The Collagen Superfamily
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.
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