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Functional Aspects of Proteoglycan Domain Structure

  • Mats Paulsson
  • Matthias Mörgelin
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 3)

Abstract

Proteoglycans, a class of extracellular macromolecules characteristically consisting of a protein core substituted with one or several glycosaminoglycan chains, have a profound influence on the physical properties of the extracellular matrix and the pericellular space. Many proteoglycans have a multidomain structure where distinct biological properties can be assigned to particular, often well conserved portions of the protein core. In the present chapter we review the functional aspects of proteoglycan domain structure using the large aggregating class of interstitial matrix proteoglycans as an example. These molecules are abundant in many types of extracellular matrix, but most pronouncedly so in cartilage. There they do by formation of large aggregates with hyaluronate fill the space between collagen fibers and make the tissue resilient to pressure (for review see Heinegård and Paulsson, 1984). Interstitial matrix does in addition contain two or more distinct populations of small proteoglycans. At least certain members of the class of small proteoglycans have affinity for collagen fibrils and are thought to regulate collagen fibril formation (Scott and Orford, 1981? Vogel et al, 1984).

Keywords

Chondroitin Sulphate Globular Domain Link Protein Chondroitin Sulphate Proteoglycan Cartilage Proteoglycan 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1989

Authors and Affiliations

  • Mats Paulsson
    • 1
  • Matthias Mörgelin
    • 1
  1. 1.Department of Biophysical ChemistryBiocenter of the University of BaselBaselSwitzerland

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