. M., Al-Khayat, H. A., Knupp, C., & Luther, P. K. (2005). Molecular architecture in muscle contractile assemblies. Advances in Protein Chemistry, 71, 17–87.PubMedCrossRefGoogle Scholar

    B. Myotendon Unit

    1. Charvet, B., Ruggiero, F., & Le Guellec, D. (2012). The development of the myotendinous junction. A review. Muscles, Ligaments, and Tendons Journal, 2, 53–63.Google Scholar
    2. Ricard-Blum, S. (2011). The collagen family. Cold Spring Harbor Perspectives in Biology, 3, a004978.PubMedPubMedCentralCrossRefGoogle Scholar

    C. Mechanotransduction

    1. Humphrey, J. D., Dufresne, E. R., & Schwartz, M. A. (2014). Mechanotransduction and extracellular matrix homeostasis. Nature Reviews. Molecular Cell Biology, 15, 802–812.PubMedPubMedCentralCrossRefGoogle Scholar

    D. Rolling, Adhesion Transmigration

    1. Ley, K., Laudanna, C., Cybulsky, M. I., & Noursharhg, S. (2007). Getting to the site of inflammation: The leukocyte adhesion cascade update. Nature Reviews Immunology, 7, 678–689.PubMedCrossRefGoogle Scholar
    2. Muller, W. A. (2013). Getting leukocytes to the site of inflammation. Veterinary Pathology, 50, 7–22.PubMedPubMedCentralCrossRefGoogle Scholar
    3. Sundd, P., Pospieszalska, M. K., & Ley, K. (2013). Neutrophil rolling at high shear: Flattening, catch bond behavior, tethers and slings. Molecular Immunology, 55, 59–69.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Nature Switzerland AG 2018

Authors and Affiliations

  • Nikos C. Apostolopoulos
    • 1
  1. 1.University of TorontoTorontoCanada

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