Collagen pp 35-84 | Cite as

The Collagen Superfamily

  • Sylvie Ricard-BlumEmail author
  • Florence Ruggiero
  • Michel van der Rest
Part of the Topics in Current Chemistry book series (TOPCURRCHEM, volume 247)


The collagen family is highly complex and shows a remarkable diversity in molecular and supramolecular organization, tissue distribution and function. Collagen types are classified in several sub-families according to sequence homologies and to similarities in their structural organization and supramolecular assembly. This overview covers advances made in this field during the last five years. Due to space limitation, the reader is referred to previous reviews for the topics not discussed hereafter. We focus on recently described fibrillar collagens (collagens XXIV and XXVII) and FACITs (collagens XVI, XIX, XX, XXI and XXII), multiplexins (collagens XV and XVIII), membrane-collagens (collagens XIII, XVII, XXIII and XXV) and collagen XXVI, on other proteins containing triple-helical domains including the members of the new Emu family and on the structure and functions of several non collagenous domains found in collagens. We also discuss data on collagen-related diseases with particular emphasis on gene therapy and on the involvement of collagens in neurodegenerative diseases, which emerge as a major threat for public health in aging populations.

Collagen Collagen-related diseases Extracellular domains 


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Authors and Affiliations

  • Sylvie Ricard-Blum
    • 1
    • 4
    Email author
  • Florence Ruggiero
    • 2
  • Michel van der Rest
    • 3
  1. 1.Institut de Biologie Structurale, CEA-CNRS UMR 5075Université Joseph FourierGrenoble Cedex 01France
  2. 2.Institut de Biologie et Chimie des protéines, CNRS UMR 5086IFR128 Biosciences GerlandLyon Cedex 07France
  3. 3.Ecole Nationale Supérieure de LyonLyon Cedex 07France
  4. 4.Institut de Biologie et Chimie des ProtéinesUMR 5086 CNRS-UCBLLyon Cedex 07France

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