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Collagen in Human Tissues: Structure, Function, and Biomedical Implications from a Tissue Engineering Perspective

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Polymer Composites – Polyolefin Fractionation – Polymeric Peptidomimetics – Collagens

Part of the book series: Advances in Polymer Science ((POLYMER,volume 251))

Abstract

The extracellular matrix is a complex biological structure encoded with various proteins, among which the collagen family is the most significant and abundant of all, contributing 30–35% of the whole-body protein. “Collagen” is a generic term for proteins that forms a triple-helical structure with three polypeptide chains, and around 29 types of collagen have been identified up to now. Although most of the members of the collagen family form such supramolecular structures, extensive diversity exists between each type of collagen. The diversity is not only based on the molecular assembly and supramolecular structures of collagen types but is also observed within its tissue distribution, function, and pathology. Collagens possess complex hierarchical structures and are present in various forms such as collagen fibrils (1.5–3.5 nm wide), collagen fibers (50–70 nm wide), and collagen bundles (150–250 nm wide), with distinct properties characteristic of each tissue providing elasticity to skin, softness of the cartilage, stiffness of the bone and tendon, transparency of the cornea, opaqueness of the sclera, etc. There exists an exclusive relation between the structural features of collagen in human tissues (such as the collagen composition, collagen fibril length and diameter, collagen distribution, and collagen fiber orientation) and its tissue-specific mechanical properties. In bone, a transverse collagen fiber orientation prevails in regions of higher compressive stress whereas longitudinally oriented collagen fibers correlate to higher tensile stress. The immense versatility of collagen compels a thorough understanding of the collagen types and this review discusses the major types of collagen found in different human tissues, highlighting their tissue-specific uniqueness based on their structure and mechanical function. The changes in collagen during a specific tissue damage or injury are discussed further, focusing on the many tissue engineering applications for which collagen scaffolds are currently being applied.

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Acknowledgments

This research was supported by the Singapore National Research Foundation under CREATE programme: The Regenerative Medicine Initiative in Cardiac Restoration Therapy (NRF-Technion WBS No. R-398-001-065-592), and the Nanoscience and Nanotechnology Initiative, Faculty of Engineering, National University of Singapore, Singapore.

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Authors and Affiliations

  1. Department of Mechanical Engineering, National University of Singapore, 9 Engineering Drive 1, Singapore, 117576, Singapore

    Preethi Balasubramanian & Seeram Ramakrishna

  2. E3-05-14, Center for Nanofibers and Nanotechnology, Nanoscience and Nanotechnology Initiative, National University of Singapore, 2 Engineering Drive 3, Singapore, 117576, Singapore

    Molamma P. Prabhakaran, Merum Sireesha & Seeram Ramakrishna

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  1. Preethi Balasubramanian
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  2. Molamma P. Prabhakaran
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  3. Merum Sireesha
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  4. Seeram Ramakrishna
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Correspondence to Molamma P. Prabhakaran .

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  1. Hiyoshi-Honcho 6-27-12, Yokohama, 223-0062, Japan

    Akihiro Abe

  2. Ch. des Colombaires 10 A, Cully, 1096, Switzerland

    Hans-Henning Kausch

  3. DWI, Textile and Macromol. Chemistry, RWTH Aachen, Pauwelsstr. 8, Aachen, 52056, Germany

    Martin Möller

  4. Dept.of Chemistry, Univ. of Stellenbosch, Private Bag X1, Matieland, 7602, South Africa

    Harald Pasch

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Balasubramanian, P., Prabhakaran, M.P., Sireesha, M., Ramakrishna, S. (2012). Collagen in Human Tissues: Structure, Function, and Biomedical Implications from a Tissue Engineering Perspective. In: Abe, A., Kausch, HH., Möller, M., Pasch, H. (eds) Polymer Composites – Polyolefin Fractionation – Polymeric Peptidomimetics – Collagens. Advances in Polymer Science, vol 251. Springer, Berlin, Heidelberg. https://doi.org/10.1007/12_2012_176

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