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A Primer of Collagen Biology: Synthesis, Degradation, Subtypes, and Role in Dupuytren’s Disease

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Dupuytren’s Disease and Related Hyperproliferative Disorders

Abstract

Collagen is the primary structural protein of the extracellular matrix. To date, 28 distinct types of collagen have been identified which serve not only as structural components of the interstitial matrix but also function as adhesive and occlusive components of basement membranes, as anchoring fibrils between cells and the interstitium, and as integrative transmembrane proteins. In addition to their structural functions, collagens have a number of physiologically important roles as well. Collagens can serve as an extracellular “sink” for a number of growth factors and cytokines that are released in active form during the process of collagen degradation; additionally, the degradation products of collagen have a number of physiologic activities that are important to the process of wound healing.

Despite their broad structural and functional diversity, all collagens have some features in common. They are the only proteins which contain hydroxyproline and are also characterized by an unusually high content of the amino acids glycine and proline. Furthermore, all collagen subtypes contain within their structure at least one domain composed of a cross-linked triple-helical motif. The triple-helical structure renders collagen impervious to enzymatic degradation by most proteases as long as it is intact; only a few proteases (known as collagenases) have the ability to recognize and digest this triple-helical motif.

The extracellular matrix collagens are not static but are constantly being remodeled in response to the local environment. Collagen remodeling is tightly regulated in vivo, resulting in a balance between synthesis and degradation which allows the quantity and quality of the extracellular matrix to be adapted precisely to physiologic need. Disregulation of the balance between these two processes has been shown to have a role in the pathogenesis of a number of fibrotic conditions, notably in Dupuytren’s contracture.

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  1. Intrexon Corporation, Germantown, MD, USA

    Susan Emeigh Hart

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  1. Susan Emeigh Hart
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Correspondence to Susan Emeigh Hart .

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Editors and Affiliations

  1. The Hand Center, S Old Dixie Highway 1002, Jupiter, 33458, Florida, USA

    Charles Eaton

  2. Strahlenzentrum Hamburg, Langenhorner Chaussee 369, Hamburg, 22419, Germany

    M. Heinrich Seegenschmiedt

  3. Manchester Interdisciplinary Biocentre, Plastic & Reconstructive Surgery, University of Manchester, Princess Street 131, Manchester, M1 7DN, United Kingdom

    Ardeshir Bayat

  4. Faculty of Medicine, Dept. of Pathology and Immunology, University of Geneva, Rue Michel-Servet 1, Geneva, 1211, Switzerland

    Giulio Gabbiani

  5. Medical Center, Department of Plastic Surgery, University of Groningen, Hanzeplein 1, Groningen, 9713 GZ, Netherlands

    Paul Werker

  6. Dupuytren e.V., Westerbuchberg 60b, Übersee, 83236, Germany

    Wolfgang Wach

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Hart, S.E. (2012). A Primer of Collagen Biology: Synthesis, Degradation, Subtypes, and Role in Dupuytren’s Disease. In: Eaton, C., Seegenschmiedt, M., Bayat, A., Gabbiani, G., Werker, P., Wach, W. (eds) Dupuytren’s Disease and Related Hyperproliferative Disorders. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-22697-7_17

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