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Adv Exp Med Biol. 2014;802:5-29. doi: 10.1007/978-94-007-7893-1_2.

Structure, physiology, and biochemistry of collagens.

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1
Departments of Molecular Pharmacology & Physiology and Orthopaedics & Sports Medicine, University of South Florida, Morsani College of Medicine, 12901 Bruce B. Downs Blvd., MDC8, Tampa, FL, 33612, USA.

Abstract

Tendons and ligaments are connective tissues that guide motion, share loads, and transmit forces in a manner that is unique to each as well as the anatomical site and biomechanical stresses to which they are subjected. Collagens are the major molecular components of both tendons and ligaments. The hierarchical structure of tendon and its functional properties are determined by the collagens present, as well as their supramolecular organization. There are 28 different types of collagen that assemble into a variety of supramolecular structures. The assembly of specific supramolecular structures is dependent on the interaction with other matrix molecules as well as the cellular elements. Multiple suprastructural assemblies are integrated to form the functional tendon/ligament. This chapter begins with a discussion of collagen molecules. This is followed by a definition of the supramolecular structures assembled by different collagen types. The general principles involved in the assembly of collagen-containing suprastructures are presented focusing on the regulation of tendon collagen fibrillogenesis. Finally, site-specific differences are discussed. While generalizations can be made, differences exist between different tendons as well as between tendons and ligaments. Compositional differences will impact structure that in turn will determine functional differences. Elucidation of the unique physiology and pathophysiology of different tendons and ligaments will require an appreciation of the role compositional differences have on collagen suprastructural assembly, tissue organization, and function.

PMID:
24443018
DOI:
10.1007/978-94-007-7893-1_2
[Indexed for MEDLINE]

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