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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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Fibrillar Collagens.

Jordi Bella1, David J S Hulmes2

  • 1Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, M13 9PT, UK. jordi.bella@manchester.ac.uk.

Sub-Cellular Biochemistry
|January 20, 2017
PubMed
Summary

Fibrillar collagens provide structural frameworks for tissues and organs, influencing mechanical strength and cellular signaling. This review details their molecular structure, biosynthesis, and assembly into functional extracellular matrix networks.

Keywords:
AssemblyBiosynthesisCross-linkingExtracellular matrixInteractionsProteolysisStructure

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Fibrillar collagens (types I, II, III, V, XI, XXIV, XXVII) are crucial for tissue structure and mechanical integrity.
  • They form three-dimensional frameworks in tissues and organs, mediating mechanical strength and cellular signaling via interactions with receptors and the extracellular matrix (ECM).

Purpose of the Study:

  • To review the structure and assembly of fibrillar collagens and their procollagen precursors.
  • To elucidate the molecular and cellular mechanisms governing collagen biosynthesis and fibril formation.
  • To summarize current understanding of collagen fibril structure and interactions within the ECM.

Main Methods:

  • Review of literature on collagen structure, biosynthesis, and assembly.
  • Analysis of data from X-ray diffraction and electron microscopy for molecular packing insights.
  • Discussion of post-translational modifications and cellular control mechanisms.

Main Results:

  • The collagen triple-helix structure is influenced by amino acid sequence, hydrogen bonding, and post-translational modifications like prolyl 4-hydroxylation.
  • Biosynthesis involves multiple steps including prolyl 3-hydroxylation, chaperones, trimerization, and proteolytic maturation.
  • Fibril assembly is under cellular control, with specific molecular packing arrangements observed in different tissues.

Conclusions:

  • Fibrillar collagens are complex macromolecules whose structure and assembly are tightly regulated.
  • Understanding their molecular packing provides insights into interactions with cellular receptors, other ECM components, and enzymes.
  • This knowledge is vital for comprehending tissue mechanics and potential therapeutic interventions.